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Article

New insights into FAK phosphorylation based on a FAT domain-defective mutation.

PloS one - 1 Jan 2014

Fang Xuqian, Liu Xiangfan, Yao Ling, Chen Changqiang, Lin Jiafei, Ni Peihua, Zheng Xinmin, Fan Qishi

Abstract excerpt

Mounting evidence suggests that the FAK N-terminal (FERM) domain controls FAK phosphorylation and function; however, little is known regarding the role of the C terminal (FAT) domain in FAK regulation. We identified a patient-derived FAK mutant, in which a 27-amino acid segment was deleted from the C-terminal FAT domain (named FAK-Del33). When FAK-Del33 was overexpressed in specific tumor cell lines, Y397...

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Identifiers

PMID: 25226367
DOI: 10.1371/journal.pone.0107134
PMCID: PMC4166415

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