Function of site-2 proteases in bacteria and bacterial pathogens Journal Article


Authors: Schneider, J. S.; Glickman, M. S.
Article Title: Function of site-2 proteases in bacteria and bacterial pathogens
Abstract: Site-2 proteases (S2Ps) are a class of intramembrane metalloproteases named after the founding member of this protein family, human S2P, which control cholesterol and fatty acid biosynthesis by cleaving Sterol Regulatory Element Binding Proteins which control cholesterol and fatty acid biosynthesis. S2Ps are widely distributed in bacteria and participate in diverse pathways that control such diverse functions as membrane integrity, sporulation, lipid biosynthesis, pheromone production, virulence, and others. The most common signaling mechanism mediated by S2Ps is the coupled degradation of transmembrane anti-Sigma factors to activate ECF Sigma factor regulons. However, additional signaling mechanisms continue to emerge as more prokaryotic S2Ps are characterized, including direct proteolysis of membrane embedded transcription factors and proteolysis of non-transcriptional membrane proteins or membrane protein remnants. In this review we seek to comprehensively review the functions of S2Ps in bacteria and bacterial pathogens and attempt to organize these proteases into conceptual groups that will spur further study. This article is part of a Special Issue entitled: Intramembrane Proteases. © 2013 Elsevier B.V. All rights reserved.
Keywords: bacterial signal transduction; site two protease
Journal Title: Biochimica et Biophysica Acta (BBA) - Biomembranes
Volume: 1828
Issue: 12
ISSN: 0005-2736
Publisher: Elsevier B.V.  
Date Published: 2013-12-01
Start Page: 2808
End Page: 2814
Language: English
DOI: 10.1016/j.bbamem.2013.04.019
PROVIDER: scopus
PUBMED: 24099002
PMCID: PMC4097180
DOI/URL:
Notes: --- - Cited By (since 1996):1 - "Export Date: 1 November 2013" - "CODEN: BBBMB" - "Source: Scopus"
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  1. Michael Glickman
    109 Glickman