The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4.
Belongs to the CRK family. Contains 1 SH2 domain. Contains 2 SH3 domains.
The C-terminal SH3 domain function as a negative modulator for transformation and the N-terminal SH3 domain appears to function as a positive regulator for transformation. The SH2 domain mediates interaction with SHB.
Phosphorylation of Crk-II (40 kDa) gives rise to a 42 kDa form. Phosphorylated on Tyr-221 upon cell adhesion. Results in the negative regulation of the association with SH2- and SH3-binding partners, possibly by the formation of an intramolecular interaction of phosphorylated Tyr-221 with the SH2 domain. This leads finally to the down-regulation of the Crk signaling pathway.
Cytoplasm. Cell membrane. Translocated to the plasma membrane upon cell adhesion.
Nieto-Pelegrin E et al. Crk adaptors negatively regulate actin polymerization in pedestals formed by enteropathogenic Escherichia coli (EPEC) by binding to Tir effector. PLoS Pathog10:e1004022 (2014).
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Li XN et al. The p38 MAPK inhibitor JLU1124 inhibits the inflammatory response induced by lipopolysaccharide through the MAPK-NF-?B pathway in RAW264.7 macrophages. Int Immunopharmacol17:785-92 (2013).
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