Literature DB >> 16725345

14-3-3 proteins as potential oncogenes.

Guri Tzivion1, Vinita Singh Gupta, Ludmila Kaplun, Vitaly Balan.   

Abstract

14-3-3 proteins are a family of highly conserved cellular proteins that play key roles in the regulation of central physiological pathways. More than 200 14-3-3 target proteins have been identified, including proteins involved in mitogenic and cell survival signaling, cell cycle control and apoptotic cell death. Importantly, the involvement of 14-3-3 proteins in the regulation of various oncogenes and tumor suppressor genes points to a potential role in human cancer. The present review summarizes current findings implicating a 14-3-3 role in cancer while discussing potential mechanisms and points of action of 14-3-3 during cancer development and progression.

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Year:  2006        PMID: 16725345     DOI: 10.1016/j.semcancer.2006.03.004

Source DB:  PubMed          Journal:  Semin Cancer Biol        ISSN: 1044-579X            Impact factor:   15.707


  83 in total

1.  Identification of potential protein targets of isothiocyanates by proteomics.

Authors:  Lixin Mi; Brian L Hood; Nicolas A Stewart; Zhen Xiao; Sudha Govind; Xiantao Wang; Thomas P Conrads; Timothy D Veenstra; Fung-Lung Chung
Journal:  Chem Res Toxicol       Date:  2011-08-26       Impact factor: 3.739

2.  14-3-3 binding sites in the snail protein are essential for snail-mediated transcriptional repression and epithelial-mesenchymal differentiation.

Authors:  Zhaoyuan Hou; Hongzhuang Peng; David E White; Pu Wang; Paul M Lieberman; Thanos Halazonetis; Frank J Rauscher
Journal:  Cancer Res       Date:  2010-05-25       Impact factor: 12.701

3.  Identification of phosphorylation sites in betaPIX and PAK1.

Authors:  Mark W Mayhew; Erin D Jeffery; Nicholas E Sherman; Kristina Nelson; Joy M Polefrone; Stephen J Pratt; Jeffrey Shabanowitz; J Thomas Parsons; Jay W Fox; Donald F Hunt; Alan F Horwitz
Journal:  J Cell Sci       Date:  2007-11-15       Impact factor: 5.285

4.  An emerin "proteome": purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture.

Authors:  James M Holaska; Katherine L Wilson
Journal:  Biochemistry       Date:  2007-07-10       Impact factor: 3.162

5.  Down-regulation of 14-3-3 isoforms and annexin A5 proteins in lung adenocarcinoma induced by the tobacco-specific nitrosamine NNK in the A/J mouse revealed by proteomic analysis.

Authors:  James D Bortner; Arunangshu Das; Todd M Umstead; Williard M Freeman; Richard Somiari; Cesar Aliaga; David S Phelps; Karam El-Bayoumy
Journal:  J Proteome Res       Date:  2009-08       Impact factor: 4.466

6.  14-3-3, an integrator of cell mechanics and cytokinesis.

Authors:  Douglas N Robinson
Journal:  Small GTPases       Date:  2010-11

7.  14-3-3Tau regulates ubiquitin-independent proteasomal degradation of p21, a novel mechanism of p21 downregulation in breast cancer.

Authors:  Bing Wang; Kang Liu; Hui-Yi Lin; Naresh Bellam; Shiyun Ling; Weei-Chin Lin
Journal:  Mol Cell Biol       Date:  2010-01-19       Impact factor: 4.272

8.  Toxoplasma gondii: effect of infection on expression of 14-3-3 proteins in human epithelial cells.

Authors:  Fernando P Monroy
Journal:  Exp Parasitol       Date:  2007-08-03       Impact factor: 2.011

9.  Biotin tagging coupled with amino acid-coded mass tagging for efficient and precise screening of interaction proteome in mammalian cells.

Authors:  Yu-Fei He; Hui-Min Bao; Xiao-Feng Xiao; Shuai Zuo; Ru-Yun Du; Si-Wei Tang; Peng-Yuan Yang; Xian Chen
Journal:  Proteomics       Date:  2009-12       Impact factor: 3.984

10.  Presence and distribution of 14-3-3 proteins in human ocular surface tissues.

Authors:  Jwalitha Shankardas; Michelle Senchyna; Slobodan D Dimitrijevich
Journal:  Mol Vis       Date:  2008-12-31       Impact factor: 2.367

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