期刊
EMBO JOURNAL
卷 23, 期 14, 页码 2777-2788出版社
WILEY
DOI: 10.1038/sj.emboj.7600291
关键词
cell migration; integrin; Nischarin; PAK
资金
- NHLBI NIH HHS [HL4500] Funding Source: Medline
- NIGMS NIH HHS [R01 GM026165, GM26165] Funding Source: Medline
Nischarin, a novel intracellular protein, was originally identified as a binding partner for the beta5beta1 integrin. Here we show that Nischarin also interacts with members of the PAK family of kinases. The amino terminus of Nischarin preferentially binds to the carboxy-terminal domain of PAK1 when the kinase is in its activated conformation. Nischarin binding to PAK1 is enhanced by active Rac, with the three proteins forming a complex, while expression of the alpha5beta1 integrin also increases the Nischarin/PAK1 association. Interaction with Nischarin strongly inhibits the ability of PAK1 to phosphorylate substrates. This effect on PAK kinase activity closely parallels Nischarin's ability to inhibit cell migration. Conversely, reduction of endogenous levels of Nischarin by RNA interference promotes cell migration. In addition, PAK1 and Nischarin colocalize in membrane ruffles, structures known to be involved in cell motility. Thus, Nischarin may regulate cell migration by forming inhibitory complexes with PAK family kinases.
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