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[Cancer Research 62, 6475-6480, November 15, 2002]
© 2002 American Association for Cancer Research

Advances in Brief

14-3-3 Interacts with the Tumor Suppressor Tuberin at Akt Phosphorylation Site(s)1

Matt Y. Liu2, Shengli Cai2, Alexsandra Espejo, Mark T. Bedford and Cheryl Lyn Walker3

Department of Carcinogenesis, Science Park-Research Division, The University of Texas M. D. Anderson Cancer Center, Smithville, Texas 78957

Tuberin, the product of the tuberous sclerosis complex 2 tumor suppressor gene, is a phosphoprotein that negatively regulates phosphatidylinositol 3'-kinase signaling downstream of Akt. Several high stringency 14-3-3 binding sites that overlapped with Akt phosphorylation sites were identified in tuberin in silico. Recognition of tuberin by an {alpha}-14-3-3 binding site-specific antibody correlated with mitogen-induced phosphorylation of tuberin and recognition of tuberin by an {alpha}-Akt phosphorylation substrate antibody. Recognition of tuberin by both antibodies was blocked by inhibiting phosphatidylinositol 3'-kinase activity. Using a protein domain microarray, a tuberin peptide containing Ser939 demonstrated phospho-specific binding to 14-3-3. Glutathione S-transferase pull-down assays with 14-3-3 fusion proteins revealed that all seven 14-3-3 isoforms (ß, {gamma}, {zeta}, {epsilon}, {tau}, {eta}, and {varsigma}) could bind tuberin, and this interaction was abrogated by competition with phosphorylated but not unphosphorylated Ser939 tuberin peptide. Tuberin also coimmunoprecipitated with 14-3-3, confirming the interaction between endogenous 14-3-3 and tuberin. These data establish the presence of functional and overlapping 14-3-3 and Akt recognition site(s) in tuberin.




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