Literature DB >> 16498703

Yeast 14-3-3 proteins.

G Paul H van Heusden1, H Yde Steensma.   

Abstract

14-3-3 proteins form a family of highly conserved proteins which are present in all eukaryotic organisms investigated, often in multiple isoforms, up to 13 in some plants. They interact with more than 200 different, mostly phosphorylated proteins. The molecular consequences of 14-3-3 binding are diverse: this binding may result in stabilization of the active or inactive phosphorylated form of the protein, to a conformational alteration leading to activation or inhibition, to a different subcellular localization, to the interaction with other proteins or to shielding of binding sites. The binding partners, and hence the 14-3-3 proteins, are involved in almost every cellular process and 14-3-3 proteins have been linked to several diseases, such as cancer, Alzheimer's disease, the neurological Miller-Dieker and spinocerebellar ataxia type 1 diseases and bovine spongiform encephalopathy (BSE). The yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe both have two genes encoding 14-3-3 proteins, BMH1 and BMH2 and rad24 and rad25, respectively. In these yeasts, 14-3-3 proteins are essential in most laboratory strains. As in higher eukaryotes, yeast 14-3-3 proteins bind to numerous proteins involved in a variety of cellular processes. Recent genome-wide studies on yeast strains with impaired 14-3-3 function support the participation of 14-3-3 proteins in numerous yeast cellular processes. Given the high evolutionary conservation of the 14-3-3 proteins, the experimental accessibility and relative simplicity of yeasts make them excellent model organisms for elucidating the function of the 14-3-3 protein family. Copyright 2006 John Wiley & Sons, Ltd.

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Year:  2006        PMID: 16498703     DOI: 10.1002/yea.1338

Source DB:  PubMed          Journal:  Yeast        ISSN: 0749-503X            Impact factor:   3.239


  42 in total

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4.  Pichia pastoris 14-3-3 regulates transcriptional activity of the methanol inducible transcription factor Mxr1 by direct interaction.

Authors:  Pabitra K Parua; Paul M Ryan; Kayla Trang; Elton T Young
Journal:  Mol Microbiol       Date:  2012-06-12       Impact factor: 3.501

5.  General Amino Acid Control and 14-3-3 Proteins Bmh1/2 Are Required for Nitrogen Catabolite Repression-Sensitive Regulation of Gln3 and Gat1 Localization.

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Journal:  Genetics       Date:  2016-12-22       Impact factor: 4.562

6.  Schizosaccharomyces pombe Dss1p is a DNA damage checkpoint protein that recruits Rad24p, Cdc25p, and Rae1p to DNA double-strand breaks.

Authors:  Saravana P Selvanathan; Anjan G Thakurta; Jothy Dhakshnamoorthy; Ming Zhou; Timothy D Veenstra; Ravi Dhar
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7.  Bioinformatic and experimental survey of 14-3-3-binding sites.

Authors:  Catherine Johnson; Sandra Crowther; Margaret J Stafford; David G Campbell; Rachel Toth; Carol MacKintosh
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8.  14-3-3 (Bmh) proteins regulate combinatorial transcription following RNA polymerase II recruitment by binding at Adr1-dependent promoters in Saccharomyces cerevisiae.

Authors:  Katherine A Braun; Pabitra K Parua; Kenneth M Dombek; Gregory E Miner; Elton T Young
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9.  Bmh1p (14-3-3) mediates pathways associated with virulence in Candida albicans.

Authors:  Michelle N Kelly; Douglas A Johnston; Bethany A Peel; Timothy W Morgan; Glen E Palmer; Joy E Sturtevant
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10.  Nucleocytoplasmic shuttling of the Golgi phosphatidylinositol 4-kinase Pik1 is regulated by 14-3-3 proteins and coordinates Golgi function with cell growth.

Authors:  Lars Demmel; Mike Beck; Christian Klose; Anne-Lore Schlaitz; Yvonne Gloor; Peggy P Hsu; Jan Havlis; Andrej Shevchenko; Eberhard Krause; Yannis Kalaidzidis; Christiane Walch-Solimena
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