Affinage

CD151

CD151 antigen · UniProt P48509

Length
253 aa
Mass
28.3 kDa
Annotated
2026-06-09
100 papers in source corpus 47 papers cited in narrative 47 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CD151 (PETA-3) is a tetraspanin scaffold protein that organizes laminin-binding integrins into lateral membrane complexes to control cell adhesion, migration, morphogenesis, and angiogenesis (PMID:7632941, PMID:9566977, PMID:10036233). It forms direct, detergent-resistant complexes specifically with integrins α3β1 and α6β1 (and comparably α7β1), while other tetraspanins associate with these integrins only indirectly through CD151 (PMID:10229664, PMID:11884516). The interaction is extracellular and stoichiometric: CD151 contacts the α3 subunit (aa 570-705) through its large extracellular loop, and a defined QRD(194-196) site is required for strong association with both α3β1 and α6β1, with complex assembly occurring early in biosynthesis (PMID:10734060, PMID:11479292, PMID:12356873). CD151 is palmitoylated on intracellular cysteines (C11/C15/C242/C243) by the DHHC2 palmitoyl transferase, which stabilizes the protein, protects it from lysosomal degradation, and promotes its associations with other tetraspanins (CD9, CD63) without disrupting the core CD151-α3β1 interaction (PMID:11907260, PMID:18508921). Through these complexes CD151 strengthens integrin adhesion to laminin under force, governs integrin diffusion mode and clustering, drives α3β1 glycosylation, and controls integrin endocytic trafficking via a C-terminal YRSL/YXXφ motif required for both integrin internalization and CD151-promoted migration (PMID:12805567, PMID:17716972, PMID:18852263, PMID:22328509). Downstream it signals through FAK, Src, Rho-family GTPases (Rac1/Cdc42/RhoA), and PI3K/Akt/eNOS to control collective migration, junction stability, MMP activation, and endothelial angiogenesis (PMID:14557253, PMID:16798740, PMID:19509057, PMID:17045834, PMID:21832275). CD151 also collaborates with growth-factor receptors—assembling Met-β4 integrin signaling complexes and modulating ErbB2 dimerization through RhoA—linking it to tumor progression and anti-receptor drug resistance (PMID:20937830, PMID:23792450, PMID:20197472). In vivo, podocyte-specific and global Cd151 deletion cause integrin-α3β1-dependent glomerular nephropathy, and host CD151 is required for efficient endothelial support of tumor metastasis (PMID:22201679, PMID:21536858). CD151 additionally functions as a host entry factor for HPV16 and HCMV and, independently of integrins, promotes resistance to anti-cancer drugs via an intracellular pool (PMID:23302890, PMID:27147745, PMID:30778617).

Mechanistic history

Synthesis pass · year-by-year structured walk · 23 steps
  1. 1995 Medium

    Established CD151 as a distinct four-transmembrane tetraspanin/TM4SF protein, defining the molecular entity before any function was known.

    Evidence cDNA cloning, sequence analysis, and Northern blot of PETA-3

    PMID:7632941

    Open questions at the time
    • No binding partners or cellular function identified
    • Topology inferred from sequence, not directly demonstrated
  2. 1998 High

    First linked CD151 to integrin biology and migration by showing it complexes with α3β1 and other tetraspanins at endothelial junctions and that antibody blockade impairs migration and invasion.

    Evidence Co-IP, immunofluorescence, time-lapse microscopy and collagen invasion in endothelial cells

    PMID:9566977

    Open questions at the time
    • Whether the integrin association is direct vs. indirect unresolved
    • Binding site on either protein unmapped
  3. 1999 High

    Defined the specificity and directness of CD151-integrin coupling, showing CD151 forms direct complexes specifically with α3β1 and α6β1 and serves as the linker through which other tetraspanins reach integrins; concurrently established CD151 as a pro-migratory, pro-metastatic factor.

    Evidence Reciprocal Co-IP across detergent conditions, epitope-blocking, overexpression and antibody inhibition in tumor and haematopoietic cells with in vivo metastasis

    PMID:10036233 PMID:10229664 PMID:10447000 PMID:9931299

    Open questions at the time
    • Molecular determinants of the direct interaction not yet mapped
    • Downstream signaling effectors unknown
  4. 2000 High

    Mapped the CD151-integrin interface to extracellular regions (α3 aa 570-705 and CD151 LEL aa 186-217) and confirmed the four-pass topology, establishing the structural basis of complex formation.

    Evidence Membrane-impermeable cross-linking, chimeric constructs and topology determination

    PMID:10734060

    Open questions at the time
    • Functional consequence of these specific residues not yet tested
    • Stoichiometry of the complex undefined
  5. 2001 High

    Defined the LEL residues (incl. CCG/PXXCC motifs and aa 195-205) needed for stable α3β1 association and showed the complex assembles early in biosynthesis, separating CD151-integrin coupling from CD151-tetraspanin homotypic interactions.

    Evidence Site-directed mutagenesis, chimeras, multi-detergent Co-IP and pulse-chase

    PMID:11479292

    Open questions at the time
    • Did not resolve the minimal QRD determinant identified later
    • Effect on downstream function not directly assayed
  6. 2002 High

    Established that palmitoylation at four cysteines, the QRD(194-196) site, and the C-terminal tail are separable functional modules: palmitoylation governs tetraspanin web assembly and stability, QRD governs strong integrin binding, and the C-terminal tail is required for morphogenesis.

    Evidence Palmitoylation-site and QRD mutagenesis, [3H]-palmitate labeling, C-terminal deletion, Matrigel morphogenesis and Co-IP; α7β1 association confirmed

    PMID:11809818 PMID:11884516 PMID:11907260 PMID:12356873

    Open questions at the time
    • Enzyme writing palmitoylation not yet identified
    • Mechanism linking C-terminal tail to morphogenesis unresolved
  7. 2002 High

    Placed CD151 pro-migratory activity downstream of FAK, demonstrating genetic dependence on FAK for CD151-enhanced motility and invasion.

    Evidence CD151 transfection into FAK(+/+) vs FAK(-/-) fibroblasts with invasion/motility and metastasis assays

    PMID:11774285

    Open questions at the time
    • Other downstream effectors (Src, Rho GTPases) not yet placed
    • How CD151 activates FAK mechanistically unresolved
  8. 2003 High

    Demonstrated CD151's biophysical role in integrin adhesion strengthening and its participation in epithelial cell-cell adhesion complexes via PKC/Cdc42 and a PTPμ/E-cadherin module.

    Evidence Magnetic-bead force assays with C-terminal mutants; Co-IP of E-cadherin junctional complex and Cdc42/Rac pulldowns with PKC inhibition

    PMID:12805567 PMID:14557253 PMID:14691142

    Open questions at the time
    • Direct vs indirect nature of multiprotein junctional complex not fully resolved
    • Mechanism connecting CD151 to PTPμ expression unclear
  9. 2005 Medium

    Extended CD151 function to pericellular proteolysis and growth-factor receptor signaling, identifying proMMP-7 as an extracellular-loop binding partner and CD151-c-Met-integrin complexes as drivers of HGF responses.

    Evidence Yeast two-hybrid and Co-IP domain mapping with in situ zymography; Co-IP and knockdown/overexpression with HGF stimulation

    PMID:16139245 PMID:16200075

    Open questions at the time
    • Stoichiometry of CD151-c-Met complex undefined
    • Whether c-Met contact is direct unresolved
  10. 2006 Medium

    Resolved the CD151 homophilic-engagement signaling cascade, linking integrin activation to FAK/Src/p38/JNK/c-Jun and AP-1-driven MMP-9 transcription.

    Evidence Stable transfection, siRNA, pathway inhibitors and MMP-9 AP-1 reporter assays

    PMID:16798740

    Open questions at the time
    • Direct kinase substrate relationships not established
    • Single-lab pathway dissection
  11. 2007 High

    Identified the C-terminal YRSL/YXXφ motif as the endocytic determinant coupling CD151-mediated integrin internalization to cell motility.

    Evidence Motif mutagenesis with internalization and migration assays across multiple integrins

    PMID:17716972

    Open questions at the time
    • Adaptor proteins reading the YXXφ motif not identified
    • Trafficking route/destination of internalized integrin undefined
  12. 2008 High

    Identified DHHC2 as the palmitoyl transferase writing CD151 palmitoylation, and showed CD151 controls α3β1 N-glycosylation and α6β4-dependent tumor signaling, deepening the post-translational and signaling regulation of the complex.

    Evidence DHHC knockdown panel with catalytic mutants; glycosylation analysis with N159Q and integrin-binding mutants; RNAi ablation with FAK/Rac1/Lck and EGFR readouts and xenografts

    PMID:18451146 PMID:18492066 PMID:18508921 PMID:18852263

    Open questions at the time
    • Mechanism by which CD151 shapes α3 glycan processing unclear
    • Whether DHHC2 acts on the integrin-bound pool specifically untested
  13. 2006 Medium

    Connected endothelial CD151 to angiogenesis through PI3K/Akt/eNOS-driven nitric oxide production.

    Evidence rAAV overexpression, signaling phosphorylation, NO measurement, and tube formation with PI3K/eNOS inhibitors in HUVEC

    PMID:17045834

    Open questions at the time
    • Receptor/integrin upstream of PI3K activation not defined here
    • Single gain-of-function model
  14. 2009 High

    Established CD151 as a regulator of RhoA at epithelial junctions and of collective migration, mechanistically tying junctional stability to the CD151-α3β1 axis.

    Evidence siRNA, collective migration, RhoA G-LISA, live imaging and rescue with WT vs integrin-binding mutant CD151; plus c-Met/α3α6 branching morphogenesis

    PMID:19159612 PMID:19509057

    Open questions at the time
    • How CD151 restrains RhoA biochemically unresolved
    • GEF/GAP intermediaries unidentified
  15. 2010 High

    Cemented CD151's role in tumor invasion and therapy resistance through Met-β4 complexes, PI3K/Akt/GSK-3β/Snail-driven MMP9, and the laminin-integrin-CD151-FAK axis conferring anti-ErbB2 drug resistance.

    Evidence RNAi/overexpression with Co-IP of Met-β4, pathway Westerns, anchorage-independent growth, xenografts and trastuzumab/lapatinib sensitivity assays

    PMID:20197472 PMID:20578262 PMID:20937830

    Open questions at the time
    • Selective MAPK-vs-AKT branching downstream of Met-β4 mechanism unresolved
    • Direct molecular link between CD151 and ErbB2 unclear
  16. 2011 High

    Provided in vivo genetic proof of CD151 function: podocyte adhesion to the glomerular basement membrane, endothelial vascular stability via RhoA/Rac1 balance, and host support of metastasis through endothelial VEGF/Src/Akt signaling.

    Evidence Conditional and global Cd151-null mice, adhesion-strength assays, Rho/Rac activity, permeability, ACE-inhibitor and experimental metastasis models

    PMID:21536858 PMID:21832275 PMID:22201679

    Open questions at the time
    • Cell-autonomous vs systemic contributions to metastasis not fully separated
    • Modifier effect of blood pressure mechanistically incomplete
  17. 2012 High

    Defined CD151 control of integrin lateral diffusion and clustering and its role in skin carcinoma initiation via STAT3 and PKCα-β4 association, refining how CD151 organizes integrins at the nanoscale and in tumor initiation.

    Evidence Single-particle tracking with talin/actin perturbations; two-stage carcinogenesis in Cd151-null mice with STAT3/β4-phosphorylation and drug sensitization; ErbB2/RhoA dimerization assays

    PMID:22328509 PMID:22824799 PMID:23792450

    Open questions at the time
    • Link between diffusion-mode control and downstream signaling not directly established
    • How CD151 promotes β4 S1424 phosphorylation unresolved
  18. 2013 High

    Broadened CD151 roles to pathogen entry (HPV16 endocytosis), distinct tetraspanin-complex division of labor in α3β1 function, and selective control of TGFβ1-induced p38 signaling and scattering.

    Evidence siRNA with CD151 domain mutants and live co-tracking for HPV16; comparative CD9/CD81 vs CD151 knockdown; shRNA with TGFβR compartmentalization and pathway-selective phosphorylation plus in vivo metastasis

    PMID:20570898 PMID:23302890 PMID:23613949

    Open questions at the time
    • Whether HPV16 contacts CD151 directly unresolved
    • Mechanism of selective p38 (not Smad/AKT/ERK) activation unclear
  19. 2014 Medium

    Implicated CD151 in immune-cell function, showing it organizes integrins at the T-cell immunological synapse to support activation signaling.

    Evidence siRNA silencing with synapse imaging, IL-2/CD69 readouts, integrin relocalization and FAK/ERK phosphorylation

    PMID:24723389

    Open questions at the time
    • Direct integrin partner at the synapse not mapped
    • Single-lab knockdown study
  20. 2016 Medium

    Identified CD151 as a proviral host factor for HCMV entry acting at the penetration step.

    Evidence RNAi screen hit validated with differentially labeled fluorescent virus penetration vs adsorption assays

    PMID:27147745

    Open questions at the time
    • Receptor/co-factor partners for HCMV penetration undefined
    • Whether integrin or tetraspanin-web involvement is required not tested
  21. 2019 High

    Resolved an integrin-independent CD151 function in drug resistance and identified CD151 in a hybrid keratinocyte adhesion structure, separating CD151 roles that require integrin binding from those that do not.

    Evidence CRISPR/siRNA ablation with apoptosis assays, QRD-mutant reconstitution and integrin-KO comparison; CD151-KO keratinocytes with compositional analysis of adhesion structures; miR-199a-3p targeting CD151 in cardiomyocytes

    PMID:30778617 PMID:31186138 PMID:31488507

    Open questions at the time
    • Molecular effector of integrin-independent drug protection unidentified
    • Intracellular CD151 binding partners mediating survival unknown
  22. 2020 Medium

    Extended CD151 to the tumor microenvironment, showing it drives midkine-dependent macrophage/monocyte recruitment including via extracellular vesicles.

    Evidence Monocyte migration with purified midkine, anti-midkine blocking of EV chemoattraction and xenograft immunohistology

    PMID:32129471

    Open questions at the time
    • Mechanism linking CD151 to midkine production unresolved
    • Role of α6β1 in this axis incompletely defined
  23. 2022 Medium

    Defined a JAM-A/α3β1/CD151/CD9 complex driving collective epithelial migration on laminin and collagen-I via cryptic lamellipodia.

    Evidence Co-IP with domain mapping, multi-component siRNA depletion and substrate-specific collective migration assays

    PMID:35067832

    Open questions at the time
    • Direct vs indirect JAM-A-CD151 contact not resolved
    • Single-lab study

Open questions

Synthesis pass · forward-looking unresolved questions
  • How CD151's separable molecular modules (palmitoylation, QRD integrin binding, YXXφ trafficking, intracellular pool) are coordinated to switch between integrin-dependent adhesion/migration roles and integrin-independent survival/viral-entry functions remains unresolved.
  • No structural model of the assembled CD151-integrin complex
  • Intracellular effectors of integrin-independent CD151 functions unidentified
  • Adaptors reading the YXXφ motif unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0098772 molecular function regulator activity 4 GO:0001618 virus receptor activity 2
Localization
GO:0005886 plasma membrane 3 GO:0005764 lysosome 2 GO:0005768 endosome 2
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1266738 Developmental Biology 3 R-HSA-1474244 Extracellular matrix organization 3 R-HSA-1643685 Disease 3
Partners
CD9DHHC2ITGA3ITGA6ITGB1ITGB4JAM-AMET
Complex memberships
CD151-α3β1 integrin complexJAM-A/α3β1/CD151/CD9 complexMet-β4 integrin signaling complextetraspanin-enriched microdomain (with CD9/CD81)

Evidence

Reading pass · 47 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 CD151 (PETA-3) was cloned and identified as a 253 amino acid protein with four transmembrane domains, a large extracellular loop with a single N-linked glycosylation site, and structural homology to the tetraspanin/TM4SF family. Northern blot confirmed broad tissue expression. cDNA cloning, Northern blot, sequence analysis Blood Medium 7632941
1998 CD151/PETA-3 localizes to endothelial cell-cell lateral junctions and forms molecular complexes with α3β1 integrin and other tetraspanins (CD9, CD81). Anti-CD151 antibodies inhibited endothelial cell migration in wound healing and invasion into collagen gels, and increased adhesion to ECM proteins. Immunofluorescence microscopy, biochemical co-immunoprecipitation, time-lapse video microscopy, collagen gel invasion assay The Journal of cell biology High 9566977
1999 CD151 associates with multiple integrin chains (β1, β3, β4, α2, α3, α5, α6) including α6β4 integrin, and is present both on the plasma membrane at cell-cell contacts and in intracellular endosomal/lysosomal compartments (co-localizing with transferrin receptor and CD63). Anti-PETA-3 antibodies inhibited endothelial cell migration and modulated in vitro angiogenesis but had no effect on neutrophil transendothelial migration. Co-immunoprecipitation, immunofluorescence confocal microscopy, immuno-electron microscopy, functional antibody inhibition assays Journal of cell science High 10036233
1999 Among tetraspanins, CD151 forms digitonin-resistant (direct) complexes specifically with integrins α3β1 and α6β1, whereas other tetraspanins associate with integrins only indirectly through CD151. An anti-CD151 antibody (TS151r) epitope maps to the integrin-binding region and its binding is blocked by α3β1 or α6β1 overexpression. Reciprocal co-immunoprecipitation in multiple detergent conditions (digitonin, Brij 97, CHAPS), antibody epitope-blocking experiments, cell surface binding quantification The Biochemical journal High 10229664
1999 CD151 (PETA-3) overexpression in HeLa cells enhanced cell migration, and anti-CD151 antibodies inhibited HEp-3 cell chemotaxis and in vivo metastasis without affecting cell adhesion or tumor growth, identifying CD151 as a positive effector of tumor cell migration and metastasis. Eukaryotic expression cloning, transfection/overexpression, chemotaxis assay, in vivo metastasis model, antibody inhibition Cancer research High 10447000
1999 CD151 associates with integrins α4β1, α5β1, α6β1, and αIIbβ3 in haematopoietic cell lines. Anti-CD151 F(ab')2 fragments induced homotypic cell adhesion dependent on energy and cytoskeletal integrity but not mediated through integrin-ligand binding. CD151 ligation did not alter integrin avidity for fibronectin, laminin, collagen, or fibrinogen. Co-immunoprecipitation, homotypic adhesion assay with F(ab')2 fragments, function-blocking antibodies, integrin ligand adhesion assays The Biochemical journal Medium 9931299
2000 CD151 directly contacts α3β1 integrin extracellularly. Using membrane-impermeable cross-linking and chimeric proteins, the association was mapped to an extracellular α3 site (aa 570-705) and a region within the large extracellular loop of CD151 (aa 186-217). Both N- and C-terminal domains of CD151 are intracellular, confirming the four-pass topology. Membrane-impermeable chemical cross-linking, chimeric integrin/tetraspanin constructs, epitope mapping, topology determination The Journal of biological chemistry High 10734060
2001 The large extracellular loop (LEL) of CD151 (aa 149-213) is required for stable (Triton X-100-resistant) association with α3β1 integrin, and 11 aa substitution (195-205) or mutations in conserved CCG and PXXCC motifs abolish this interaction. The CCG motif mutation selectively prevents homotypic CD151-CD151 interaction without affecting association with other tetraspanins. CD151-α3β1 complex assembly occurs early in biosynthesis, before CD151-tetraspanin associations. Site-directed mutagenesis, CD151/CD9 chimeras, co-immunoprecipitation in Triton X-100 and Brij 96, biosynthetic pulse-chase The Journal of biological chemistry High 11479292
2002 CD151 is palmitoylated at intracellular N-terminal and C-terminal cysteine residues (C11, C15, C242, C243). Simultaneous mutation of these cysteines (tetra mutant) eliminates >90% of palmitoylation, markedly diminishes associations with other tetraspanins (CD9, CD63), increases diffuse distribution, reduces stability during biosynthesis, but does not disrupt CD151-α3β1 integrin association or localization into detergent-resistant microdomains. Site-directed mutagenesis of palmitoylation sites, [3H]-palmitate labeling, co-immunoprecipitation, immunofluorescence, biosynthesis/stability assays Molecular biology of the cell High 11907260
2002 CD151 associates with α7β1 integrin comparably to α3β1. Most tissues expressing laminin-binding integrins show CD151-integrin complexes, but the association is subject to cell-type-specific regulation as shown by differential TS151r epitope accessibility in vivo. Co-immunoprecipitation, immunohistochemistry with epitope-blocking antibodies, K562 cell surface expression studies Journal of cell science Medium 11884516
2002 An extracellular QRD(194-196) site in CD151 is required for strong (Triton X-100-resistant) association with both α3β1 and α6β1 integrins, and this association occurs early in biosynthesis with α subunit precursors. QRD→INF mutation disrupts CD151-integrin association and impairs α3/α6 integrin-dependent cellular cable formation on Matrigel and cell spreading. Site-directed mutagenesis (QRD→INF), co-immunoprecipitation in Triton X-100 and Brij 96, biosynthetic pulse-chase, cell morphology assays on Matrigel The Journal of cell biology High 12356873
2002 CD151-α6β1 complex acts as a functional unit for cellular morphogenesis on Matrigel. Deletion or exchange of the short 8 amino acid C-terminal tail of CD151 causes a dominant negative effect that suppresses α6β1-dependent cell network formation and spreading on laminin-1, without disrupting α6β1 association or adhesion to Matrigel. C-terminal deletion/exchange mutagenesis, cell network formation assay on Matrigel, cell adhesion assay, co-immunoprecipitation Molecular biology of the cell High 11809818
2002 CD151 enhances cell motility and invasion in a FAK-dependent manner. CD151 overexpression in FAK(+/+) fibroblasts increased invasion and motility (inhibitable by anti-CD151 mAb), while CD151 overexpression in FAK(-/-) fibroblasts produced no enhancement and was unaffected by anti-CD151 mAb, demonstrating that FAK is required for CD151-mediated pro-migratory effects. Transfection of CD151 into FAK(+/+) and FAK(-/-) fibroblasts, Matrigel invasion assay, cell motility assay, antibody inhibition International journal of cancer High 11774285
2003 CD151 is required for α6β1 integrin adhesion strengthening to laminin-1. Cells expressing a C-terminal region-mutant CD151 showed impaired adhesion strengthening under defined applied forces (0-1.5 nN), without affecting static adhesion to laminin-1 or detachment of fibronectin/anti-α6-coated beads. Magnetic bead force application (0-1.5 nN), bead detachment assay, site-directed mutagenesis of CD151 C-terminal region, NIH 3T3 transfection system Proceedings of the National Academy of Sciences of the United States of America High 12805567
2003 CD151 in complex with α3β1 integrin functions as a component of a cell-cell adhesion complex in epithelial cells, stimulating E-cadherin-mediated adhesion by regulating PTPμ expression and organizing a multimolecular complex containing PKCβII, RACK1, PTPμ, β-catenin, and E-cadherin. Co-immunoprecipitation, gene expression analysis, PTPμ reporter assays, epistasis using α3 integrin-deficient cells The Journal of cell biology Medium 14691142
2003 CD151 overexpression in A431 epithelial cells accelerates intercellular adhesion via PKC- and Cdc42-dependent actin cytoskeletal reorganization. CD151 engagement induced Cdc42-dependent filopodial extension and enhanced E-cadherin puncta formation and its anchorage to the cytoskeletal matrix; calphostin C (PKC inhibitor) blocked these effects. Overexpression, anti-CD151 mAb perturbation, Cdc42/Rac GTP-pull-down, pharmacological inhibition (calphostin C), immunofluorescence The Journal of cell biology Medium 14557253
2005 CD151 interacts with proMMP-7 (promatrilysin-1) through the propeptide of proMMP-7 and the C-terminal extracellular loop of CD151, as mapped by yeast two-hybrid and co-immunoprecipitation. This CD151-proMMP-7 interaction promotes pericellular activation of proMMP-7 on the cell surface, as demonstrated by in situ zymography blocked by anti-CD151 antibody. Yeast two-hybrid screen, co-immunoprecipitation, 125I-labeled proMMP-7 binding assay, confocal colocalization, in situ zymography with antibody inhibition Laboratory investigation High 16200075
2005 CD151 forms a structural and functional complex with c-Met/HGF receptor and integrin α3/α6. Knockdown of CD151 or integrin α3/α6 almost completely abrogated HGF-stimulated cell growth and migration in salivary gland cancer cells; forced CD151 expression enhanced HGF-dependent effects. Co-immunoprecipitation, siRNA knockdown, gain-of-function transfection, cell growth and migration assays with HGF stimulation Biochemical and biophysical research communications Medium 16139245
2006 CD151-mediated homophilic interactions between cells activate integrin-dependent signaling through FAK, Src, p38 MAPK, JNK, and c-Jun, leading to AP-1-dependent transcription of MMP-9 and enhanced cell motility. Inhibitors/siRNAs against FAK, Src, p38 MAPK, and JNK abrogated these CD151-induced effects; integrin α3β1/α6β1 activation was a prerequisite. Stable transfection, siRNA knockdown, pharmacological inhibition, MMP-9 promoter AP-1 reporter assay, co-immunoprecipitation The Journal of biological chemistry Medium 16798740
2006 CD151 silencing in epidermal carcinoma cells impairs motility on laminin-5, causes persistent adhesive contacts, disrupts α3β1 association with tetraspanin-enriched microdomains, reduces α3β1 bulk detergent extractability, and impairs α3β1 internalization during migration. Both α3β1- and α6β4-dependent adhesion to laminin-5 were also impaired. CD151 re-expression reversed these defects. Retroviral RNAi, cell motility/adhesion assays on laminin-5, detergent solubility fractionation, integrin internalization assay, rescue experiment Molecular biology of the cell High 16571677
2007 CD151 contains a YRSL (YXXφ) endocytosis/sorting motif in its C-terminal cytoplasmic domain. Mutation of this motif markedly attenuates CD151 internalization, completely abrogates CD151-promoted cell migration on laminin, and diminishes internalization of associated integrins (α3β1, α5β1, α6β1), demonstrating that CD151-mediated integrin trafficking is critical for promoting cell motility. YXXφ motif mutagenesis, internalization assays, cell migration assays on ECM substrates, co-localization studies The Journal of biological chemistry High 17716972
2008 DHHC2, a DHHC-domain palmitoyl transferase, is the primary enzyme responsible for palmitoylation of tetraspanins CD151 and CD9. DHHC2 associates with CD151 and CD9 but not other cell-surface proteins; DHHC2 knockdown diminishes CD151/CD9 palmitoylation. Catalytically inactive DHHC2 (DH→AA or C→S mutations) fails to promote palmitoylation. DHHC2-dependent palmitoylation promotes CD9-CD151 associations, protects CD151 and CD9 from lysosomal degradation, and shifts cells toward increased cell-cell contacts. DHHC enzyme knockdown panel, [3H]-palmitate labeling, co-immunoprecipitation, catalytic mutant DHHC2, stability assays, cell morphology analysis Molecular biology of the cell High 18508921
2008 CD151 regulates N-glycosylation of α3β1 integrin specifically (not other associated proteins). CD151 knockdown reduces Fucα1-2Gal and bisecting GlcNAc modifications on α3 integrin N-glycans. Direct CD151-integrin contact is required but not sufficient; CD151 glycosylation at Asn159 in the LEL is also essential. Changes in α3β1 glycosylation correlate with impaired cell migration toward laminin-332. siRNA knockdown, glycan analysis, CD151 glycosylation mutant (N159Q), co-immunoprecipitation, migration assay, rescue with WT vs. mutant CD151 The Journal of biological chemistry High 18852263
2008 CD151 ablation in basal-like mammary tumor cells redistributes α6β4 integrin subcellularly, severs molecular links between integrins and tetraspanin-enriched microdomains, reduces cell migration/invasion/spreading, and diminishes signaling through FAK, Rac1, and Lck while disrupting EGFR-α6 integrin collaboration. CD151 ablation delays tumor progression in xenograft models. RNAi ablation, integrin localization imaging, FAK/Rac1/Lck phosphorylation assays, EGFR co-immunoprecipitation, xenograft tumor models Cancer research High 18451146
2008 CD151 regulates integrin α3β1 cell morphology and intracellular signaling on laminin-511. CD151 knockdown in A549 cells causes aberrant membrane protrusions and reduces tyrosine phosphorylation of FAK, Src, p130Cas, and paxillin, independent of the reduction in adhesive activity, suggesting CD151 controls both integrin adhesion strength and integrin-stimulated signaling through distinct mechanisms. RNAi knockdown, cell morphology analysis, phosphorylation assays (FAK, Src, p130Cas, paxillin), integrin-activating antibody rescue The FEBS journal Medium 18492066
2009 CD151 loss destabilizes E-cadherin-dependent carcinoma cell-cell junctions and enhances collective tumor cell sheet migration. This occurs through excessive RhoA activation, loss of actin organization at junctions, and increased basal stress fibers. A CD151 mutant with impaired α3β1 association fails to restore junctional stability, linking the CD151-α3β1 axis to RhoA regulation at junctions. siRNA silencing, collective migration assay, RhoA activity pulldown (G-LISA), actin staining, live-cell junction remodeling imaging, CD151 mutant rescue Journal of cell science High 19509057
2009 CD151 forms a structural and functional complex with c-Met and integrin α3/α6 in breast cancer cells. Knockdown of CD151, integrin α3, or integrin α6 abolished HGF-induced branching morphogenesis and reduced Akt phosphorylation, placing CD151 in the HGF/c-Met/integrin signaling axis. Co-immunoprecipitation, siRNA knockdown, HGF-stimulated morphogenesis assay, Akt phosphorylation measurement Biochemical and biophysical research communications Medium 19159612
2009 CD151 on endothelial cells promotes angiogenesis via the PI3K/Akt pathway, activating Akt and eNOS leading to increased nitric oxide production. CD151 overexpression increased HUVEC proliferation, migration, and tube formation; PI3K inhibitor (LY294002) and eNOS inhibitor (L-NAME) attenuated these effects. rAAV-mediated overexpression, PI3K/Akt/eNOS phosphorylation assays, NO measurement, proliferation/migration/tube formation assays, pharmacological inhibition The international journal of biochemistry & cell biology Medium 17045834
2010 CD151 promotes MMP9 expression in HCC cells through the PI3K/Akt/GSK-3β/Snail signaling pathway. CD151 overexpression increased MMP9, and CD151 knockdown reduced MMP9 expression and impaired microvessel formation in vitro. siRNA knockdown, overexpression, PI3K/Akt/GSK-3β/Snail signaling pathway analysis by Western blot, MMP9 expression assay, in vitro microvessel formation assay Hepatology Medium 20578262
2010 CD151 is required for Met-dependent cancer cell growth and survival. CD151 depletion impairs HGF-driven proliferation, anchorage-independent growth, and protection from anoikis. Mechanistically, CD151 is required for formation of Met-β4 integrin signaling complexes; CD151 depletion blocks HGF-induced β4 integrin phosphorylation, Grb2-Gab1 association, and MAPK (but not AKT) activation. RNAi silencing, co-immunoprecipitation of Met-β4 integrin complex, phosphorylation assays (β4, MAPK, AKT), anchorage-independent growth assay, xenograft model The Journal of biological chemistry High 20937830
2010 CD151 knockdown, combined with trastuzumab, inhibits ErbB2 activation and downstream signaling through Akt, Erk1/2, and FAK in ErbB2+ breast cancer cells adherent to laminin-5, sensitizing them to trastuzumab and lapatinib. The laminin-integrin-CD151-FAK axis provides resistance to anti-ErbB2 agents. siRNA knockdown, drug sensitivity assays, ErbB2/Akt/Erk1/2/FAK phosphorylation Western blot, 3D laminin-5 adhesion assay Cancer research Medium 20197472
2011 CD151 in podocytes is required for integrin α3β1-mediated adhesion strength to laminin in the glomerular basement membrane. Podocyte-specific Cd151 deletion leads to glomerular nephropathy, and blood pressure is a critical modifier—global Cd151-null mice on FVB background develop renal disease, with ACE inhibition prolonging survival. Conditional and global knockout mice, cell adhesion strength assays, histology, ACE inhibitor treatment, blood pressure manipulation The Journal of clinical investigation High 22201679
2011 CD151 maintains vascular stability by promoting endothelial cell-cell and cell-matrix adhesions through confining cytoskeletal tension: CD151 loss elevates RhoA signaling (increasing actin cytoskeletal traction) and diminishes Rac1 activity (reducing cortical actin meshwork). RhoA inhibition or cAMP activation stabilizes CD151-silenced endothelial structures. siRNA silencing, Cd151 knockout endothelial cells, Rho/Rac activity assays, permeability assays, pharmacological RhoA inhibition, endothelial tube formation assay Blood High 21832275
2011 Host animal CD151 is required for efficient tumor metastasis. CD151-null mice show markedly diminished experimental lung metastasis after Lewis lung carcinoma or B16F10 injection. CD151-null mouse lung endothelial cells show diminished support for tumor cell adhesion, transendothelial migration, and permeability induction. VEGF-induced Src and Akt signaling was diminished in CD151-null endothelial cells. CD151-null mice, experimental metastasis models (i.v. injection), isolated null endothelial cells, transendothelial migration assay, permeability assay, VEGF signaling assays Blood High 21536858
2012 CD151 knockdown in MDA-MB-231 mammary cells impairs α6 integrin clustering without decreasing α6 expression or activation. CD151 knockdown shifts α6 integrin diffusion from predominantly random-confined diffusion (RCD) to directed motion (DMO), a dysregulating effect sensitive to actin disruption but desensitized to talin knockdown and phorbol ester stimulation. CD151 effects on diffusion mode are specific to α6 (not αv) integrins. Single particle tracking (SPT), siRNA knockdown, mode-of-diffusion analysis, phorbol ester and EGF stimulation, talin knockdown, actin disruption Journal of cell science High 22328509
2012 CD151 promotes skin squamous cell carcinoma (SCC) initiation and progression by supporting STAT3 activation and PKCα-α6β4 integrin association. CD151 supports PKC-dependent β4 S1424 phosphorylation and regulates α6β4 subcellular distribution to promote an invasive state. CD151 ablation sensitizes mouse skin to carcinogens and drugs targeting EGFR, PKC, Jak2/Tyk2, and STAT3. Two-stage chemical carcinogenesis in Cd151 knockout mice, STAT3 activation assay, PKCα-β4 co-immunoprecipitation, β4 phosphorylation Western blot, pharmacological sensitization Oncogene High 22824799
2012 The α3β1-CD151 complex regulates ErbB2 dimerization and phosphorylation through RhoA. Depletion of either α3β1 or CD151 reduces ErbB2 phosphorylation, reduces ErbB2 dimerization, and increases RhoA activity. RhoA directly controls ErbB2 dimerization. Combined expression of α3β1 and CD151 enhances Herceptin efficacy. siRNA knockdown, ErbB2 dimerization assay, ErbB2 phosphorylation Western blot, RhoA activity (G-LISA), Herceptin treatment in 3D culture, Rho manipulation Oncogene Medium 23792450
2013 CD151 mediates HPV16 endocytosis. Surface-bound HPV16 co-moves with CD151 in the plane of the membrane before cointernalization. CD151 depletion reduces HPV16 endocytosis (not binding). The C-terminal cytoplasmic region (but not tyrosine-based sorting motif) and palmitoylation of CD151 are required; CD151-associated integrins α3β1 and α6β1/4 are also involved; CD151 QRD integrin-binding site mutants do not restore virus internalization. CD151 depletion (siRNA), live-cell co-tracking, internalization assay, CD151 domain mutants (C-terminal deletion, YRSL, palmitoylation, QRD), integrin siRNA knockdown Journal of virology High 23302890
2013 CD151 depletion in CD151-silenced carcinoma cells disrupts α3β1 integrin association with tetraspanin-enriched microdomains and impairs α3β1 internalization. CD9/CD81 complex but not CD151 is required for α3β1 association with PKCα and directed α3β1-dependent motility; CD151 is required for early spreading events. These two tetraspanin complexes have overlapping but distinct roles in α3β1 function. RNAi silencing of CD9/CD81 vs. CD151, co-immunoprecipitation with PKCα, directed motility assay, spreading assay, cell morphology analysis, PKC inhibitor PloS one Medium 23613949
2013 CD151 depletion specifically attenuates TGFβ1-induced scattering and proliferation of breast cancer cells in 3D Matrigel, requiring its association with α3β1 or α6 integrins but independent of tetraspanin-enriched microdomain recruitment. CD151 regulates compartmentalization of TGFβ type I receptor (ALK-5) and specifically controls TGFβ1-induced p38 activation (not Smad2/3, c-Akt, or Erk1/2). shRNA knockdown, 3D Matrigel scattering assay, TGFβ receptor localization, p38/Smad2/3/Akt/Erk1/2 phosphorylation assays, CD151 mutant rescue, experimental lung metastasis Cancer research High 20570898
2014 CD151 and CD9 congregate at the T-cell side of the immunological synapse. Silencing CD151 or CD9 blunts IL-2 secretion and CD69 expression by APC-conjugated T cells, diminishes α4β1 relocalization to the IS, reduces high-affinity β1 integrin accumulation at the contact, and decreases FAK and ERK1/2 phosphorylation, without affecting CD3 or actin accumulation at the IS. siRNA silencing, immunological synapse imaging, IL-2 ELISA, CD69 flow cytometry, integrin relocalization and activation assays, FAK/ERK phosphorylation European journal of immunology Medium 24723389
2016 CD151 is a proviral host factor for HCMV entry, supporting viral penetration (but not adsorption) into endothelial cells and fibroblasts. CD151 depletion impairs infection by virus strains with broad or narrow cell tropism equally, as shown by fluorescent virus with differentially labeled capsid and envelope proteins. Targeted RNAi screen (96 genes), CD151 depletion (siRNA), HCMV infection assay, fluorescent virus penetration vs. adsorption assay Journal of virology Medium 27147745
2019 CD151, through binding to integrin α3β1, stabilizes a hybrid adhesion structure (with features of both hemidesmosomes and tetraspanin-enriched microdomains) containing CD151-α3β1/α6β4 integrin complexes and plectin but not keratin filaments, in the central region of keratinocytes. Classic hemidesmosomes (α6β4/plectin/BP180/BP230/keratin) do not require CD151. CD151 knockout keratinocytes, α3β1-CD151 co-immunoprecipitation, immunofluorescence of adhesion structure components, spreading/adhesion kinetics assay Journal of cell science Medium 31488507
2019 CD151 supports anti-cancer drug resistance independent of integrins. CD151 ablation sensitizes tumor cells to gefitinib and camptothecin (increasing apoptosis). Drug sensitization occurs even when integrins are unengaged; integrin α3/α6 ablation does not mimic CD151 ablation; the CD151-QRD mutant (diminished integrin association) reconstitutes drug protection as effectively as WT CD151. Anti-cancer drug treatment selectively upregulates intracellular non-integrin-associated CD151. CD151 ablation (CRISPR/siRNA), apoptosis assays (cleaved caspase-3, cleaved PARP, annexin V, PI), CD151-QRD mutant reconstitution, integrin α3/α6 ablation comparison, intracellular vs. surface CD151 fractionation Cellular and molecular life sciences High 30778617
2019 CD151 in cardiomyocytes suppresses proliferation by inducing p38 expression. miR-199a-3p directly targets CD151 mRNA, suppresses CD151, and promotes cardiomyocyte proliferation. Cd151 gain-of-function reduced cardiomyocyte proliferation; Cd151 loss-of-function increased it. Pharmacological p38 inhibition rescued the Cd151 inhibitory effect on proliferation. Luciferase reporter assay (miR-199a-3p/CD151 3'UTR), Cd151 gain- and loss-of-function in cardiomyocytes, p38 inhibitor rescue, proliferation assays Biochemical and biophysical research communications Medium 31186138
2020 CD151 in inflammatory breast cancer cells promotes macrophage recruitment through a midkine-dependent mechanism. CD151 increases midkine production; purified midkine stimulates monocyte migration specifically. CD151-expressing IBC-derived extracellular vesicles have chemoattractive potential for monocytes, blocked by anti-midkine antibodies. This pathway also involves integrin α6β1. In vitro monocyte migration assay, midkine purification and functional assay, anti-midkine antibody blocking of EV chemoattraction, xenograft immunohistology, chemokine profiling The Journal of pathology Medium 32129471
2022 JAM-A forms a complex with α3β1 integrin and tetraspanins CD151 and CD9 through its extracellular domain. This complex regulates collective cell migration of polarized epithelial cells on laminin and collagen-I (not fibronectin/vitronectin). Depletion of JAM-A, α3β1 integrin, or CD151/CD9 impairs cryptic lamellipodia dynamics and slows collective migration. Co-immunoprecipitation, domain mapping experiments, siRNA depletion of JAM-A/α3β1/CD151/CD9, collective migration assay, substrate-specificity experiments Cellular and molecular life sciences Medium 35067832

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1998 Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with alpha3 beta1 integrin localized at endothelial lateral junctions. The Journal of cell biology 227 9566977
2002 Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology. Molecular biology of the cell 202 11907260
1999 Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. The Biochemical journal 185 10229664
1997 Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 175 9111230
2000 Direct extracellular contact between integrin alpha(3)beta(1) and TM4SF protein CD151. The Journal of biological chemistry 161 10734060
2018 LncRNA SNHG3 induces EMT and sorafenib resistance by modulating the miR-128/CD151 pathway in hepatocellular carcinoma. Journal of cellular physiology 158 30132868
2015 The tetraspanins CD151 and Tspan8 are essential exosome components for the crosstalk between cancer initiating cells and their surrounding. Oncotarget 147 25544774
2008 CD151 accelerates breast cancer by regulating alpha 6 integrin function, signaling, and molecular organization. Cancer research 147 18451146
1999 PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function. Journal of cell science 147 10036233
1999 Eukaryotic expression cloning with an antimetastatic monoclonal antibody identifies a tetraspanin (PETA-3/CD151) as an effector of human tumor cell migration and metastasis. Cancer research 140 10447000
2003 Tetraspanin CD151 regulates alpha6beta1 integrin adhesion strengthening. Proceedings of the National Academy of Sciences of the United States of America 134 12805567
2002 An extracellular site on tetraspanin CD151 determines alpha 3 and alpha 6 integrin-dependent cellular morphology. The Journal of cell biology 133 12356873
2003 alpha3beta1 integrin-CD151, a component of the cadherin-catenin complex, regulates PTPmu expression and cell-cell adhesion. The Journal of cell biology 132 14691142
2002 Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo. Journal of cell science 129 11884516
2013 Tetraspanin CD151 mediates papillomavirus type 16 endocytosis. Journal of virology 121 23302890
2007 Tetraspanin CD151 promotes cell migration by regulating integrin trafficking. The Journal of biological chemistry 114 17716972
2010 Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists. Cancer research 111 20197472
2006 A critical role for tetraspanin CD151 in alpha3beta1 and alpha6beta4 integrin-dependent tumor cell functions on laminin-5. Molecular biology of the cell 109 16571677
2010 CD151 modulates expression of matrix metalloproteinase 9 and promotes neoangiogenesis and progression of hepatocellular carcinoma. Hepatology (Baltimore, Md.) 108 20578262
2002 Function of the tetraspanin CD151-alpha6beta1 integrin complex during cellular morphogenesis. Molecular biology of the cell 108 11809818
2003 CD151 regulates epithelial cell-cell adhesion through PKC- and Cdc42-dependent actin cytoskeletal reorganization. The Journal of cell biology 105 14557253
2002 CD151 enhances cell motility and metastasis of cancer cells in the presence of focal adhesion kinase. International journal of cancer 97 11774285
2001 Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis. The Journal of biological chemistry 94 11479292
2006 Homophilic interactions of Tetraspanin CD151 up-regulate motility and matrix metalloproteinase-9 expression of human melanoma cells through adhesion-dependent c-Jun activation signaling pathways. The Journal of biological chemistry 90 16798740
1995 Molecular cloning of cDNA encoding a novel platelet-endothelial cell tetra-span antigen, PETA-3. Blood 90 7632941
1999 Transmembrane 4 superfamily protein CD151 (PETA-3) associates with beta 1 and alpha IIb beta 3 integrins in haemopoietic cell lines and modulates cell-cell adhesion. The Biochemical journal 87 9931299
2013 CD151 in cancer progression and metastasis: a complex scenario. Laboratory investigation; a journal of technical methods and pathology 86 24247563
2007 Roles of rapH and rapG in positive regulation of rapamycin biosynthesis in Streptomyces hygroscopicus. Journal of bacteriology 82 17468238
2007 Role of CD151, A tetraspanin, in porcine reproductive and respiratory syndrome virus infection. Virology journal 80 17572908
2013 MicroRNA-124 suppresses breast cancer cell growth and motility by targeting CD151. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 79 23816858
2008 DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151. Molecular biology of the cell 79 18508921
1996 SFA-1, a novel cellular gene induced by human T-cell leukemia virus type 1, is a member of the transmembrane 4 superfamily. Journal of virology 74 8627808
2009 CD151 regulates tumorigenesis by modulating the communication between tumor cells and endothelium. Molecular cancer research : MCR 72 19531562
2012 Integrin-associated CD151 drives ErbB2-evoked mammary tumor onset and metastasis. Neoplasia (New York, N.Y.) 68 22952421
2011 Blood pressure influences end-stage renal disease of Cd151 knockout mice. The Journal of clinical investigation 68 22201679
2010 Tetraspanin CD151 regulates transforming growth factor beta signaling: implication in tumor metastasis. Cancer research 68 20570898
2024 CD151-enriched migrasomes mediate hepatocellular carcinoma invasion by conditioning cancer cells and promoting angiogenesis. Journal of experimental & clinical cancer research : CR 67 38840183
2006 Bacillus subtilis RghR (YvaN) represses rapG and rapH, which encode inhibitors of expression of the srfA operon. Molecular microbiology 66 16553878
2009 Tetraspanin CD151 regulates RhoA activation and the dynamic stability of carcinoma cell-cell contacts. Journal of cell science 65 19509057
2009 Tetraspanins CD37 and CD151 differentially regulate Ag presentation and T-cell co-stimulation by DC. European journal of immunology 64 19089816
2018 Extracellular vesicles with altered tetraspanin CD9 and CD151 levels confer increased prostate cell motility and invasion. Scientific reports 62 29891991
2005 Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151. Laboratory investigation; a journal of technical methods and pathology 62 16200075
2012 Clinical significance of CD151 overexpression in subtypes of invasive breast cancer. British journal of cancer 60 22294188
2021 Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer. Molecular & cellular proteomics : MCP 59 34265469
2012 Tetraspanin CD151 plays a key role in skin squamous cell carcinoma. Oncogene 59 22824799
2013 Tspan8 and CD151 promote metastasis by distinct mechanisms. European journal of cancer (Oxford, England : 1990) 57 23683890
2008 Regulation of CD151 by hypoxia controls cell adhesion and metastasis in colorectal cancer. Clinical cancer research : an official journal of the American Association for Cancer Research 56 19073968
2014 Tetraspanins CD9 and CD151 at the immune synapse support T-cell integrin signaling. European journal of immunology 54 24723389
2011 Tetraspanin CD151 as a target for antibody-based cancer immunotherapy. Biochemical Society transactions 52 21428938
2008 Tetraspanin CD151 regulates glycosylation of (alpha)3(beta)1 integrin. The Journal of biological chemistry 52 18852263
2013 Integrin-free tetraspanin CD151 can inhibit tumor cell motility upon clustering and is a clinical indicator of prostate cancer progression. Cancer research 48 24220242
2011 Tetraspanin CD151 maintains vascular stability by balancing the forces of cell adhesion and cytoskeletal tension. Blood 48 21832275
2005 CD151 forms a functional complex with c-Met in human salivary gland cancer cells. Biochemical and biophysical research communications 48 16139245
1998 SFA-1/PETA-3 (CD151), a member of the transmembrane 4 superfamily, associates preferentially with alpha 5 beta 1 integrin and regulates adhesion of human T cell leukemia virus type 1-infected T cells to fibronectin. Journal of immunology (Baltimore, Md. : 1950) 48 9743375
2010 The tetraspanin CD151 is required for Met-dependent signaling and tumor cell growth. The Journal of biological chemistry 47 20937830
2007 CD151 dynamics in carcinoma-stroma interaction: integrin expression, adhesion strength and proteolytic activity. Laboratory investigation; a journal of technical methods and pathology 45 17632541
2021 CD151 drives cancer progression depending on integrin α3β1 through EGFR signaling in non-small cell lung cancer. Journal of experimental & clinical cancer research : CR 44 34108040
2017 Recessive mutation in tetraspanin CD151 causes Kindler syndrome-like epidermolysis bullosa with multi-systemic manifestations including nephropathy. Matrix biology : journal of the International Society for Matrix Biology 44 29138120
2011 Diminished metastasis in tetraspanin CD151-knockout mice. Blood 44 21536858
2013 The CD9/CD81 tetraspanin complex and tetraspanin CD151 regulate α3β1 integrin-dependent tumor cell behaviors by overlapping but distinct mechanisms. PloS one 40 23613949
2010 Overexpression of CD151 as an adverse marker for intrahepatic cholangiocarcinoma patients. Cancer 40 20715158
2014 MiR-506 inhibits PRRSV replication in MARC-145 cells via CD151. Molecular and cellular biochemistry 39 24878990
2014 miR-152 suppresses gastric cancer cell proliferation and motility by targeting CD151. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 39 25119599
2008 The tetraspanin CD151 regulates cell morphology and intracellular signaling on laminin-511. The FEBS journal 38 18492066
2006 Activation of the phosphatidylinositol 3-kinase/protein kinase Akt pathway mediates CD151-induced endothelial cell proliferation and cell migration. The international journal of biochemistry & cell biology 38 17045834
2019 miR-199a-3p promotes cardiomyocyte proliferation by inhibiting Cd151 expression. Biochemical and biophysical research communications 37 31186138
2012 CD151 restricts the α6 integrin diffusion mode. Journal of cell science 37 22328509
2015 CD151-A Striking Marker for Cancer Therapy. Biomarkers in cancer 36 25861224
2014 The tetraspanin CD151 in papillomavirus infection. Viruses 36 24553111
2011 Profiling of the tetraspanin CD151 web and conspiracy of CD151/integrin β1 complex in the progression of hepatocellular carcinoma. PloS one 36 21961047
2013 Integrin α3β1-CD151 complex regulates dimerization of ErbB2 via RhoA. Oncogene 35 23792450
2018 Tspan8 and Tspan8/CD151 knockout mice unravel the contribution of tumor and host exosomes to tumor progression. Journal of experimental & clinical cancer research : CR 34 30541597
2018 MiR-124 aggravates failing hearts by suppressing CD151-facilitated angiogenesis in heart. Oncotarget 32 29581851
2017 Interrogation of Functional Cell-Surface Markers Identifies CD151 Dependency in High-Grade Serous Ovarian Cancer. Cell reports 32 28273451
2011 CD151 expression can predict cancer progression in clear cell renal cell carcinoma. Histopathology 30 21323946
2009 CD151 gene delivery after myocardial infarction promotes functional neovascularization and activates FAK signaling. Molecular medicine (Cambridge, Mass.) 30 19603100
2006 CD151 gene delivery activates PI3K/Akt pathway and promotes neovascularization after myocardial infarction in rats. Molecular medicine (Cambridge, Mass.) 30 17225869
2019 Tetraspanin CD151 and integrin α3β1 contribute to the stabilization of integrin α6β4-containing cell-matrix adhesions. Journal of cell science 28 31488507
2016 Tetraspanin CD151 Promotes Initial Events in Human Cytomegalovirus Infection. Journal of virology 28 27147745
2016 The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding site of integrin αvβ3. The Biochemical journal 28 27993971
2009 CD151 regulates HGF-stimulated morphogenesis of human breast cancer cells. Biochemical and biophysical research communications 28 19159612
2022 JAM-A interacts with α3β1 integrin and tetraspanins CD151 and CD9 to regulate collective cell migration of polarized epithelial cells. Cellular and molecular life sciences : CMLS 27 35067832
2012 Knockdown of cathepsin B and uPAR inhibits CD151 and α3β1 integrin-mediated cell adhesion and invasion in glioma. Molecular carcinogenesis 26 22495828
2020 The CD151-midkine pathway regulates the immune microenvironment in inflammatory breast cancer. The Journal of pathology 25 32129471
2021 Activation of GPER by E2 promotes proliferation, invasion and migration of breast cancer cells by regulating the miR-124/CD151 pathway. Oncology letters 24 33868470
2016 CD151 mediates netrin-1-induced angiogenesis through the Src-FAK-Paxillin pathway. Journal of cellular and molecular medicine 24 27558487
2015 CD151 knockdown inhibits osteosarcoma metastasis through the GSK-3β/β-catenin/MMP9 pathway. Oncology reports 24 26707073
2013 Tetraspanins CD9 and CD151, epidermal growth factor receptor and cyclooxygenase-2 expression predict malignant progression in oral epithelial dysplasia. British journal of cancer 24 24201754
2010 The migration and invasion of human prostate cancer cell lines involves CD151 expression. Oncology reports 24 21042756
2012 CD151 promotes cancer cell metastasis via integrins α3β1 and α6β1 in vitro. Molecular medicine reports 23 23007325
2013 CD151 is associated with prostate cancer cell invasion and lymphangiogenesis in vivo. Oncology reports 22 24174171
2011 An atypical Phr peptide regulates the developmental switch protein RapH. Journal of bacteriology 21 21908671
2023 Exploring the role of CD151 in the tumor immune microenvironment: Therapeutic and clinical perspectives. Biochimica et biophysica acta. Reviews on cancer 20 37094754
2020 CD151 in Respiratory Diseases. Frontiers in cell and developmental biology 20 32117989
2019 Integrin-independent support of cancer drug resistance by tetraspanin CD151. Cellular and molecular life sciences : CMLS 20 30778617
2016 Regulation of Glioblastoma Tumor-Propagating Cells by the Integrin Partner Tetraspanin CD151. Neoplasia (New York, N.Y.) 20 26992919
2011 Role of tetraspanin CD151-α3/α6 integrin complex: Implication in angiogenesis CD151-integrin complex in angiogenesis. The international journal of biochemistry & cell biology 20 21237282
2021 The Context-Dependent Impact of Integrin-Associated CD151 and Other Tetraspanins on Cancer Development and Progression: A Class of Versatile Mediators of Cellular Function and Signaling, Tumorigenesis and Metastasis. Cancers 19 33919420
2020 Expression and distribution of CD151 as a partner of alpha6 integrin in male germ cells. Scientific reports 19 32152440
2016 CD151 Regulates T-Cell Migration in Health and Inflammatory Bowel Disease. Inflammatory bowel diseases 19 26529559

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