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Src kinase associated phosphoprotein 1

SKAP55, pp55, Src kinase-associated phosphoprotein of 55 kDa
This gene encodes a T cell adaptor protein, a class of intracellular molecules with modular domains capable of recruiting additional proteins but that exhibit no intrinsic enzymatic activity. The encoded protein contains a unique N-terminal region followed by a PH domain and C-terminal SH3 domain. Along with the adhesion and degranulation-promoting adaptor protein, the encoded protein plays a critical role in inside-out signaling by coupling T-cell antigen receptor stimulation to the activation of integrins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Fyb, Src, CD11b, alpha-Synuclein, V1a
Papers on SKAP55
ADAP and SKAP55 deficiency suppresses PD-1 expression in CD8+ cytotoxic T lymphocytes for enhanced anti-tumor immunotherapy.
Wang et al., Shanghai, China. In Embo Mol Med, Jun 2015
In this study, we have identified that the ADAP-SKAP55 signaling module reduced CD8(+) CTL cytotoxicity and enhanced PD-1 expression in a Fyn-, Ca(2+)-, and NFATc1-dependent manner.
Intracellular TCR-signaling pathway: novel markers for lymphoma diagnosis and potential therapeutic targets.
Marafioti et al., London, United Kingdom. In Am J Surg Pathol, 2014
With this background, we evaluated the expression of 5 intracellular proteins-GADS, DOK2, SKAP55, ITK, and PKCα-involved in T-cell receptor signaling in normal and neoplastic hematologic tissue samples, using antibodies raised against fixation-resistant epitopes of the 5 molecules.
The N terminus of SKAP55 enables T cell adhesion to TCR and integrin ligands via distinct mechanisms.
Bunnell et al., Boston, United States. In J Cell Biol, 2014
In addition to regulating integrin activation, we show that Src kinase-associated phosphoprotein of 55 kD (SKAP55) is required for microcluster persistence and movement, junctional stabilization, and integrin-independent adhesion via the TCR.
Multistage T cell-dendritic cell interactions control optimal CD4 T cell activation through the ADAP-SKAP55-signaling module.
Shimizu et al., Minneapolis, United States. In J Immunol, 2013
Regulation of multistage contact behaviors and optimal T cell signaling involves the interaction of ADAP with the adapter src kinase-associated phosphoprotein of 55 kDa (SKAP55).
ADAP regulates cell cycle progression of T cells via control of cyclin E and Cdk2 expression through two distinct CARMA1-dependent signaling pathways.
Shimizu et al., Minneapolis, United States. In Mol Cell Biol, 2012
Adhesion and degranulation-promoting adapter protein (ADAP) is a multifunctional scaffold that regulates T cell receptor-mediated activation of integrins via association with the SKAP55 adapter and the NF-κB pathway through interactions with both the CARMA1 adapter and serine/threonine kinase transforming growth factor β-activated kinase 1 (TAK1).
Integrin signalling and function in immune cells.
Wang et al., Shanghai, China. In Immunology, 2012
This review discusses the key signalling complexes regulating integrin activation and function in both 'inside-out' and 'outside-in' pathways in T lymphocytes, including kinases, SLP-76, VAV1, ADAP, SKAP-55, RapL, RIAM, Rap1, Talin and Kindlin.
Genetic polymorphisms in androgen receptor-binding sites predict survival in prostate cancer patients receiving androgen-deprivation therapy.
Bao et al., Kao-hsiung, Taiwan. In Ann Oncol, 2012
single-nucleotide polymorphisms in ARRDC3, FLT1, and SKAP1 were significant predictors for survival androgen-deprivation therapy in prostate cancer patients.
CCR7-mediated LFA-1 functions in T cells are regulated by 2 independent ADAP/SKAP55 modules.
Schraven et al., Magdeburg, Germany. In Blood, 2012
Here, we have assessed the role of the ADAP/SKAP55 module for CCR7-mediated signaling.
SKAP1 protein PH domain determines RapL membrane localization and Rap1 protein complex formation for T cell receptor (TCR) activation of LFA-1.
Rudd et al., Cambridge, United Kingdom. In J Biol Chem, 2011
N-terminal myr-tagged SKAP1 for membrane binding facilitated constitutive RapL membrane and Rap1 binding and effectively substituted for PI3K and TCR ligation in the activation of LFA-1 in T cells.
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.
Shimizu et al., Minneapolis, United States. In J Immunol, 2011
Data suggest that the presence or absence of associated SKAP55 defines functionally distinct pools of ADAP.
A genome-wide association study identifies susceptibility loci for ovarian cancer at 2q31 and 8q24.
Ovarian Cancer Association Consortium (OCAC) et al., Rochester, United States. In Nat Genet, 2010
Single nucleotide polymorphism in SKAP1 is associated with ovarian cancer.
T cell receptor "inside-out" pathway via signaling module SKAP1-RapL regulates T cell motility and interactions in lymph nodes.
Rudd et al., Cambridge, United Kingdom. In Immunity, 2010
findings define a T cell receptor "inside-out" pathway via N-SKAP1-C-RapL that regulates T cell adhesion, motility, and arrest times with dendritic cells in lymph nodes.
HPK1 associates with SKAP-HOM to negatively regulate Rap1-mediated B-lymphocyte adhesion.
Achatz et al., Salzburg, Austria. In Plos One, 2009
HPK1 associates with SKAP1 to negatively regulate Rap1-mediated B-lymphocyte adhesion.
SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesion.
Rudd et al., Cambridge, United Kingdom. In Trends Cell Biol, 2008
New candidates include immune-cell-specific adaptor proteins ADAP, SKAP-55 and SKAP-55-related (SKAP-55R).
Small GTPases and LFA-1 reciprocally modulate adhesion and signaling.
Philips et al., New York City, United States. In Immunol Rev, 2007
adhesion and degranulation-promoting adapter protein (ADAP) and Src kinase-associated phosphoprotein of 55 kDa (SKAP-55)].
Adaptors and linkers in T and B cells.
Schraven et al., Magdeburg, Germany. In Curr Opin Immunol, 2004
Finally, an involvement of the cytosolic adaptors ADAP, SKAP-55 and Cbl-b in the regulation of lymphocyte adhesion and migration has been demonstrated.
T-cell integrins: more than just sticking points.
McDowall et al., London, United Kingdom. In J Cell Sci, 2004
Signalling pathways involving ADAP, Vav-1 and SKAP-55, as well as Rap1 and RAPL, cause clustering of leukocyte function-associated antigen-1 (LFA-1; integrin alphaLbeta2).
SKAP-55 regulates integrin adhesion and formation of T cell-APC conjugates.
Rudd et al., London, United Kingdom. In Nat Immunol, 2003
SKAP-55 regulates integrin-mediated adhesion and conjugate formation between T cells and antigen-presenting cells
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