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Heat shock protein 90? stabilizes focal adhesion kinase and enhances cell migration and invasion in breast cancer cells.

ABSTRACT: Focal adhesion kinase (FAK) acts as a regulator of cellular signaling and may promote cell spreading, motility, invasion and survival in malignancy. Elevated expression and activity of FAK frequently correlate with tumor cell metastasis and poor prognosis in breast cancer. However, the mechanisms by which the turnover of FAK is regulated remain elusive. Here we report that heat shock protein 90? (HSP90?) interacts with FAK and the middle domain (amino acids 233-620) of HSP90? is mainly responsible for this interaction. Furthermore, we found that HSP90? regulates FAK stability since HSP90? inhibitor 17-AAG triggers FAK ubiquitylation and subsequent proteasome-dependent degradation. Moreover, disrupted FAK-HSP90? interaction induced by 17-AAG contributes to attenuation of tumor cell growth, migration, and invasion. Together, our results reveal how HSP90? regulates FAK stability and identifies a potential therapeutic strategy to breast cancer.

SUBMITTER: Xiong X 

PROVIDER: S-EPMC4120946 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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Heat shock protein 90β stabilizes focal adhesion kinase and enhances cell migration and invasion in breast cancer cells.

Xiong Xiangyang X   Wang Yao Y   Liu Chengmei C   Lu Quqin Q   Liu Tao T   Chen Guoan G   Rao Hai H   Luo Shiwen S  

Experimental cell research 20140528 1

Focal adhesion kinase (FAK) acts as a regulator of cellular signaling and may promote cell spreading, motility, invasion and survival in malignancy. Elevated expression and activity of FAK frequently correlate with tumor cell metastasis and poor prognosis in breast cancer. However, the mechanisms by which the turnover of FAK is regulated remain elusive. Here we report that heat shock protein 90β (HSP90β) interacts with FAK and the middle domain (amino acids 233-620) of HSP90β is mainly responsib  ...[more]

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