TAILIEUCHUNG - Báo cáo khoa học: PI3K⁄Akt signalling-mediated protein surface expression sensed by 14-3-3 interacting motif

The regulation of protein expression on the cell surface membrane is an important component of the cellular response to extracellular signalling. The translation of extracellular signalling into specific protein localization often involves the post-translational modification of cargo proteins. | ỊFEBS Journal PI3K Akt signalling-mediated protein surface expression sensed by 14-3-3 interacting motif Jean-Ju Chung1 z Yukari Okamoto2 Brian Coblitz1 f Min Li1 Yun Qiu3 and Sojin Shikano2 1 Department of Neuroscience Johns Hopkins University Baltimore MD USA 2 Department of Biochemistry and Molecular Genetics University of Illinois at Chicago IL USA 3 Department of Pharmacology and ExperimentalTherapeutics University of Maryland Baltimore MD USA Keywords 14-3-3 Akt GPR15 PI3K regulation of surface expression Correspondence S. Shikano Department of Biochemistry and Molecular Genetics University of Illinois at Chicago 900 S. Ashland Ave. Chicago IL 60607 USA Fax 1 312 413 0353 Tel 1 312 413 2029 E-mail sshikano@ Present addresses Howard Hughes MedicalInstitute Department of Cardiology Children s HospitalBoston Harvard Medical School Boston MA USA fDepartment of BiologicalSciences Columbia University New York NY USA Received 21 May 2009 revised 2 July 2009 accepted 24 July 2009 doi The regulation of protein expression on the cell surface membrane is an important component of the cellular response to extracellular signalling. The translation of extracellular signalling into specific protein localization often involves the post-translational modification of cargo proteins. Using a genetic screen of random peptides we have previously identified a group of C-terminal sequences represented by RGRSWTY-COOH termed SWTY which are capable of overriding an endoplasmic reticulum localization signal and directing membrane proteins to the cell surface via specific binding to 14-3-3 proteins. The identity of the kinase signalling pathways that drive phosphorylation and 14-3-3 binding of the SWTY sequence is not known. In this study we report that the activation of the phosphoinositide 3-kinase PI3K protein kinase B Akt pathway by the over-expression of active kinases stimulation with fetal bovine serum or growth factors can a phosphorylate

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