ACAP4 physically interacts with CrkII. Functional characterization showed that the interaction is required for the recruitment of ACAP4 to the plasma membrane where ACAP4 functions to regulate the recycling of the signal transducer integrin beta1.
Findings delineate a novel role for Crk Tyr239 phosphorylation in the regulation of Src kinases as well as a potential molecular explanation for a long-standing question as to how Crk regulates the activation of Src kinases.
Crk-dependent increased phosphorylation of CD3zeta coincided with inhibition of TCR downmodulation supporting a positive role for Crk adaptor proteins in TCR-mediated signal amplification.
Data indicate the role of tyrosine phosphorylation in regulating modular domain utilization in v-crk sarcoma virus CT10 oncogene homolog (avian) protein (Crk).
The present data demonstrate that immunophilins regulate CrkII but not CrkI activity in T cells and suggest that CsA and FK506 inhibit selected effector T cell functions via a CrkII-dependent mechanism.
Crk1/2 and CrkL are physically linked functionally complement each other during podocyte foot process spreading and together are required for developing typical foot process architecture.
differential binding selectivity of Crk and CrkL to their downstream partners Dock 180 and C3G was demonstrated in ovarian cancer cell line SKOV3 through coimmunoprecipitation
These results imply that binding capacity of influenza A virus NS1 to CRK/CRKL has evolved in virus strains that over-induce the antiviral acting JNK-ATF2 signalling module and helps to suppress the detrimental apoptosis promoting action of this pathway.
results suggest that biological functions attributed to the association of Zap70 with Vav after T cell activation may equally reflect the association of Zap70 with CrkII and further support a regulatory role for CrkII in TCR-linked signal transduction
while N-terminal SH3 of CrkII promotes assembly between CrkII and DOCK180 the C-terminal SH3 of CrkII regulates the stability and turnover of the DOCK180/ELMO complex
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