| 2000 |
Crystal structure of P-selectin lectin-EGF domains co-complexed with the N-terminal domain of human PSGL-1 modified by tyrosine sulfation and sialyl Lewis X revealed the molecular basis of high-affinity P-selectin/PSGL-1 interaction, showing how sulfated tyrosines and glycan cooperate for binding. |
X-ray crystallography (crystal structure of P-selectin LE domains with PSGL-1 N-terminal peptide) |
Cell |
High |
11081633
|
| 1995 |
Tyrosine sulfation of a consensus motif within the N-terminal ~20 residues of PSGL-1 is essential for P-selectin binding; mutation of N-terminal tyrosines to phenylalanine abolishes P-selectin adhesion, and sulfation inhibitors block HL-60 rolling on P-selectin. |
Site-directed mutagenesis, sulfation inhibitors, cell rolling assay on P-selectin-coated coverslips |
Cell |
High |
7585950
|
| 1998 |
Dimerization of PSGL-1 through a single conserved extracellular cysteine (C320) is essential for functional recognition of P-selectin; monomeric C320A mutant fails to support rolling or binding to P-selectin chimeras despite intact surface expression. |
Cysteine-to-alanine mutagenesis, Western blot under native/denaturing conditions, low-shear adhesion and flow-chamber rolling assays in stable K562 transfectants |
The Journal of cell biology |
High |
9660879
|
| 1999 |
PSGL-1 is required for P-selectin-mediated neutrophil rolling and leukocyte recruitment in early inflammation (30 min post-trauma); however, it is not required for E-selectin-mediated rolling 2 h after TNF-α stimulation, as shown in PSGL-1 gene-knockout mice. |
Targeted gene disruption (PSGL-1 knockout mice), intravital microscopy of cremaster venules, chemical peritonitis model |
The Journal of experimental medicine |
High |
10601352
|
| 2002 |
PSGL-1 associates with Syk kinase through ERM proteins (ezrin/moesin); engagement of PSGL-1 induces Syk tyrosine phosphorylation and SRE-dependent transcriptional activation. ITAM-mutated moesin or Syk dead-kinase mutant abrogates PSGL-1-induced transcription. |
Co-immunoprecipitation, dominant-negative overexpression, pharmacological Syk inhibition (piceatannol), SRE reporter assay |
Immunity |
High |
12387735
|
| 2002 |
Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton via moesin (but not other ERM proteins) is essential for leukocyte rolling on P-selectin; cytoplasmic truncation abolishes rolling without affecting P-selectin binding or surface distribution of PSGL-1. |
Stable transfection with truncated PSGL-1 (ΔCyto), actin cytoskeletal toxin treatment, co-immunoprecipitation with ERM proteins, rolling assay in flow chamber |
Blood |
High |
12036880
|
| 2008 |
The PSGL-1 cytoplasmic domain is dispensable for leukocyte rolling on P-selectin (when PSGL-1 surface density is matched) but is essential for Syk-dependent activation of LFA-1 (αLβ2) to convert fast rolling to slow rolling on ICAM-1. |
ΔCD knock-in mice expressing cytoplasmic-domain-deleted PSGL-1, O-sialoglycoprotein endopeptidase titration to match PSGL-1 density, intravital microscopy, Syk phosphorylation assay |
Blood |
High |
18550846
|
| 2008 |
E-selectin engagement of PSGL-1 activates Syk and p38 MAPK to induce slow neutrophil rolling via an ITAM-dependent pathway requiring Src-family kinase Fgr and ITAM adaptor proteins DAP12 and FcRγ, independently of Gαi-coupled receptors. |
Gene-deficient mice (fgr−/−, Tyrobp−/− Fcrg−/−), flow chamber rolling assay, intravital microscopy, Syk/p38 phosphorylation assay, mixed bone marrow chimeras, peritonitis model |
The Journal of experimental medicine |
High |
18794338
|
| 2010 |
E-selectin engagement of either PSGL-1 or CD44 triggers slow rolling through a common lipid-raft-dependent pathway using SFKs Hck, Lyn, and Fgr; Bruton's tyrosine kinase (BTK) acts as a key intermediate between Syk and p38. PSGL-1's cytoplasmic domain is required for SFK activation during this process. |
Gene-deficient mice, flow chamber and intravital microscopy, lipid raft disruption, kinase inhibitors, phosphorylation assays |
Blood |
High |
20299514
|
| 2007 |
Among E-selectin ligands on neutrophils, PSGL-1 plays the major role in initial leukocyte capture, ESL-1 is critical for converting initial tethers to slow rolling, and CD44 controls rolling velocity and mediates E-selectin-dependent redistribution of PSGL-1 and L-selectin to the major pole via p38 signaling. |
Gene-targeted and RNA-targeted loss-of-function in mice, intravital microscopy, flow chamber assay |
Immunity |
High |
17442598
|
| 1996 |
PSGL-1 on neutrophils serves as a ligand for L-selectin, supporting L-selectin–PSGL-1-mediated neutrophil–neutrophil aggregation as the first step in homotypic aggregation. |
Anti-PSGL-1 Fab inhibition, simultaneous antibody blocking of L-selectin and PSGL-1 on separate cell populations, flow cytometry aggregation assay |
Blood |
Medium |
8839831
|
| 1997 |
PSGL-1 is the sole P-selectin-binding glycoprotein on Th1 cells (not Th2 cells) despite similar surface expression levels; PSGL-1 on Th1 supports P-selectin binding and partially mediates their migration into cutaneous delayed-type hypersensitivity lesions. |
Affinity isolation with P-selectin-Ig fusion protein, flow cytometry binding assay, antibody blocking in cell adhesion assay and in vivo DTH model |
The Journal of experimental medicine |
High |
9053457
|
| 1999 |
PSGL-1 engagement by P-selectin on activated platelets triggers tyrosine kinase-dependent (genistein-sensitive) phosphorylation of a 110 kDa protein and activates CD11b/CD18 (β2 integrin) on PMNs; a non-adhesion-blocking anti-PSGL-1 antibody alone triggers the same β2-integrin-dependent aggregation. |
Mixed-cell shear-flow aggregation assay, antibody blocking (anti-P-selectin, anti-CD11b/CD18, anti-PSGL-1), tyrosine kinase inhibitors (genistein), tyrosine phosphorylation assay, CHO-P transfectants |
Blood |
High |
9920836
|
| 2013 |
A subset of PSGL-1 molecules is constitutively associated with L-selectin on neutrophils; this PSGL-1–L-selectin complex signals through Src family kinases and ITAM adaptors to activate LFA-1, and requires the L-selectin cytoplasmic tail for signaling output. |
Co-immunoprecipitation of endogenous PSGL-1 and L-selectin, L-selectin cytoplasmic tail mutants, flow chamber rolling assay, intravital microscopy, SFK inhibitors |
The Journal of experimental medicine |
High |
24127491
|
| 2007 |
PSGL-1 signals through Akt/mTOR upon macrophage adherence to promote translational upregulation of ROCK-1 (but not ROCK-2) mRNA, which is required for macrophage chemotaxis and phagocytosis; PSGL-1-deficient macrophages phenocopy mTOR inhibition. |
PSGL-1−/− macrophages, rapamycin treatment, ribosome loading assay, ROCK-1/2 Western blot, chemotaxis and phagocytosis assays |
The EMBO journal |
High |
17245434
|
| 2016 |
PSGL-1 ligation on exhausted CD8+ T cells inhibits TCR and IL-2 signaling and upregulates PD-1, leading to diminished survival upon TCR stimulation. PSGL-1-deficient mice clear chronic virus due to intrinsically improved effector T cell survival with reduced inhibitory receptor expression. |
PSGL-1−/− mice in chronic LCMV infection model, TCR/IL-2 signaling assays, PD-1 expression measurement, T cell survival assays, melanoma tumor model |
Immunity |
High |
27192578
|
| 2023 |
PSGL-1 attenuates TCR signaling upstream of PD-1 by directly restraining Zap70 phosphorylation and maintaining expression of the Zap70 inhibitor Sts-1; PSGL-1 requires co-ligation with TCR to suppress CD8+ T cell activation and drive terminal exhaustion. |
PSGL-1−/− mice, Zap70 phosphorylation assays, Sts-1 expression analysis, co-ligation experiments, tumor models with pharmacologic PSGL-1 blockade |
Cell reports |
High |
37115668
|
| 2019 |
VISTA binds PSGL-1 selectively at acidic pH through multiple histidine residues along the rim of the VISTA extracellular domain; this interaction suppresses T cells in the tumor microenvironment and can be blocked by pH-selective antibodies. |
Binding assays, site-directed mutagenesis of VISTA histidines, pH-selective blocking antibodies, in vivo immune suppression assays |
Nature |
High |
31645726
|
| 2019 |
HIV-1 Vpu binds PSGL-1 and induces its ubiquitination and degradation through the ubiquitin ligase SCFβ-TrCP2; PSGL-1 (induced by IFN-γ) inhibits HIV-1 reverse transcription and blocks virion infectivity by incorporating into progeny virions. |
Isobaric-tag mass spectrometry proteomics, co-immunoprecipitation, ubiquitination assay, siRNA knockdown, HIV infectivity assays, reverse transcription assay in primary CD4+ T cells |
Nature microbiology |
High |
30833724
|
| 2020 |
Virion-incorporated PSGL-1 blocks HIV-1 infectivity by preventing attachment of virions to target cells, independently of the viral glycoprotein; the extracellular N-terminal domain of PSGL-1 is necessary, and the cytoplasmic tail contributes to inhibition. Vpu (and Nef) down-regulate PSGL-1 from the cell surface to partially escape this restriction. |
HIV infectivity assays with PSGL-1 domain deletion mutants, particle attachment assays to CD4+ cells, Vpu/Nef expression, murine leukemia virus and influenza A virus infectivity assays |
Proceedings of the National Academy of Sciences of the United States of America |
High |
32193343 32273392
|
| 2020 |
Virion incorporation of PSGL-1 and CD43 inhibits HIV-1 attachment to both CD4+ target cells and fibroblastic reticular cells mediating transinfection; the full-length ectodomain of PSGL-1 is required, consistent with steric blockade of virus-cell contact. |
HIV-1 particle attachment assays, PSGL-1 ectodomain truncation mutants, CD4− cell transinfection assay, Gag copatching analysis |
Proceedings of the National Academy of Sciences of the United States of America |
High |
32193343
|
| 2020 |
PSGL-1 directly binds F-actin to restrict actin dynamics, inhibiting HIV DNA synthesis; incorporated PSGL-1 also binds gp41 and sequesters it at the plasma membrane, reducing Env incorporation into virions and impairing viral entry. |
F-actin co-sedimentation/binding assay, cryo-EM and super-resolution imaging of Env on virions, gp41 co-immunoprecipitation, HIV DNA synthesis assay |
Cell discovery |
Medium |
32802403
|
| 2007 |
Crystal structure of the radixin FERM domain complexed with a PSGL-1 juxtamembrane peptide reveals that PSGL-1 binds FERM subdomain C in a beta-strand mode; non-conserved large residues (Met9, His8) compensate for the absence of the canonical Motif-1 alanine, providing structural basis for PSGL-1–ERM interaction. |
X-ray crystallography of radixin FERM–PSGL-1 peptide complex |
Genes to cells |
High |
18076570
|
| 2004 |
Human FucT-VII plays the predominant role in generating selectin-binding carbohydrate ligands on PSGL-1, while FucT-IV also contributes; core-2 O-glycans attached to Thr-57 are critical for L- and P-selectin rolling, whereas E-selectin uses additional PSGL-1 binding sites (>75% of rolling is Thr-57-independent). |
CHO cell transfections with FucT-IV and/or FucT-VII plus core-2 GlcNAcT, PSGL-1 Thr-57 and Thr-44 alanine mutants, rolling adhesion assays on L-, P-, and E-selectin |
The Journal of biological chemistry |
High |
15579466
|
| 2002 |
For L-selectin binding, Tyr-51 at the PSGL-1 N-terminus plays a predominant role (contrasting with P-selectin where Tyr-48 is key); core-2 O-glycans on Thr-57 are critical for optimal L-selectin binding and for controlling rolling velocity. |
Tyr-to-Phe and Thr-to-Ala mutagenesis, CHO cell expression with core-2 GlcNAcT and FucT-VII, L-selectin binding assays, rolling adhesion assays, molecular modeling |
The Journal of biological chemistry |
High |
12403782
|
| 2000 |
PSGL-1 is expressed on platelets at 25–100-fold lower levels than leukocytes; platelet PSGL-1 is functional and mediates platelet rolling in mesenteric venules, as shown by anti-PSGL-1 antibody blockade in intravital microscopy. |
P-selectin-IgG affinity purification, Western blot, anti-PSGL-1 immunopurification, flow cytometry, intravital microscopy with antibody blockade |
The Journal of experimental medicine |
High |
10770806
|
| 2005 |
P-selectin and its ligand PSGL-1 mediate recruitment of adult lymphoid progenitors to the thymus; PSGL-1−/− thymi contain fewer early thymic progenitors, and thymic P-selectin expression is regulated by niche occupancy, suggesting a homeostatic P-selectin/PSGL-1 thymic homing axis. |
Parabiosis, competitive thymus reconstitution, short-term homing assays, PSGL-1−/− mice |
Nature immunology |
High |
15880112
|
| 1999 |
PSGL-1 ligation on human CD34+ hematopoietic progenitor cells (the sole P-selectin receptor on these cells) by immobilized or soluble P-selectin, or by anti-PSGL-1 antibody, profoundly suppresses HPC proliferation stimulated by growth factors. |
P-selectin-IgG affinity purification to identify PSGL-1 as the sole receptor, immobilized/soluble ligand and antibody ligation, colony-forming proliferation assays |
Immunity |
High |
10514015
|
| 2013 |
Engagement of PSGL-1 and CXCR2 on rolling neutrophils cooperatively propagates signals to induce β2 integrin-dependent arrest in flow-restricted inferior vena cava. PSGL-1 signaling in this context uses Tyr-145 (not Tyr-112/128) of SLP-76 and does not require L-selectin; cooperative PSGL-1/CXCR2 signaling increases thrombus frequency and size partly by stimulating NET release. |
Genetically engineered mice, spinning-disk intravital microscopy, ultrasonography, IVC flow restriction model, pharmacological PSGL-1/CXCR2 blockade, NET quantification |
Blood |
High |
30068506
|
| 2011 |
ADAM8 metalloprotease is associated with PSGL-1 through ERM proteins and proteolytically cleaves PSGL-1; ADAM8 knockdown increases PSGL-1 surface expression and enhances leukocyte rolling on P-selectin, identifying ADAM8 as a sheddase regulating PSGL-1 function. |
Co-immunoprecipitation via ERM proteins, ADAM8 siRNA knockdown, PSGL-1 surface expression assay, leukocyte rolling assay on P-selectin |
European journal of immunology |
Medium |
22229154
|
| 2012 |
The ERM-binding sequence (EBS) of the PSGL-1 cytoplasmic tail (key residues Arg-337 and Lys-338) is required for leukocyte tethering and rolling on L-, P-, and E-selectin and for ERK activation; however, EBS is dispensable for Syk phosphorylation and E-selectin-induced slow rolling. |
EBS deletion and alanine-substitution mutagenesis in 32D leukocytes, rolling assays on selectins, ERK and Syk phosphorylation assays |
The Journal of biological chemistry |
High |
22311979
|
| 2012 |
PSGL-1 does not require dimerization or cytoskeletal anchorage to signal β2 integrin-dependent slow rolling; FRAP documented cytoskeletal restraint of WT PSGL-1, and actin depolymerization or cytoplasmic-tail mutation increasing lateral mobility did not impair slow rolling, whereas chemokine-triggered arrest remained cytoskeleton-dependent. |
FRAP, latrunculin B treatment, retroviral transduction of WT and mutant PSGL-1 into PSGL-1−/− macrophages, rolling/arrest assays, β2-hybrid domain swing-out assay |
The Journal of biological chemistry |
High |
22511754
|
| 2008 |
Sorting nexin 20/SLIC-1 interacts with the PSGL-1 cytoplasmic domain and directs PSGL-1 to endosomes via its Phox homology domain; loss of the murine SLIC-1 homologue does not alter PSGL-1 signaling or neutrophil adhesion, indicating SLIC-1 is a sorting but not signaling regulator. |
Yeast two-hybrid screen, co-immunoprecipitation, colocalization in endosomes, murine SLIC-1 KO functional assays |
European journal of immunology |
Medium |
18196517
|
| 2003 |
Peritoneal macrophages synthesize and constitutively express P-selectin on their plasma membrane; P-selectin is rapidly internalized to lysosomes. Macrophage-macrophage interactions in flow are mediated by P-selectin on one macrophage binding PSGL-1 on another. |
Metabolic labeling, flow cytometry, Western blot, immunoelectron microscopy, flow-based macrophage aggregation assay with blocking antibodies |
The Journal of cell biology |
Medium |
14662752
|
| 2009 |
Flotillin-1 and -2 co-immunoprecipitate and colocalize with PSGL-1 in resting and stimulated neutrophils, associating with PSGL-1 in actin-dependent membrane microdomains that accumulate in the uropod; PSGL-1 is not required for formation of flotillin caps. |
Co-immunoprecipitation, immunofluorescence colocalization, PSGL-1−/− neutrophils, differentiated HL-60 overexpression |
PloS one |
Medium |
19404397
|
| 2004 |
Sulfated tyrosines at the PSGL-1 N-terminus (not O-glycans or N-glycans) mediate interaction with the chemokine CCL27 (CTACK); mutation of N-terminal tyrosines to phenylalanine abolishes binding, and PSGL-1 expression on CCR10+ cells reduces chemotactic responses to CCL27. |
Recombinant PSGL-1-Ig binding assay with multiple chemokines, arylsulfatase/glycosidase treatment, sulfation-inhibitor synthesis, Tyr→Phe mutagenesis, CCR10+ cell chemotaxis assay |
The Journal of biological chemistry |
High |
15466853
|
| 2015 |
The N-termini of PSGL-1 and CCR7 have overlapping binding sites for CCL19; chemical-shift mapping shows the interactions are competitive, providing a structural basis for PSGL-1's enhancement of CCL19-mediated T cell recruitment. |
NMR solution structure of CCL19, chemical shift perturbation mapping with PSGL-1 and CCR7 N-terminal peptides |
Biochemistry |
Medium |
26115234
|
| 2007 |
EphB4 activation with ephrin-B2-Fc upregulates PSGL-1 expression on endothelial progenitor cells; PSGL-1 siRNA reverses both the enhanced EPC adhesion to E/P-selectin and the proangiogenic effect of EphB4 activation in a mouse hindlimb ischemia model. |
EphB4 siRNA, PSGL-1 siRNA, EPC adhesion assay, mouse hindlimb ischemia model, neutralizing antibodies to E/P-selectin |
The Journal of clinical investigation |
Medium |
17510705
|
| 2013 |
A single amino acid at EV71 capsid VP1-145 acts as a molecular switch controlling binding to PSGL-1: G or Q at VP1-145 permits binding to PSGL-1 sulfated tyrosines (mediated by conserved lysines VP1-242/244), while E at VP1-145 turns the VP1-244 lysine inward to prevent PSGL-1 binding. |
Site-directed mutagenesis of VP1-145, VP1-242, and VP1-244; cell binding assays on PSGL-1-expressing cells; crystal structure comparison of EV71 isolates |
PLoS pathogens |
High |
23935488
|
| 2013 |
EV71 entry mediated by PSGL-1 requires caveolar endocytosis (caveolin-1-dependent), whereas SCARB2-mediated entry uses clathrin-dependent endocytosis; PSGL-1 and SCARB2 thus dictate distinct endocytic routes for EV71. |
Specific endocytosis inhibitors, caveolin-1 siRNA, clathrin knockdown, confocal colocalization of EV71 with caveolae in Jurkat T cells and PSGL-1-L929 cells vs. RD cells |
Journal of virology |
High |
23760234
|
| 2016 |
Soluble Siglec-5 binds PSGL-1 on leukocytes in a sialic-acid-dependent and calcium-dependent manner (sialidase treatment reduces binding by 79%); PSGL-1 and Siglec-5 are in close proximity (<40 nm) on PBMCs. Soluble Siglec-5 variants block PSGL-1-mediated leukocyte rolling on E/P-selectin in vitro and in vivo. |
Soluble Siglec-5 binding assay, sialidase treatment, Duolink proximity ligation assay, in vitro perfusion rolling assay, in vivo TNF-α inflammation model |
Scientific reports |
Medium |
27892504
|
| 2021 |
GALNT4-catalyzed O-glycosylation of PSGL-1 is required for P-selectin-induced β2 integrin activation on monocytes and for monocyte adhesion and transmigration; GALNT4 overexpression increases PSGL-1 O-glycosylation and activates Akt/mTOR and IκBα/NFκB downstream of P-selectin/PSGL-1 engagement. |
VVL lectin pulldown, PSGL-1 immunoprecipitation for O-glycosylation, GALNT4 shRNA knockdown and overexpression, β2-integrin activation assay, monocyte adhesion/transmigration under flow, ApoE−/− mouse atherosclerosis model |
Journal of molecular and cellular cardiology |
Medium |
34974060
|
| 2023 |
P-selectin binding to PSGL-1 on tumor-associated macrophages activates the JNK/STAT1 pathway, driving transcription of complement C5 and release of C5a, which activates C5aR1 to shift TAMs toward a pro-tumor phenotype; PSGL-1 inhibition reduces CRC growth. |
Western blot for JNK/STAT1, dual-luciferase reporter and ChIP assay for C5 transcription, ELISA for C5a, siRNA knockdown of PSGL-1, AOM/DSS mouse CRC model, FACS |
Theranostics |
Medium |
37064877
|
| 2023 |
P-selectin stimulation of neutrophils via PSGL-1 activates the Syk/Ca2+/PAD4 signaling pathway to induce NET formation; pharmacological inhibition of P-selectin (PSI-697) reduces PAD4 expression and NETs in pancreatic tissue and ameliorates acute pancreatitis in mice. |
Western blot for Syk phosphorylation, intracellular calcium imaging, PAD4 expression assay, flow cytometry and immunofluorescence for NETs, PSI-697 treatment in caerulein-AP mouse model |
Frontiers in immunology |
Medium |
37841279
|
| 2014 |
PSGL-1 (CD162) but not CD44, when deleted by CRISPR-Cas9 from AML cell line KG1a, abolishes E-selectin-mediated chemo-resistance in vitro; absence of CD162 on AML cells delays leukemia onset, reduces BM retention, and increases chemotherapy sensitivity in vivo. |
CRISPR-Cas9 knockout of CD162 or CD44, in vitro E-selectin adhesion/chemo-resistance assays, preclinical murine AML model |
Frontiers in cell and developmental biology |
High |
32793603
|
| 2014 |
Basic residues in HIV-1 Gag matrix domain and a polybasic sequence in the PSGL-1 cytoplasmic tail mediate coclustering of PSGL-1 with assembling Gag at the plasma membrane, promoting virion incorporation of PSGL-1. |
Quantitative two-color superresolution localization microscopy, Gag matrix mutants, PSGL-1 cytoplasmic tail chimera experiments in T and HeLa cells |
Journal of virology |
Medium |
25320329
|
| 2020 |
PSGL-1 expression in virus-producing cells impairs incorporation of SARS-CoV and SARS-CoV-2 spike glycoproteins into pseudovirions and blocks pseudovirus attachment and infection of target cells, extending PSGL-1's antiviral restriction to coronaviruses. |
Pseudovirus infectivity assays, spike glycoprotein incorporation Western blot, PSGL-1 expression in virus-producing cells |
Viruses |
Medium |
33396594
|
| 2005 |
PSGL-1 cross-linking induces tyrosine-phosphorylation-dependent and c-Abl-involved F-actin polymerization and redistribution in neutrophils; c-Abl relocalizes to F-actin foci, and the Abl inhibitor STI571 blocks the cytoskeletal reorganization. |
Anti-PSGL-1 antibody cross-linking, cytoskeletal fractionation, genistein and STI571 inhibition, F-actin immunofluorescence and redistribution assay |
Journal of cellular biochemistry |
Medium |
15526280
|
| 1998 |
Characterization of O-linked oligosaccharides on PSGL-1 isolated from HL-60 cells showed that only ~4.5% of O-linked glycans (core-2 structures with sialic acid and fucose on N-acetyllactosamine) constitute the selectin-binding fraction; most O-glycans lack fucose and are insufficient for selectin binding. |
3H-glucosamine metabolic labeling, P-selectin/E-selectin affinity chromatography, ion-exchange/size exclusion/lectin/paper chromatography, exoglycosidase treatments, chemical modifications |
Glycoconjugate journal |
Medium |
10211703
|
| 2014 |
PI3K is required for PSGL-1-induced β1 integrin clustering (but not for β1 integrin conformation changes or total expression), and PSGL-1-PI3K-β1 integrin signaling promotes Jurkat cell adhesion to fibronectin. |
PI3K inhibitors, anti-PSGL-1 antibody ligation, β1 integrin clustering assay, conformation-sensitive antibody assay, Jurkat adhesion to fibronectin |
Molecular and cellular biochemistry |
Low |
24122451
|