Novel role for CRK adaptor proteins as essential components of SRC/FAK signaling for epithelial-mesenchymal transition and colorectal cancer aggressiveness.
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.
Data report that CRK elevates the expression of ErbB2 in bladder cancer (BC) cells which is transferred to the recipient cells in target organs by exosomes contributing to the distant metastasis of BC.
A reduced miR-126 expression and an elevated Crk protein expression alone or in combination statistically correlated with aggressive clinicopathological characteristics such as larger tumor size deeper local invasion more lymph node metastasis advanced TNM stage and poorer prognosis.
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.
In individuals with class I 17p13.3 microduplications including CRK we recommend biochemical evaluation of the growth hormone axis. Providers caring for these patients should be aware of their possible risk for the development of central precocious puberty.
Study investigated structures and thermodynamics of the interactions mediated by N-terminal Src homology 3 domain of CrkII and proline-rich motifs (PRMs) of cAbl kinase highlight the role of interfacial water molecules and the conformational entropy in the SH3:PRM interactions
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