Src directly phosphorylates Bif-1 and prevents its interaction with Bax and the initiation of anoikis

Hirohito Yamaguchi, Nicholas T. Woods, Jay F. Dorsey, Yoshinori Takahashi, Nicole R. Gjertsen, Timothy Yeatman, Jie Wu, Hong Gang Wang

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

Bif-1 interacts with Bax and enhances its conformational rearrangement, resulting in apoptosis. However, the molecular mechanism governing the interaction between Bif-1 and Bax is poorly defined. Here we provide evidence that Bif-1 is phosphorylated, an event that can be repressed by apoptotic stimuli. The protein kinase c-Src binds to and directly phosphorylates Bif-1 on tyrosine 80. Moreover, Src phosphorylation of Bif-1 suppresses the interaction between Bif-1 and Bax, resulting in the inhibition of Bax activation during anoikis. Together, these results suggest that phosphorylation of Bif-1 impairs its binding to Bax and represses apoptosis, providing another mechanism by which Src oncogenic signaling can prevent cell death.

Original languageEnglish (US)
Pages (from-to)19112-19118
Number of pages7
JournalJournal of Biological Chemistry
Volume283
Issue number27
DOIs
StatePublished - Jul 4 2008

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Yamaguchi, H., Woods, N. T., Dorsey, J. F., Takahashi, Y., Gjertsen, N. R., Yeatman, T., Wu, J., & Wang, H. G. (2008). Src directly phosphorylates Bif-1 and prevents its interaction with Bax and the initiation of anoikis. Journal of Biological Chemistry, 283(27), 19112-19118. https://doi.org/10.1074/jbc.M709882200