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J. Biol. Chem., Vol. 283, Issue 27, 19112-19118, July 4, 2008

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Src Directly Phosphorylates Bif-1 and Prevents Its Interaction with Bax and the Initiation of Anoikis^*

From the H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33612

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.

Received for publication, December 4, 2007 , and in revised form, April 11, 2008.

^* This work was supported, in whole or in part, by the National Institutes of Health. This work was also supported by the American Cancer Society and the Flight Attendant Medical Research Institute. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Both authors contributed equally to this work.

² Present address: The University of Texas M. D. Anderson Cancer Center, Houston, TX 77030.

³ To whom correspondence should be addressed: Drug Discovery Program, Moffitt Cancer Center, 12902 Magnolia Dr., Tampa, FL 33612. Tel.: 813-745-6764; Fax: 813-745-7265; E-mail: Hong-Gang.Wang{at}Moffitt.org.

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