SKAP1 protein PH domain determines RapL membrane localization and Rap1 protein complex formation for T cell receptor (TCR) activation of LFA-1. (Q38676163)

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scientific article published on 13 June 2011

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English	SKAP1 protein PH domain determines RapL membrane localization and Rap1 protein complex formation for T cell receptor (TCR) activation of LFA-1.	scientific article published on 13 June 2011

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

SKAP1 protein PH domain determines RapL membrane localization and Rap1 protein complex formation for T cell receptor (TCR) activation of LFA-1. (English)

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

author name string

Monika Raab

1

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

Xin Smith

2

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

Yves Matthess

3

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

Klaus Strebhardt

4

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

Christopher E Rudd

5

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Europe PubMed Central

PMC publication ID

5 September 2017

language of work or name

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publication date

13 June 2011

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Europe PubMed Central

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5 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

PMC publication ID

5 September 2017

286

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Europe PubMed Central

PMC publication ID

5 September 2017

34

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

29663-29670

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

T cell receptor "inside-out" pathway via signaling module SKAP1-RapL regulates T cell motility and interactions in lymph nodes

1 reference

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SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility

1 reference

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RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences

1 reference

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The Skap-hom Dimerization and PH Domains Comprise a 3′-Phosphoinositide-Gated Molecular Switch

1 reference

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SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesion

1 reference

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6 September 2017

The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1

1 reference

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Spatiotemporal regulation of the kinase Mst1 by binding protein RAPL is critical for lymphocyte polarity and adhesion

1 reference

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Regulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor protein

1 reference

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Intracellular signalling controlling integrin activation in lymphocytes

1 reference

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An essential role for SKAP-55 in LFA-1 clustering on T cells that cannot be substituted by SKAP-55R

1 reference

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1 reference

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ADAP-SLP-76 binding differentially regulates supramolecular activation cluster (SMAC) formation relative to T cell-APC conjugation

1 reference

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Membranes as messengers in T cell adhesion signaling

1 reference

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Rap1 up-regulation and activation on plasma membrane regulates T cell adhesion.

1 reference

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Integrin avidity regulation: are changes in affinity and conformation underemphasized?

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Itk functions to control actin polymerization at the immune synapse through localized activation of Cdc42 and WASP.

1 reference

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RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1

1 reference

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SKAP-55 regulates integrin adhesion and formation of T cell-APC conjugates

1 reference

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Adaptor FYB (Fyn-binding protein) regulates integrin-mediated adhesion and mediator release: differential involvement of the FYB SH3 domain

1 reference

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SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55

1 reference

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Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase

1 reference

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Cutting edge: SLP-76 cooperativity with FYB/FYN-T in the Up-regulation of TCR-driven IL-2 transcription requires SLP-76 binding to FYB at Tyr595 and Tyr651

1 reference

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Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130) interacts with SLP-76 and up-regulates interleukin 2 production

1 reference

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FYN-T-FYB-SLP-76 interactions define a T-cell receptor zeta/CD3-mediated tyrosine phosphorylation pathway that up-regulates interleukin 2 transcription in T-cells

1 reference

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Adaptors and molecular scaffolds in immune cell signaling

1 reference

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Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130

1 reference

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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

1 reference

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Signaling in the immunological synapse: defining the optimal size

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Biochemistry. PI3K charges ahead

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12 December 2020

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10.1074/JBC.M111.222661

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

5 September 2017

PubMed publication ID

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Europe PubMed Central

PMC publication ID

5 September 2017

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