Grb7 protein stability modulated by pin1 in association with cell cycle progression

Yu Ling Tai, Li Hsuan Tung, Yu Chi Lin, Pei Jung Lu, Pei Yu Chu, Ming Yang Wang, Wei Pang Huang, Ko Chien Chen, Hsinyu Lee, Tang Long Shen

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

Growth factor receptor bound protein-7 (Grb7) is a multi-domain adaptor protein that is co-opted by numerous tyrosine kinases involved in various cellular signaling and functions. The molecular mechanisms underlying the regulation of Grb7 remain unclear. Here, we revealed a novel negative post-translational regulation of Grb7 by the peptidylprolyl cis/trans isomerase, Pin1. Our data show that phosphorylation of Grb7 protein on the Ser194-Pro motif by c-Jun N-terminal kinase facilitates its binding with the WW domain of Pin1. Subsequently, Grb7 is degraded by the ubiquitin- and proteasome-dependent proteolytic pathway. Indeed, we found that Pin1 exerts its peptidyl-prolyl cis/trans isomerase activity in the modulation of Grb7 protein stability in regulation of cell cycle progression at the G2-M phase. This study illustrates a novel regulatory mechanism in modulating Grb7-mediated signaling, which may take part in pathophysiological consequences.

Original languageEnglish
Article numbere0163617
JournalPloS one
Volume11
Issue number9
DOIs
Publication statusPublished - 2016 Sep

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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