Literature DB >> 16769213

14-3-3 proteins: regulation of endoplasmic reticulum localization and surface expression of membrane proteins.

Sojin Shikano1, Brian Coblitz, Meng Wu, Min Li.   

Abstract

The density and composition of cell surface proteins are major determinants for cellular functions. Regulation of cell surface molecules occurs at several levels, including the efficiency of surface transport, and is therefore of great interest. As the major phosphoprotein-binding modules, 14-3-3 proteins are known for their crucial roles in a wide range of cellular activities, including the subcellular localization of target proteins. Accumulating evidence suggests a role for 14-3-3 in surface transport of membrane proteins, in which 14-3-3 binding reduces endoplasmic reticulum (ER) localization, thereby promoting surface expression of membrane proteins. Here, we focus on recent evidence of 14-3-3-mediated surface transport and discuss the possible molecular mechanisms.

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Year:  2006        PMID: 16769213     DOI: 10.1016/j.tcb.2006.05.006

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  31 in total

1.  Phosphorylation-dependent C-terminal binding of 14-3-3 proteins promotes cell surface expression of HIV co-receptor GPR15.

Authors:  Yukari Okamoto; Sojin Shikano
Journal:  J Biol Chem       Date:  2010-12-28       Impact factor: 5.157

2.  Identification of Novel 14-3-3 Residues That Are Critical for Isoform-specific Interaction with GluN2C to Regulate N-Methyl-D-aspartate (NMDA) Receptor Trafficking.

Authors:  Connie Chung; Wei-Hua Wu; Bo-Shiun Chen
Journal:  J Biol Chem       Date:  2015-07-30       Impact factor: 5.157

3.  Structural basis for protein-protein interactions in the 14-3-3 protein family.

Authors:  Xiaowen Yang; Wen Hwa Lee; Frank Sobott; Evangelos Papagrigoriou; Carol V Robinson; J Günter Grossmann; Michael Sundström; Declan A Doyle; Jonathan M Elkins
Journal:  Proc Natl Acad Sci U S A       Date:  2006-11-03       Impact factor: 11.205

Review 4.  Mechanisms of cardiac potassium channel trafficking.

Authors:  David F Steele; Jodene Eldstrom; David Fedida
Journal:  J Physiol       Date:  2007-04-05       Impact factor: 5.182

5.  Dimerization is essential for 14-3-3zeta stability and function in vivo.

Authors:  Georgia Messaritou; Sofia Grammenoudi; Efthimios M C Skoulakis
Journal:  J Biol Chem       Date:  2009-11-17       Impact factor: 5.157

Review 6.  Minireview: Role of intracellular scaffolding proteins in the regulation of endocrine G protein-coupled receptor signaling.

Authors:  Cornelia Walther; Stephen S G Ferguson
Journal:  Mol Endocrinol       Date:  2015-05-05

7.  GAPDH binds Akt to facilitate cargo transport in the early secretory pathway.

Authors:  Ellen J Tisdale; Nikunj K Talati; Cristina R Artalejo; Assia Shisheva
Journal:  Exp Cell Res       Date:  2016-11-03       Impact factor: 3.905

Review 8.  Forward trafficking of ion channels: what the clinician needs to know.

Authors:  James W Smyth; Robin M Shaw
Journal:  Heart Rhythm       Date:  2010-05-25       Impact factor: 6.343

9.  15N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins.

Authors:  Sandeep Chhabra; Patrick Fischer; Koh Takeuchi; Abhinav Dubey; Joshua J Ziarek; Andras Boeszoermenyi; Daniel Mathieu; Wolfgang Bermel; Norman E Davey; Gerhard Wagner; Haribabu Arthanari
Journal:  Proc Natl Acad Sci U S A       Date:  2018-02-05       Impact factor: 11.205

10.  14-3-3 Protein regulates cell adhesion in the seminiferous epithelium of rat testes.

Authors:  Elissa W P Wong; Shengyi Sun; Michelle W M Li; Will M Lee; C Yan Cheng
Journal:  Endocrinology       Date:  2009-07-16       Impact factor: 4.736

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