Affinage

SKAP1

Src kinase-associated phosphoprotein 1 · UniProt Q86WV1

Length
359 aa
Mass
41.4 kDa
Annotated
2026-04-28
41 papers in source corpus 26 papers cited in narrative 26 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SKAP1 (SKAP55) is a T cell-specific adaptor protein that orchestrates TCR-mediated inside-out signaling to integrins, coupling antigen receptor engagement to cell adhesion, de-adhesion, and immune synapse formation. SKAP1 constitutively binds ADAP via its SH3 domain, which stabilizes SKAP1 protein levels and enables plasma membrane recruitment; its PH domain senses PI3K-generated lipids (through residues R131, D120, K152) and recruits the RapL–Rap1 complex to the membrane, driving LFA-1 clustering and T cell–APC conjugation (PMID:15939789, PMID:21669874, PMID:20346707, PMID:15849195). Beyond integrin activation, SKAP1 negatively regulates the Ras–ERK pathway by sequestering RasGRP1 away from the trans-Golgi network, promotes PD-1 expression through a Fyn–Ca²⁺–NFATc1 axis relevant to anti-tumor immunity, and scaffolds PLK1 at N-terminal S31 to optimize T cell division (PMID:18320039, PMID:25851535, PMID:31320682). A distinct LFA-1-triggered signaling arm uses FAK1/PYK2-phosphorylated LAT-Y171 and GRB2 to recruit SKAP1 into complexes that mediate de-adhesion and modulate T cell–DC dwell times (PMID:28699640).

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1997 High

    Identification of SKAP55 as a Fyn-SH2-binding substrate in T cells established it as a novel PH- and SH3-domain-containing signaling adaptor downstream of Src-family kinases.

    Evidence GST-SH2 pulldowns and molecular cloning from human T lymphocytes

    PMID:9195899

    Open questions at the time
    • No known function or downstream partners beyond Src-family kinase binding
    • Physiological role of PH and SH3 domains unknown
  2. 1998 High

    Discovery of the constitutive SKAP55–ADAP (SLAP-130/FYB) interaction via the SH3 domain defined SKAP1 as part of a stable adaptor module, raising the question of what this module does in TCR signaling.

    Evidence Yeast two-hybrid, co-IP in COS cells, truncation mutants, confocal colocalization

    PMID:9671755 PMID:9748251

    Open questions at the time
    • Functional consequence of the SKAP55–ADAP module unknown
    • How the module is regulated by TCR stimulation unclear
  3. 2000 High

    Structural characterization of a non-canonical RKxxYxxY motif in SKAP55 bound by the Fyn SH3 domain, with functional inhibition of NF-AT transcription, showed that Fyn engagement of SKAP55 uses an atypical mechanism with signaling consequences.

    Evidence 2D NMR of Fyn-SH3 with RKGDYASY peptide, alanine scanning, NF-AT reporter in T cells

    PMID:10856234

    Open questions at the time
    • Relationship between Fyn-SH3 binding and integrin signaling not yet explored
    • Whether phosphorylation of the RKxxYxxY motif regulates binding in vivo unknown
  4. 2002 Medium

    Demonstration that SKAP55 translocates to lipid rafts upon TCR ligation and interacts with CD45 and Grb2 positioned it as a signal-responsive scaffold linking proximal TCR machinery to downstream effectors.

    Evidence Co-IP, lipid raft fractionation, Y232F and Y271 mutagenesis, IL-2 and MAPK reporter assays in Jurkat cells

    PMID:11909961 PMID:12171928

    Open questions at the time
    • Overexpression-based system; endogenous stoichiometry not confirmed
    • Direct connection to integrin activation not yet established
  5. 2003 High

    SKAP55 was shown to be essential for TCR-induced LFA-1 clustering and T cell–APC conjugate formation, establishing integrin inside-out signaling as its primary biological function.

    Evidence Overexpression/SH3-deletion mutants, adhesion assays to ICAM-1/fibronectin, confocal at immune synapse

    PMID:12652296

    Open questions at the time
    • Mechanism connecting SKAP55 to LFA-1 activation unknown
    • Loss-of-function (KD/KO) confirmation pending
  6. 2005 High

    siRNA knockdown confirmed a non-redundant requirement for SKAP55 (not compensated by SKAP55R) in inside-out LFA-1 signaling, and ADAP was shown to stabilize SKAP55 protein, explaining why ADAP deficiency phenocopies SKAP55 loss.

    Evidence siRNA in T cells with LFA-1 clustering readouts; pulse-chase in ADAP-deficient Jurkat cells

    PMID:15849195 PMID:15939789

    Open questions at the time
    • Downstream effectors linking SKAP55 to LFA-1 still unidentified
    • Whether SKAP55 degradation is proteasome-dependent not resolved
  7. 2006 High

    The ADAP/SKAP55 module was shown to be required for membrane retention of activated Rap1, and Fyn phosphorylation of Tyr-294 in SKAP55 was found to regulate ADAP-SH3c binding, linking kinase input to integrin signaling output.

    Evidence Rap1 membrane localization in module-disrupted cells; SPR for pY294 disruption of ADAP binding; Y294F mutant blocks LFA-1 adhesion

    PMID:16461356 PMID:16980616

    Open questions at the time
    • Identity of the Rap1 effector bridging SKAP55 to LFA-1 unknown
    • Role of dimerization in Rap1 membrane retention unclear
  8. 2008 Medium

    SKAP55 was found to negatively regulate Ras–ERK signaling by binding and sequestering RasGRP1 away from the trans-Golgi network, revealing a second major signaling axis beyond integrin regulation.

    Evidence Skap1−/− primary T cells showing ERK hyperactivation and increased TGN-localized RasGRP1; co-IP with C-terminal mapping

    PMID:17658605 PMID:18320039

    Open questions at the time
    • Whether RasGRP1 sequestration operates simultaneously with integrin signaling unclear
    • Structural basis of SKAP55–RasGRP1 interaction unresolved
  9. 2010 High

    Identification of the SKAP1–RapL–Rap1 ternary complex that directly binds LFA-1, with in vivo validation by two-photon imaging showing reduced T cell dwell times in Skap1−/− lymph nodes, provided the molecular bridge between SKAP1 and integrin activation.

    Evidence Skap1−/− primary T cells, RapL-L224A point mutant, co-IP, intravital two-photon imaging in lymph nodes

    PMID:20346707

    Open questions at the time
    • How PH domain lipid sensing drives RapL recruitment mechanistically not yet resolved
    • Contribution of RIAM-containing complexes versus RapL complexes not delineated
  10. 2011 High

    The PH domain of SKAP1 (R131) was shown to mediate PI3K-dependent membrane targeting that recruits RapL, and two distinct ADAP/SKAP55 pools (RapL/Mst1 and RIAM/Kindlin-3/Mst1) were identified as parallel arms controlling LFA-1 affinity and avidity.

    Evidence R131M mutant, PI3K inhibitor, myristoylated SKAP1 rescue; co-IP of two pools with CCR7 stimulation and in vivo homing

    PMID:21525391 PMID:21669874 PMID:22117043

    Open questions at the time
    • Whether both pools operate simultaneously at the same synapse unknown
    • Lipid species specificity of PH domain not defined
  11. 2013 High

    SKAP55 dimerization via the N-terminal region was shown to enable RIAM co-immunoprecipitation, talin recruitment, and SLP-76 microcluster persistence, integrating SKAP55 oligomerization with the spatiotemporal dynamics of TCR signaling complexes.

    Evidence Engineered tandem dimer constructs, TIRF/timelapse imaging of SLP-76 microclusters, integrin assays

    PMID:24368808

    Open questions at the time
    • Stoichiometry of dimers versus monomers in resting versus activated T cells unknown
    • Crystal/cryo-EM structure of SKAP55 dimer absent
  12. 2015 Medium

    SKAP55 was discovered to promote PD-1 expression via a Fyn–Ca²⁺–NFATc1 pathway, and Skap55−/− CD8+ CTLs showed enhanced anti-tumor activity, revealing a role beyond adhesion in immune checkpoint regulation.

    Evidence Skap55−/− and Adap−/− mice, DC-vaccine tumor models, adoptive transfer, CsA inhibition, PD-1 flow cytometry

    PMID:25851535

    Open questions at the time
    • Whether SKAP55 directly regulates NFATc1 nuclear translocation or acts indirectly unresolved
    • Mechanism independent of ADAP not excluded
    • Generalizability to human tumors not tested
  13. 2017 High

    A distinct LFA-1-triggered de-adhesion pathway was mapped: LFA-1 cross-linking activates FAK1/PYK2, which phosphorylates LAT-Y171 to recruit GRB2–SKAP1 complexes that shorten T cell–DC dwell times, separating adhesion-promoting and de-adhesion functions of SKAP1.

    Evidence Co-IP, kinase assay, LAT-Y171 mutant, T cell–DC dwell time imaging, proliferation assay

    PMID:28699640

    Open questions at the time
    • Downstream effector of LAT-GRB2-SKAP1 in de-adhesion not identified
    • Whether this pathway intersects with RapL-dependent adhesion signaling unclear
  14. 2019 Medium

    SKAP1 was identified as a PLK1 scaffold phosphorylated at S31, required for optimal PLK1 kinase activity and timely T cell division, extending SKAP1 function beyond adhesion into cell cycle regulation.

    Evidence PLK1 kinase assay, S31 mutant rescue of siRNA knockdown, cell cycle marker analysis

    PMID:31320682

    Open questions at the time
    • Whether PLK1 scaffolding is T cell-specific or generalizable unknown
    • How TCR signaling connects to S31 phosphorylation timing unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • A structural model of full-length SKAP1 (including the dimer interface, PH domain lipid contacts, and SH3-mediated interactions) is lacking, and the mechanism by which SKAP1 coordinates its multiple signaling outputs — integrin activation, Ras–ERK suppression, PD-1 regulation, and cell cycle control — in space and time remains unresolved.
  • No crystal or cryo-EM structure of SKAP1 alone or in complex
  • Spatiotemporal coordination of SKAP1 signaling pools at the immune synapse undefined
  • In vivo phenotype of SKAP1 point mutants (e.g., R131M, S31A) in mice not reported

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0008289 lipid binding 2
Localization
GO:0005886 plasma membrane 5 GO:0005829 cytosol 2
Pathway
GO:0098631 cell adhesion mediator activity 5 R-HSA-168256 Immune System 5 R-HSA-162582 Signal Transduction 4 R-HSA-1640170 Cell Cycle 1
Partners
ADAPFYNGRB2PLK1RAP1RAPLRASGPR1RIAM
Complex memberships
ADAP/SKAP55 moduleADAP/SKAP55-RIAM-Kindlin-3-Mst1 complexSKAP1-RapL-Rap1 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 substrate that associates with p59fyn in human T-lymphocytes via its SH2 domain, and selectively binds to isolated SH2 domains of Lck, Lyn, Src, and Fyn but not ZAP70, Syk, Shc, SLP-76, Grb2, PI3K, or c-abl in vitro. The protein contains a pleckstrin homology domain, a C-terminal SH3 domain, and several potential tyrosine phosphorylation sites. GST-SH2 domain pulldown, molecular cloning, in vitro binding assays The Journal of biological chemistry High 9195899
1998 SKAP55 (SKAP1) binds directly to SLAP-130 (ADAP/FYB) via the SH3 domain of SKAP55 and the proline-rich sequence of SLAP-130, as demonstrated by co-immunoprecipitation, co-expression in COS cells, and two-hybrid analysis. Two-hybrid screen, co-expression/co-IP in COS cells, truncation mutants The Journal of biological chemistry High 9671755 9748251
1998 FYB (ADAP/SLAP-130) serves as a binding partner for SKAP55 (SKAP1) in T cells; both proteins colocalize in the perinuclear region and SKAP55 acts as a substrate for FYN kinase. The interaction is mediated through the SH3 domain of SKAP55. Two-hybrid screen with FYB as bait, immunofluorescence confocal microscopy, kinase assay Proceedings of the National Academy of Sciences of the United States of America High 9671755
2000 The SH3 domain of FYN binds to a novel proline-independent RKxxYxxY motif in SKAP55 (SKAP1). This non-canonical motif binding overlaps with the proline-based binding site on the charged surface of the SH3 domain. Expression of the RKGDYASY peptide inhibited TcRzeta/CD3-mediated NF-AT transcription in T cells. Peptide precipitation, alanine scanning, 2D NMR of FYN-SH3 with bound peptide, in vivo co-expression The EMBO journal High 10856234
2002 SKAP55 (SKAP1) is phosphorylated at Tyr-232 and associates with CD45 in vivo; anti-CD3 stimulation promotes SKAP55 tyrosine phosphorylation and translocation from cytoplasm to membrane. SKAP55 couples CD45 with Src family kinases, positively regulating TCR-mediated IL-2 promoter transcriptional activation. Yeast two-hybrid, mutational analysis (Y232F), overexpression in Jurkat, IL-2 promoter reporter assay Molecular and cellular biology Medium 11909961
2002 SKAP55 (SKAP1) forms homodimers through its SH3 domain and SK region, translocates to lipid rafts upon TCR activation, and interacts with Fyn kinase and Grb-2 at Tyr-271. Overexpression of SKAP55 in Jurkat cells activates MAPK following TCR engagement. Co-immunoprecipitation, mutational analysis, stable overexpression, lipid raft fractionation The Journal of biological chemistry Medium 12171928
2003 SKAP55 (SKAP1) regulates LFA-1-mediated adhesion and T cell-APC conjugate formation. SKAP55 colocalizes with actin at the T cell-APC synapse and promotes LFA-1 clustering. Conjugate formation requires the SKAP-55 SH3 domain and is accompanied by translocation of SKAP-55 to membrane rafts regulated by both LFA-1 and TCR ligation. Overexpression, adhesion assays (fibronectin/ICAM-1), confocal microscopy, lipid raft fractionation, SH3 deletion mutants Nature immunology High 12652296
2003 In mast cells, SKAP55 (SKAP1) forms a complex with SLAP-130 and MIST; collaboration of SLAP-130 with SKAP55 recruits MIST to Fyn rather than Lyn, regulated by higher affinity binding of SLAP-130/SKAP55 to the Fyn-SH2 domain compared to the Lyn-SH2 domain. Co-immunoprecipitation, direct binding assays, affinity comparison FEBS letters Medium 12681493
2005 siRNA knockdown of SKAP-55 (SKAP1) identified an essential role for this adaptor in TCR-mediated inside-out signaling for LFA-1 clustering and T cell-APC conjugation, distinct from TCR-CD3 clustering. SKAP-55R cannot compensate for loss of SKAP-55 in LFA-1 clustering. siRNA knockdown, LFA-1 clustering assay, conjugation assay The Journal of experimental medicine High 15939789
2005 SKAP55 (SKAP1) protein is rapidly degraded (half-life ~15-20 min) in the absence of ADAP, and ADAP stabilizes SKAP55 by causing a 5-fold decrease in its proteolysis rate. This stabilization requires the SH3 domain-mediated SKAP55-ADAP interaction. ADAP-deficient Jurkat cell line, protein stability/pulse-chase analysis, SH3 domain inactivation, restoration of ADAP expression The Journal of biological chemistry High 15849195
2006 The ADAP/SKAP55 signaling module is required for TCR-mediated inside-out signaling; disruption of ADAP/SKAP55 interaction displaces activated Rap1 from the plasma membrane without affecting its GTPase activity. Membrane targeting of the ADAP/SKAP55 module induces T-cell adhesion in the absence of TCR stimulation. Module disruption experiments, Rap1 membrane localization assay, constitutive membrane targeting constructs Molecular and cellular biology High 16980616
2006 Fyn kinase phosphorylates Tyr-294 in the RKXXY294XXY297 motif of SKAP-55 (SKAP1), blocking the ADAP C-terminal SH3 domain binding to this motif (confirmed by plasmon resonance). Phosphorylation of Tyr-294 (but not Tyr-297) disrupts ADAP-SH3c binding, and Y294F mutation blocks TCR-induced LFA-1-mediated adhesion to ICAM-1 and IL-2 promoter activity. In vivo phosphorylation by Fyn, plasmon resonance interaction analysis, Y294F and Y297F mutants, LFA-1 adhesion assay, IL-2 promoter reporter The Journal of biological chemistry High 16461356
2007 SKAP55 (SKAP1) co-immunoprecipitates with RasGRP1, the Ras guanine nucleotide exchange factor. Binding requires the C-terminus of SKAP55 and is enhanced by tyrosine phosphorylation. Overexpression of SKAP55 disrupts TCR-to-Ras-Erk-AP1 signaling and IL-2 gene transcription, while knockdown decreases AP-1 reporter activity and ERK phosphorylation. Co-immunoprecipitation, RNAi knockdown, overexpression, reporter gene assay, ERK phosphorylation assay Molecular immunology Medium 17658605
2008 SKAP-55 (SKAP1) binds to RasGRP1 via its C-terminus and negatively regulates the p21ras-ERK pathway. SKAP-55 deficient primary T-cells show hyper-activation of ERK and increased RasGRP1 in the trans-Golgi network (where p21ras is activated), indicating SKAP-55 restricts RasGRP1 availability at the TGN. Skap1-/- primary T-cells, ERK phosphorylation assay, RasGRP1 localization by microscopy, C-terminal binding mutant, RNAi knockdown in T-cell lines PloS one Medium 18320039
2010 SKAP1 (SKAP-55) N-terminal domain binds the C-terminal SARAH domain of RapL to form a SKAP1-RapL-Rap1 complex that binds LFA-1. In Skap1-/- primary T-cells, TCR-induced Rap1-RapL complex formation and LFA-1 binding are absent. A RapL mutation (L224A) that abrogates SKAP1 binding disrupts vesicular colocalization and T cell-DC conjugation, and reduces T cell dwell times with DCs in lymph nodes. Skap1-/- primary T-cells, co-IP, RapL point mutation (L224A), two-photon intravital imaging in lymph nodes, conjugation assays Immunity High 20346707
2011 The PH domain of SKAP1 (specifically residue R131) is required for RapL translocation to plasma membranes and subsequent Rap1 and LFA-1 binding. PI3K pathway-dependent membrane targeting of SKAP1 via its PH domain enables RapL membrane recruitment. N-terminal myristoylated SKAP1 constitutively recruits RapL to membranes and activates LFA-1 without TCR ligation. PH domain R131M mutation, membrane fractionation, LFA-1/ICAM-1 binding assay, myr-tagged SKAP1 rescue, PI3K inhibitor The Journal of biological chemistry High 21669874
2011 Physical association of SKAP55 (SKAP1) with ADAP, through the PH domain of SKAP55 (residue R131), recruits ADAP to LFA-1 integrin complexes after TCR stimulation and is necessary and sufficient for integrin function rescue in ADAP-deficient T-cells. This SKAP55-ADAP association restricts ADAP's ability to interact with the NF-κB signalosome (CARMA1/TAK1), defining distinct functional pools. SKAP-ADAP chimeric fusion protein, R131M PH domain mutant, integrin activation assays, NF-κB reporter, LFA-1 co-IP in ADAP-/- T cells Journal of immunology High 21525391
2011 Two independent pools of the ADAP/SKAP55 module exist in T cells: one interacting with a RAPL/Mst1 complex and another linked to a RIAM/Mst1/Kindlin-3 complex; both complexes require ADAP/SKAP55 for binding to LFA-1 upon CCR7 stimulation, regulating both affinity and avidity of LFA-1. Co-immunoprecipitation, CCR7-stimulated adhesion assays, ADAP/SKAP55 module loss-of-function, in vivo homing assays Blood Medium 22117043
2013 SKAP55 (SKAP1) dimerizes via its N-terminal region and the dimerization enables coimmunoprecipitation of RIAM, talin recruitment into TCR-induced adhesive junctions, and inside-out signaling to β1 integrins. SKAP55 dimerization and ADAP binding together are required for SLP-76 microcluster persistence and movement. Tandem dimer constructs, co-IP, timelapse/TIRF microscopy of SLP-76 microclusters, integrin signaling assays The Journal of cell biology High 24368808
2015 The ADAP-SKAP55 signaling module promotes PD-1 expression on CD8+ CTLs in a Fyn-, Ca2+-, and NFATc1-dependent manner. SKAP55 or ADAP knockout reduces PD-1 expression and enhances anti-tumor CTL activity. Adoptive transfer of SKAP55-deficient CD8+ CTLs blocks tumor growth. Skap55-/- and Adap-/- mice, DC vaccine tumor models, adoptive transfer, NFATc1 inhibitor (CsA), flow cytometry for PD-1 EMBO molecular medicine Medium 25851535
2016 Skap1-/- T-cells show reduced translocation of talin and RIAM to the T cell-DC contact interface, and an altered pattern of talin cleavage. Expression of a calpain cleavage-resistant talin (L432G) restored impaired adhesion of Skap1-/- T-cells with DCs, demonstrating SKAP1 affects talin function at the LFA-1 activation interface. Skap1-/- T cells, confocal imaging of talin/RIAM translocation, calpain-resistant talin rescue, T cell-DC conjugation assay Immunology letters Medium 26905930
2017 LFA-1 cross-linking activates FAK1/PYK2, which phosphorylates LAT at Y171 to enable binding of the GRB2-SKAP1 adaptor complex. These LAT-GRB2-SKAP1 complexes are distinct from canonical LAT-GADs-SLP-76 complexes and mediate LFA-1-induced de-adhesion/decreased T cell-DC dwell times. LAT-Y171 mutation reduced T cell-DC binding and proliferation. Co-IP, kinase assay, LAT-Y171 point mutation, T cell-DC dwell time imaging, DO11.10 T cell proliferation assay Nature communications High 28699640
2017 Within the PH domain of SKAP55 (SKAP1), residue D120 retains SKAP55 in the cytoplasm of resting T cells, while K152 promotes membrane recruitment via actin binding upon TCR triggering. K152-dependent actin interaction promotes talin binding to LFA-1, facilitating LFA-1 affinity modulation. Point mutations D120 and K152, subcellular localization assays, actin binding assay, talin co-IP, LFA-1 affinity assay Molecular and cellular biology Medium 28052935
2018 SKAP1 forms homodimers mediated by residues A17 to L21 in its N-terminal region. SKAP1 homodimer formation is not required for RapL binding. Co-IP of truncation/deletion mutants, N-terminal region mapping BMC research notes Medium 30522503
2019 SKAP1 is phosphorylated by PLK1 and binds PLK1 at its N-terminal serine 31 (S31); this interaction is required for optimal PLK1 kinase activity. siRNA knockdown of SKAP1 reduces the rate of T-cell division and delays expression of PLK1, Cyclin A, and pH3. Reconstitution with WT SKAP1 but not SKAP1-S31 mutant restores normal cell division. Co-IP, PLK1 kinase assay, siRNA knockdown, S31 point mutant rescue, cell cycle marker analysis Scientific reports Medium 31320682
2024 Two SKAP1 modules control interaction with SRC kinases: one composed of motifs in the second interdomain interacting with the SH2 domain of SRC kinases, and another composed of the DIM domain modulated by the SH3 domain and SRC kinase activation status. Modular dissection with deletion constructs, comparison with SKAP2, binding assays PloS one Low 38483858

Source papers

Stage 0 corpus · 41 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
2013 A Dof transcription factor, SCAP1, is essential for the development of functional stomata in Arabidopsis. Current biology : CB 104 23453954
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 80 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 51 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
2002 SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription. Molecular and cellular biology 28 11909961
2021 The Multiple Roles of the Cytosolic Adapter Proteins ADAP, SKAP1 and SKAP2 for TCR/CD3 -Mediated Signaling Events. Frontiers in immunology 26 34295339
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
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
2003 Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 adaptor complex in mast cells. FEBS letters 20 12681493
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) 19 39269257
2023 Multi-functional adaptor SKAP1: regulator of integrin activation, the stop-signal, and the proliferation of T cells. Frontiers in immunology 18 37325633
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
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
2023 SKAP1 Is a Novel Biomarker and Therapeutic Target for Gastric Cancer: Evidence from Expression, Functional, and Bioinformatic Analyses. International journal of molecular sciences 9 37511629
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