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Papers In Press, published online ahead of print June 7, 2004
Department of Cell Biology, Nara Institute of Science and Technology, Ikoma, Nara 630-0192
Corresponding Author: hitoh{at}bs.naist.jp
Cell migration plays key roles in physiological and pathological phenomena, such as development and oncogenesis. The adaptor proteins Grb2, CrkII, and Nck1 are composed only of a single Src homology (SH) 2 domain and some SH3 domains, giving specificity to each signal transduction pathway. However, little is known about the relationships between their adaptor proteins and cell migration, which are regulated by the G protein-coupled receptor (GPCR). Here, we show that Nck1, but not Grb2 or CrkII, mediates the inhibition of cell migration induced by the endothelin-1 (ET-1) and endothelin type A (ETA) receptor. The small interference RNA and dominat negative mutants of Nck1 inhibited the ET-1-induced inhibition. Although overexpression of wild-type Nck1 was detected in the cytosol and did not affect cell migration, expression of the myristoylation signal sequence-conjugated Nck1 was in the membrane and induced activation of Cdc42 and c-Jun N-terminal kinase (JNK), inhibiting cell migration. Taken together, these results suggest that the endothelin A receptor transduces the signal of inhibition of cell migration through Cdc42-dependent JNK activation by using Nck1. These findings provide new insights into the GPCR-mediated regulation of cell migration.[
J. Biol. Chem, 10.1074/jbc.M402767200
Submitted on March 11, 2004
Revised on June 2, 2004
Accepted on June 7, 2004
The adaptor protein Nck1 mediates endothelin A receptor-regulated cell migration through the Cdc42-dependent c-Jun N-terminal kinase pathway
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