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Showing SKAP1 — SKAP55 is a alias.

SKAP1

Src kinase-associated phosphoprotein 1 · UniProt Q86WV1

Length
359 aa
Mass
41.4 kDa
Annotated
2026-06-10
40 papers in source corpus 26 papers cited in narrative 26 extracted findings
Cross-family judge vs UniProt: tie faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SKAP1 (SKAP55) is a T cell-restricted cytosolic adaptor that couples T-cell receptor (TCR) engagement to integrin-mediated adhesion through 'inside-out' signaling, controlling LFA-1 clustering and the formation of stable T cell-antigen-presenting cell conjugates (PMID:12652296, PMID:15939789). It functions as part of a constitutive module with the adaptor ADAP (FYB/SLAP-130), an interaction mediated by the SKAP1 SH3 domain binding a proline-rich region of ADAP and reciprocally stabilizing SKAP1 against proteolytic degradation (PMID:9748251, PMID:15849195). The ADAP/SKAP1 module recruits activated Rap1 to the plasma membrane, where SKAP1 bridges Rap1 to its effector RapL via a direct N-terminal interaction with the RapL SARAH domain, assembling a SKAP1-RapL-Rap1 complex that engages LFA-1 and drives integrin activation (PMID:16980616, PMID:20346707). Membrane localization of this module requires the SKAP1 PH domain, which directs RapL membrane translocation and, through residue-specific actin binding, promotes talin recruitment to LFA-1 (PMID:21669874, PMID:28052935); SKAP1 loss alters calpain-mediated talin cleavage and impairs talin/RIAM delivery to the contact interface (PMID:24368808, PMID:26905930). Beyond adhesion, SKAP1 binds the Ras activator RasGRP1 through its C-terminus to negatively regulate the Ras-ERK pathway (PMID:18320039), and the ADAP/SKAP1 module promotes PD-1 expression on CD8+ T cells via an NFATc1-dependent pathway, with its deletion enhancing anti-tumor immunity (PMID:25851535). SKAP1 was first identified as a constitutive partner of the Src-family kinase Fyn and a Fyn substrate, with Fyn-mediated phosphorylation of a non-canonical RKxxYxxY motif controlling its interactions (PMID:9195899, PMID:10856234, PMID:16461356).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1997 High

    Established SKAP1 as a Src-kinase-associated adaptor, defining its domain architecture and placing it within proximal TCR signaling.

    Evidence GST-SH2 pulldown, molecular cloning, and in vitro SH2 binding assays in T-lymphocytes

    PMID:9195899

    Open questions at the time
    • Functional consequence of Fyn association not established
    • Downstream effectors unknown at this stage
  2. 1998 High

    Identified ADAP (FYB/SLAP-130) as the principal SH3-domain partner of SKAP1, defining the core adaptor module.

    Evidence Yeast two-hybrid, co-IP, and truncation mapping in T and COS cells

    PMID:9671755 PMID:9748251

    Open questions at the time
    • Functional output of the ADAP-SKAP1 complex not yet defined
    • Whether the interaction is constitutive or regulated unclear
  3. 2000 High

    Defined a proline-independent RKxxYxxY motif as the structural basis for Fyn-SH3 recognition of SKAP1, linking the interaction to TCR-driven transcription.

    Evidence Peptide precipitation, alanine scanning, 2D NMR, and NF-AT reporter assay

    PMID:10856234

    Open questions at the time
    • Physiological role of Fyn-SKAP1 binding in adhesion not yet connected
  4. 2003 High

    Showed SKAP1 controls integrin-mediated adhesion and immunological synapse formation, defining its core cellular function in inside-out signaling.

    Evidence Overexpression/dominant-negative studies, adhesion assays, confocal microscopy, raft fractionation

    PMID:12652296

    Open questions at the time
    • Molecular link from SKAP1 to LFA-1 not yet identified
    • SH3-domain dependence implicated but mechanism unresolved
  5. 2005 High

    Demonstrated SKAP1 is non-redundantly required for TCR-induced LFA-1 clustering and that its stability depends on ADAP, establishing the module as a functional unit.

    Evidence siRNA knockdown with LFA-1 clustering/conjugation readouts; ADAP-deficient cell reconstitution with pulse-chase half-life analysis

    PMID:15849195 PMID:15939789

    Open questions at the time
    • The membrane effector bridging SKAP1 to integrin still unidentified
    • Mechanism of SKAP1 proteolysis in absence of ADAP unknown
  6. 2006 High

    Identified Rap1 membrane recruitment as the output of the ADAP/SKAP1 module and mapped Fyn phosphorylation of Y294 as a regulatory switch for the ADAP-SKAP1 interaction.

    Evidence Dominant-negative module disruption, Rap1 activity/fractionation assays, SPR binding, and Y294F/Y297F mutagenesis with functional readouts

    PMID:16461356 PMID:16980616

    Open questions at the time
    • How Rap1 connects to LFA-1 downstream not yet defined
    • Effector linking Rap1 to integrin still unknown
  7. 2008 High

    Established a second SKAP1 function as a negative regulator of the Ras-ERK pathway through C-terminal binding of RasGRP1.

    Evidence Knockout primary T cells, RNAi, co-IP, C-terminal deletion mutants, ERK/ELK assays, RasGRP1 localization

    PMID:17658605 PMID:18320039

    Open questions at the time
    • Mechanism by which SKAP1 controls RasGRP1 Golgi localization unresolved
    • Integration of adhesion and Ras-regulatory roles unclear
  8. 2011 High

    Resolved the SKAP1-RapL-Rap1-LFA-1 connectivity, showing the N-terminus binds the RapL SARAH domain and the PH domain drives RapL membrane localization to assemble the integrin-activating complex.

    Evidence Skap1-/- primary T cells, co-IP, RapL L224A and PH-domain R131M mutants, intravital two-photon imaging, membrane fractionation

    PMID:20346707 PMID:21525391 PMID:21669874

    Open questions at the time
    • PH-domain lipid/membrane ligand not directly identified at this stage
    • Distinction between integrin and NF-kB arms of ADAP only partially mapped
  9. 2013 High

    Showed SKAP1 dimerization and ADAP binding are required for SLP-76 microcluster stabilization and recruitment of RIAM/talin, extending its scaffolding role to junctional stability and beta1 integrins.

    Evidence Live-cell SLP-76 microcluster imaging, dimerization mutants, tandem-dimer constructs, RIAM/talin co-IP, adhesion assays

    PMID:24368808

    Open questions at the time
    • How dimerization couples to talin recruitment mechanistically unresolved
  10. 2016 Medium

    Linked SKAP1 to talin processing, showing it controls calpain-mediated talin cleavage and talin/RIAM delivery to the contact interface.

    Evidence Skap1-/- T cells, talin/RIAM localization, talin cleavage assay, non-cleavable talin L432G rescue

    PMID:26905930

    Open questions at the time
    • Single lab; direct biochemical link between SKAP1 and calpain not established
    • How SKAP1 modulates cleavage mechanistically unknown
  11. 2017 High

    Defined SKAP1 in an LFA-1/FAK1-driven de-adhesion pathway via LAT-GRB2-SKAP1 complexes, and refined PH-domain control of cytoplasmic versus membrane localization.

    Evidence Co-IP, LAT Y171 mutant, FAK1/PYK2 assays, T cell-DC dwell time and proliferation assays; PH-domain D120/K152 mutants with actin co-IP

    PMID:28052935 PMID:28699640

    Open questions at the time
    • Switch between adhesion-promoting and de-adhesion complexes not fully mapped
    • K152-actin functional data from single lab (Medium)
  12. 2019 Medium

    Extended SKAP1 function beyond adhesion to T-cell cycle control as a scaffold for PLK1 at serine 31, with PD-1 regulation establishing immunoregulatory roles.

    Evidence siRNA knockdown, co-IP, in vitro phosphorylation, S31 mutant reconstitution, cell cycle analysis; plus Skap55-/- DC vaccine tumor models for PD-1/NFATc1

    PMID:25851535 PMID:31320682

    Open questions at the time
    • PLK1-scaffolding data from single lab
    • Mechanistic link between adhesion-adaptor and cell-cycle roles unresolved
  13. 2024 Low

    Began dissecting the modular determinants distinguishing SKAP1 from its paralog SKAP2 in Src-kinase binding.

    Evidence Domain dissection and binding comparisons between SKAP1 and SKAP2 modules

    PMID:38483858

    Open questions at the time
    • Low-confidence modular dissection, single lab with limited orthogonal validation
    • Functional consequences of paralog-specific binding not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • How SKAP1's distinct roles — integrin inside-out signaling, Ras-ERK regulation, de-adhesion, PD-1 control, and PLK1-dependent cell cycling — are coordinated within a single T cell remains unresolved.
  • No unified model integrating adhesion and cell-cycle functions
  • Structural basis of PH-domain membrane/lipid engagement undefined
  • Temporal switching between adhesion and de-adhesion complexes unmapped

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0008092 cytoskeletal protein binding 2 GO:0098772 molecular function regulator activity 2
Localization
GO:0005886 plasma membrane 4 GO:0005829 cytosol 2
Pathway
R-HSA-168256 Immune System 4 R-HSA-1474244 Extracellular matrix organization 3 R-HSA-162582 Signal Transduction 3
Partners
FYBFYNGRB2LATPLK1RAP1RAPLRASGRP1
Complex memberships
ADAP-SKAP1 moduleLAT-GRB2-SKAP1 complexSKAP1-RapL-Rap1-LFA-1 complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 SKAP55 (SKAP1) was identified as a novel adaptor protein that constitutively associates with the Src-family kinase p59(fyn) in T-lymphocytes. SKAP55 contains a pleckstrin homology domain, a C-terminal SH3 domain, and tyrosine phosphorylation sites. In vitro binding assays showed SKAP55 selectively binds SH2 domains of Lck, Lyn, Src, and Fyn but not ZAP70, Syk, Shc, SLP-76, Grb2, PI3K, or c-abl. SKAP55 is constitutively tyrosine phosphorylated in resting T-lymphocytes. GST-Fyn-SH2 domain pulldown, molecular cloning, co-immunoprecipitation, in vitro SH2 domain binding assays The Journal of biological chemistry High 9195899
1998 SKAP55 binds FYB (ADAP/SLAP-130) through its SH3 domain and acts as a substrate for FYN kinase in T cells. FYB and SKAP55 colocalize in the perinuclear region of cells. A related protein SKAP55R also binds FYB via its SH3 domain. Yeast two-hybrid screen, co-immunoprecipitation, immunofluorescence confocal microscopy Proceedings of the National Academy of Sciences of the United States of America High 9671755
1998 SKAP55 directly associates with SLAP-130 (ADAP/FYB) in human T-cells. The interaction involves the SH3 domain of SKAP55 and the proline-rich sequence of SLAP-130, as demonstrated by truncation mutants and yeast two-hybrid. Co-immunoprecipitation from T cells, co-expression in COS cells, yeast two-hybrid with truncated mutants The Journal of biological chemistry High 9748251
2000 The SH3 domain of FYN binds a novel proline-independent RKxxYxxY motif in SKAP55. Class I SH3 domains bound this motif while class II domains did not. Two-dimensional NMR of FYN-SH3 bound to the RKGDYASY peptide showed overlap with the proline-rich peptide binding site on the charged surface of the SH3 domain. Alanine scanning confirmed the requirement for the arginine, lysine and tandem tyrosines. Expression of the RKGDYASY peptide inhibited TcRzeta/CD3-mediated NF-AT transcription in T cells. Peptide precipitation, alanine scanning mutagenesis, 2D NMR, in vivo co-expression, NF-AT reporter assay The EMBO journal High 10856234
2002 SKAP55 undergoes TCR-induced translocation from cytoplasm to membrane and to lipid rafts. Upon TCR activation, SKAP55 forms homodimers through its SH3 domain and SK region, interacts with Fyn kinase and Grb-2 (dependent on phosphorylation of Y271), and its stable overexpression activates MAPK following TCR engagement. Co-immunoprecipitation, mutational analysis, subcellular fractionation, MAPK activation assays, stable overexpression The Journal of biological chemistry Medium 12171928
2002 SKAP55 associates with CD45 in T cells via Tyr-232 of SKAP55 (identified by yeast two-hybrid and mutational analysis). Anti-CD3 stimulation promotes SKAP55 tyrosine phosphorylation and membrane translocation. Overexpression of SKAP55 induces IL-2 promoter activation, while SKAP55-Y232F mutant suppresses it and causes Fyn hyperphosphorylation with decreased kinase activity, suggesting SKAP55 couples CD45 with Src kinases for their dephosphorylation and TCR signal activation. Yeast two-hybrid, mutational analysis, in vivo co-expression, IL-2 promoter reporter assay, kinase activity assay Molecular and cellular biology Medium 11909961
2003 SKAP-55 (SKAP1) regulates integrin-mediated adhesion and T cell-APC conjugate formation. SKAP-55 enhances adhesion to fibronectin and ICAM-1, colocalizes with actin at the T cell-APC immunological synapse, and promotes LFA-1 clustering. This function requires the SKAP-55 SH3 domain. SKAP-55 translocates to membrane rafts upon LFA-1 and TCR co-ligation. Overexpression and dominant-negative studies, adhesion assays, confocal microscopy, membrane raft fractionation, co-localization Nature immunology High 12652296
2003 In mast cells, SKAP55 forms an adaptor complex with SLAP-130 and MIST. SLAP-130 requires collaboration with SKAP55 for the recruitment of MIST to Lyn. MIST is preferentially recruited to Fyn (over Lyn) due to higher affinity binding of the SLAP-130/SKAP55 complex to the Fyn-SH2 domain. Co-immunoprecipitation, direct binding assays, affinity comparisons FEBS letters Medium 12681493
2005 SKAP-55 is essential for TCR-mediated 'inside-out signaling' required for LFA-1 clustering and T cell-APC conjugation. siRNA knockdown of SKAP-55 abolished LFA-1 clustering but had no effect on TCR-CD3 clustering. SKAP-55R (SKAP2) cannot substitute for SKAP-55 in this function, indicating a unique non-redundant role. siRNA knockdown, LFA-1 clustering assay, T cell-APC conjugation assay The Journal of experimental medicine High 15939789
2005 SKAP55 protein stability is dependent on ADAP. In ADAP-deficient Jurkat T cells, SKAP55 has a half-life of ~15-20 min (vs ~90 min in the presence of ADAP) due to increased proteolysis. ADAP restores SKAP55 stability 5-fold by decreasing its degradation rate. This protective effect requires the SKAP55 SH3 domain (which mediates SKAP55-ADAP interaction). ADAP-deficient cell line reconstitution, protein stability/pulse-chase analysis, SH3 domain inactivation mutant The Journal of biological chemistry High 15849195
2006 The ADAP/SKAP55 signaling module is involved in TCR-mediated inside-out signaling by recruiting activated Rap1 to the plasma membrane. Disruption of the ADAP/SKAP55 module displaces Rap1 from the plasma membrane without affecting Rap1 GTPase activity. Membrane-targeted ADAP/SKAP55 induces T-cell adhesion in the absence of TCR stimulation. Dominant-negative disruption of ADAP/SKAP55 module, membrane fractionation, Rap1 activity assays, constitutive membrane targeting constructs, adhesion assays Molecular and cellular biology High 16980616
2006 ADAP SH3c domain binds a non-canonical RKxxY294xxY297 motif in SKAP-55. FYN kinase phosphorylates Y294 in vivo, blocking ADAP-SH3c binding. Surface plasmon resonance showed phosphorylation of Y294 mediates dissociation while Y297 phosphorylation had no effect. The Y294F mutation blocked TCR-induced LFA-1-mediated adhesion to ICAM-1 and IL-2 promoter activity. In vivo phosphorylation assays, surface plasmon resonance, mutational analysis (Y294F, Y297F), adhesion assays, IL-2 promoter reporter assay The Journal of biological chemistry High 16461356
2007 SKAP55 co-immunoprecipitates with the Ras activator RasGRP1. Binding requires the C-terminus of SKAP55 and is enhanced by tyrosine phosphorylation of SKAP55. SKAP55 overexpression disrupts TCR-to-Ras-Erk-AP1 signaling, while knockdown decreases ERK phosphorylation and AP-1 activation. Constitutively active Ras or Raf-1 overcomes the inhibitory effect of SKAP55 overexpression. Co-immunoprecipitation, RNAi knockdown, overexpression, AP-1/NF-AT reporter assays, ERK phosphorylation assay, epistasis with constitutively active Ras/Raf Molecular immunology Medium 17658605
2008 SKAP-55 binds RasGRP1 via its C-terminus and negatively regulates the p21(ras)-ERK pathway. SKAP-55-deficient primary T-cells show defective LFA-1 adhesion concurrent with hyper-activation of ERK. Loss of RasGRP1 binding abrogates SKAP-55 inhibition of ERK/ELK. SKAP-55-/- T-cells show increased RasGRP1 presence in the trans-Golgi network following TCR activation. Knockout primary T cells, RNAi knockdown, co-immunoprecipitation, C-terminal deletion mutants, ERK/ELK activation assays, RasGRP1 localization by microscopy PloS one High 18320039
2010 SKAP1 N-terminal domain binds the C-terminal SARAH domain of RapL, forming a SKAP1-RapL-Rap1 complex that binds LFA-1. In Skap1-/- primary T cells, TCR-induced Rap1-RapL complex formation and LFA-1 binding failed to occur. A RapL mutation (L224A) that abrogated SKAP1 binding disrupted component colocalization in vesicles and T cell-DC conjugation. RapL expression slowed T cell motility in lymph nodes, an effect reversed by L224A mutation with reduced dwell times with DCs. Skap1-/- primary T cells, co-immunoprecipitation, RapL mutants, intravital two-photon imaging in lymph nodes, T cell-DC conjugation assay Immunity High 20346707
2011 The PH domain of SKAP1 is required for RapL membrane localization and Rap1-LFA-1 complex formation. A PH domain-inactivating mutation (R131M) markedly impaired RapL translocation to membranes, Rap1 and LFA-1 binding, and LFA-1-ICAM-1 adhesion. N-terminal myristoylated SKAP1 facilitated constitutive RapL membrane and Rap1 binding, effectively substituting for PI3K and TCR ligation in LFA-1 activation. PH domain point mutation (R131M), membrane fractionation, co-immunoprecipitation, constitutive membrane-targeting (myr-SKAP1), LFA-1 adhesion assay, PI3K inhibitor studies The Journal of biological chemistry High 21669874
2011 The SKAP55 PH domain (specifically R131M mutation) determines the ability of the ADAP/SKAP55 module to recruit ADAP to LFA-1 integrin complexes upon TCR stimulation. Association of ADAP with SKAP55 is both sufficient and necessary for rescue of integrin function in ADAP-deficient T cells. The R131M SKAP55 mutant, while unable to restore integrin function, restored NF-κB signaling in ADAP-deficient T cells, indicating that SKAP55 association with ADAP segregates integrin and NF-κB functions of ADAP. SKAP-ADAP chimeric fusion protein, ADAP-deficient T cell reconstitution, PH domain mutation (R131M), LFA-1 co-immunoprecipitation, NF-κB reporter assay, integrin adhesion assay Journal of immunology High 21525391
2011 The ADAP/SKAP55 module regulates CCR7-mediated LFA-1 activation by forming two independent pools: one interacting with a RAPL/Mst1 complex and the other linked to a RIAM/Mst1/Kindlin-3 complex. Both complexes require ADAP/SKAP55 for binding to LFA-1 upon CCR7 stimulation. Loss of the module delays T-cell homing and reduces intranodal motility in vivo. Co-immunoprecipitation, LFA-1 affinity/avidity assays, in vivo homing assays, intravital imaging Blood High 22117043
2013 SKAP55 is required for SLP-76 microcluster persistence and movement, junctional stabilization, and integrin-independent adhesion via the TCR. These functions require SKAP55 dimerization and ADAP interaction. The SKAP55 dimerization motif enables co-immunoprecipitation of RIAM, recruitment of talin into TCR-induced adhesive junctions, and inside-out signaling to β1 integrins. A tandem dimer with two ADAP-binding SKAP55 SH3 domains stabilized SLP-76 microclusters but could not support adhesion to integrin ligands. Fluorescence microscopy of SLP-76 microclusters, SKAP55 dimerization domain mutants, tandem dimer constructs, co-immunoprecipitation of RIAM and talin, integrin adhesion assays The Journal of cell biology High 24368808
2015 The ADAP-SKAP55 signaling module promotes PD-1 expression on CD8+ T cells in a Fyn-, Ca2+-, and NFATc1-dependent manner. Knockout of SKAP55 or ADAP reduced PD-1 expression on CD8+ effector cells and enhanced anti-tumor immunity in DC vaccine models. NFATc1 inhibitor CsA also downregulated PD-1, consistent with SKAP55 acting upstream of NFATc1. Skap55-/- and Adap-/- knockout mice, DC vaccine tumor models, adoptive T cell transfer, NFATc1 inhibitor (CsA), flow cytometry for PD-1/CTLA-4/Treg EMBO molecular medicine High 25851535
2016 SKAP1-deficient T cells show reduced translocation of talin and RIAM to the T cell-APC contact interface. Skap1-/- T cells show an altered pattern of talin cleavage (by calpain). Expression of a calpain-cleavage-resistant talin mutant (L432G) rescued the impaired adhesion of Skap1-/- T cells with DCs. Skap1-/- T cells, confocal microscopy of contact interface, talin/RIAM localization, talin cleavage assay, non-cleavable talin (L432G) reconstitution, T cell-DC conjugation assay Immunology letters Medium 26905930
2017 LFA-1 cross-linking activates FAK1/PYK2 which phosphorylate LAT selectively on Y171, leading to formation of LAT-GRB2-SKAP1 complexes distinct from canonical LAT-GADs-SLP-76 complexes. LFA-1 cross-linking increased LAT-GRB2-SKAP1 relative to LAT-GADs-SLP-76 complexes and decreased T cell-DC dwell times dependent on LAT-Y171, reducing T cell binding to DCs and proliferation. Co-immunoprecipitation, LAT Y171 mutant, FAK1/PYK2 activation assays, T cell-DC dwell time analysis, T cell proliferation assay Nature communications High 28699640
2017 Within the SKAP55 PH domain, D120 facilitates cytoplasmic retention of SKAP55 in non-stimulated T cells, while K152 promotes membrane recruitment via actin binding upon TCR triggering. K152-dependent PH domain interaction with actin promotes talin binding to LFA-1, facilitating LFA-1 activation. PH domain point mutations (D120, K152), subcellular fractionation, actin co-immunoprecipitation, talin-LFA-1 binding assay, LFA-1 activation assay Molecular and cellular biology Medium 28052935
2018 SKAP1 forms homodimers mediated by residues A17 to L21 in the N-terminal region. SKAP1 dimerization is not required for its binding to RapL. Co-immunoprecipitation of truncation/deletion mutants, N-terminal deletion mapping BMC research notes Medium 30522503
2019 SKAP1 is phosphorylated by and binds to PLK1 at N-terminal serine 31 (S31). This interaction is needed for optimal PLK1 kinase activity. siRNA knockdown of SKAP1 reduced T-cell division and delayed expression of PLK1, Cyclin A and pH3. Reconstitution with WT SKAP1 but not the S31 mutant restored normal cell division. SKAP1-PLK1 binding is dynamically regulated during the T-cell cycle. siRNA knockdown, co-immunoprecipitation, in vitro phosphorylation assay, S31 point mutation reconstitution, cell cycle analysis (Cyclin A, pH3, PLK1 expression) Scientific reports Medium 31320682
2024 Two modules control SKAP1 interaction with SRC kinases: one composed of two conserved motifs in the second interdomain that interact with the SH2 domain of SRC kinases, and a second module composed of the DIM (dimerization) domain modulated by the SH3 domain and SRC kinase activation state. These binding properties differ between SKAP1 and its paralog SKAP2. Domain dissection/truncation analysis, binding comparisons between SKAP1 and SKAP2 modules PloS one Low 38483858

Source papers

Stage 0 corpus · 40 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55. The EMBO journal 133 10856234
1998 FYB (FYN binding protein) serves as a binding partner for lymphoid protein and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells. Proceedings of the National Academy of Sciences of the United States of America 117 9671755
2006 The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1. Molecular and cellular biology 104 16980616
2010 T cell receptor "inside-out" pathway via signaling module SKAP1-RapL regulates T cell motility and interactions in lymph nodes. Immunity 94 20346707
2003 SKAP-55 regulates integrin adhesion and formation of T cell-APC conjugates. Nature immunology 94 12652296
1997 Molecular cloning of SKAP55, a novel protein that associates with the protein tyrosine kinase p59fyn in human T-lymphocytes. The Journal of biological chemistry 91 9195899
1998 Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130. The Journal of biological chemistry 83 9748251
2008 SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesion. Trends in cell biology 81 18760924
1998 SKAP-HOM, a novel adaptor protein homologous to the FYN-associated protein SKAP55. FEBS letters 74 9755858
2011 CCR7-mediated LFA-1 functions in T cells are regulated by 2 independent ADAP/SKAP55 modules. Blood 63 22117043
2015 ADAP and SKAP55 deficiency suppresses PD-1 expression in CD8+ cytotoxic T lymphocytes for enhanced anti-tumor immunotherapy. EMBO molecular medicine 53 25851535
2005 An essential role for SKAP-55 in LFA-1 clustering on T cells that cannot be substituted by SKAP-55R. The Journal of experimental medicine 48 15939789
2005 Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells. The Journal of biological chemistry 46 15849195
2011 SKAP1 protein PH domain determines RapL membrane localization and Rap1 protein complex formation for T cell receptor (TCR) activation of LFA-1. The Journal of biological chemistry 35 21669874
2017 LFA-1 activates focal adhesion kinases FAK1/PYK2 to generate LAT-GRB2-SKAP1 complexes that terminate T-cell conjugate formation. Nature communications 31 28699640
2021 The Multiple Roles of the Cytosolic Adapter Proteins ADAP, SKAP1 and SKAP2 for TCR/CD3 -Mediated Signaling Events. Frontiers in immunology 28 34295339
2002 SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription. Molecular and cellular biology 28 11909961
2006 Regulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor protein. The Journal of biological chemistry 26 16461356
2019 Immune adaptor SKAP1 acts a scaffold for Polo-like kinase 1 (PLK1) for the optimal cell cycling of T-cells. Scientific reports 25 31320682
2024 SKAP1 Expression in Cancer Cells Enhances Colon Tumor Growth and Impairs Cytotoxic Immunity by Promoting Neutrophil Extracellular Trap Formation via the NFATc1/CXCL8 Axis. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 24 39269257
2007 SKAP55 modulates T cell antigen receptor-induced activation of the Ras-Erk-AP1 pathway by binding RasGRP1. Molecular immunology 23 17658605
2002 SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation. The Journal of biological chemistry 22 12171928
2023 Multi-functional adaptor SKAP1: regulator of integrin activation, the stop-signal, and the proliferation of T cells. Frontiers in immunology 20 37325633
2003 Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 adaptor complex in mast cells. FEBS letters 20 12681493
2013 The N terminus of SKAP55 enables T cell adhesion to TCR and integrin ligands via distinct mechanisms. The Journal of cell biology 18 24368808
2011 The pleckstrin homology domain in the SKAP55 adapter protein defines the ability of the adapter protein ADAP to regulate integrin function and NF-kappaB activation. Journal of immunology (Baltimore, Md. : 1950) 18 21525391
2016 T-cell immune adaptor SKAP1 regulates the induction of collagen-induced arthritis in mice. Immunology letters 15 27181093
2008 Adaptor SKAP-55 binds p21 activating exchange factor RasGRP1 and negatively regulates the p21-ERK pathway in T-cells. PloS one 15 18320039
2013 Multistage T cell-dendritic cell interactions control optimal CD4 T cell activation through the ADAP-SKAP55-signaling module. Journal of immunology (Baltimore, Md. : 1950) 12 23918975
2022 THUMPD3-AS1 facilitates cell growth and aggressiveness by the miR-218-5p/SKAP1 axis in colorectal cancer. Cell biochemistry and biophysics 11 35538197
2023 SKAP1 Is a Novel Biomarker and Therapeutic Target for Gastric Cancer: Evidence from Expression, Functional, and Bioinformatic Analyses. International journal of molecular sciences 10 37511629
2017 D120 and K152 within the PH Domain of T Cell Adapter SKAP55 Regulate Plasma Membrane Targeting of SKAP55 and LFA-1 Affinity Modulation in Human T Lymphocytes. Molecular and cellular biology 10 28052935
2018 Immune adaptor protein SKAP1 (SKAP-55) forms homodimers as mediated by the N-terminal region. BMC research notes 8 30522503
2009 SKAP1 is dispensable for chemokine-induced migration of primary T-cells. Immunology letters 8 19883688
2016 Non-cleavable talin rescues defect in the T-cell conjugation of T-cells deficient in the immune adaptor SKAP1. Immunology letters 7 26905930
2023 Splicing annotation of endometrial cancer GWAS risk loci reveals potentially causal variants and supports a role for NF1 and SKAP1 as susceptibility genes. HGG advances 5 36908940
2022 Two independent cis-acting elements are required for the guard cell-specific expression of SCAP1, which is essential for late stomatal development. The Plant journal : for cell and molecular biology 2 35061307
2018 Complete Genome Sequences of Six BI Cluster Streptomyces Bacteriophages, HotFries, Moozy, Rainydai, RavenPuff, Scap1, and SenditCS. Microbiology resource announcements 2 30533665
2024 Role of two modules controlling the interaction between SKAP1 and SRC kinases comparison with SKAP2 architecture and consequences for evolution. PloS one 1 38483858
2026 HIV immunological non-responders show low SKAP1 concentration and DNA hypermethylation in the SKAP1 promotor region: Low Skap1 in HIV Immunological Non-Responders. AIDS (London, England) 0 42013451

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