Literature DB >> 16237703

O-GlcNAc cycling: how a single sugar post-translational modification is changing the way we think about signaling networks.

Chad Slawson1, Michael P Housley, Gerald W Hart.   

Abstract

O-GlcNAc is an ubiquitous post-translational protein modification consisting of a single N-acetlyglucosamine moiety linked to serine or threonine residues on nuclear and cytoplasmic proteins. Recent work has begun to uncover the functional roles of O-GlcNAc in cellular processes. O-GlcNAc modified proteins are involved in sensing the nutrient status of the surrounding cellular environment and adjusting the activity of cellular proteins accordingly. O-GlcNAc regulates cellular responses to hormones such as insulin, initiates a protective response to stress, modulates a cell's capacity to grow and divide, and regulates gene transcription. This review will focus on recent work involving O-GlcNAc in sensing the environment and regulating signaling cascades. (c) 2005 Wiley-Liss, Inc.

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Year:  2006        PMID: 16237703     DOI: 10.1002/jcb.20676

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  73 in total

Review 1.  Regulation of autophagy by protein post-translational modification.

Authors:  Willayat Yousuf Wani; Michaël Boyer-Guittaut; Matthew Dodson; John Chatham; Victor Darley-Usmar; Jianhua Zhang
Journal:  Lab Invest       Date:  2014-11-03       Impact factor: 5.662

2.  Support vector machine-based mucin-type o-linked glycosylation site prediction using enhanced sequence feature encoding.

Authors:  Manabu Torii; Hongfang Liu; Zhang-Zhi Hu
Journal:  AMIA Annu Symp Proc       Date:  2009-11-14

3.  Protein O-GlcNAcylation: A critical regulator of the cellular response to stress.

Authors:  John C Chatham; Richard B Marchase
Journal:  Curr Signal Transduct Ther       Date:  2010-01

Review 4.  Role of protein O-linked N-acetyl-glucosamine in mediating cell function and survival in the cardiovascular system.

Authors:  Norbert Fülöp; Richard B Marchase; John C Chatham
Journal:  Cardiovasc Res       Date:  2006-07-29       Impact factor: 10.787

5.  Beta-catenin in the liver: an integrator of proliferation and metabolism?

Authors:  Lawrence A Scheving; William E Russell
Journal:  Gastroenterology       Date:  2006-11       Impact factor: 22.682

6.  Two-dimensional gel-based approaches for the assessment of N-Linked and O-GlcNAc glycosylation in human and simian immunodeficiency viruses.

Authors:  David R M Graham; Megan J Mitsak; Steven T Elliott; Dawn Chen; Stephen A Whelan; Gerald W Hart; Jennifer E Van Eyk
Journal:  Proteomics       Date:  2008-12       Impact factor: 3.984

Review 7.  Functional O-GlcNAc modifications: implications in molecular regulation and pathophysiology.

Authors:  Krithika Vaidyanathan; Sean Durning; Lance Wells
Journal:  Crit Rev Biochem Mol Biol       Date:  2014-02-14       Impact factor: 8.250

8.  Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome.

Authors:  Mitsutaka Ogawa; Shogo Sawaguchi; Takami Kawai; Daita Nadano; Tsukasa Matsuda; Hirokazu Yagi; Koichi Kato; Koichi Furukawa; Tetsuya Okajima
Journal:  J Biol Chem       Date:  2014-12-08       Impact factor: 5.157

9.  Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes.

Authors:  Stephen A Whelan; Wagner B Dias; Lakshmanan Thiruneelakantapillai; M Daniel Lane; Gerald W Hart
Journal:  J Biol Chem       Date:  2009-12-17       Impact factor: 5.157

10.  Influence of glucosamine on glomerular mesangial cell turnover: implications for hyperglycemia and hexosamine pathway flux.

Authors:  Leighton R James; Catherine Le; James W Scholey
Journal:  Am J Physiol Endocrinol Metab       Date:  2009-11-10       Impact factor: 4.310

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