| Literature DB >> 28759036 |
Y-R Chen1, H-C Chou1, C-H Yang1, H-Y Chen1,2, Y-W Liu1, T-Y Lin1, C-L Yeh1, W-T Chao2, H-H Tsou3,4, H-C Chuang5, T-H Tan5,6.
Abstract
Vaccinia H1-related phosphatase (VHR/DUSP3) is a member of the dual-specificity phosphatase family. Deregulation of VHR is observed in various malignant diseases. We identified focal adhesion kinase (FAK) as a VHR-interacting molecule. Over-expression of VHR decreased tyrosine phosphorylation of FAK and decreasing VHR promoted FAK tyrosine phosphorylation. In vitro assays proved that recombinant VHR directly dephosphorylated FAK and paxillin. VHR-knockout mice did not have obvious abnormality; however, VHR-knockout cells showed decreased expression of integrins and FAK but stronger FAK and paxillin phosphorylation upon attachment to fibronectin. Additionally, VHR-knockout fibroblast and lung epithelial cells had elevated ligand-induced epidermal growth factor receptor (EGFR) phosphorylation. Inducible expression of VHR suppressed directional cell migration, and VHR deficiency resulted in a higher cell migratory ability. VHR-knockout cells have stronger FAK phosphorylation in cell adhesions, long-lasting trailing ends and slower turnover of focal adhesions. These collective data indicate that VHR is a FAK phosphatase and participates in regulating the formation and disassembly of focal adhesions.Entities:
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Year: 2017 PMID： 28759036 DOI： 10.1038/onc.2017.255
Source DB: PubMed Journal: Oncogene ISSN： 0950-9232 Impact factor: 9.867