Document Detail

Global mapping of protein phosphorylation events identifies Ste20, Sch9 and the cell-cycle regulatory kinases Cdc28/Pho85 as mediators of fatty acid starvation responses in Saccharomyces cerevisiae.
MedLine Citation:
PMID:  22218487     Owner:  NLM     Status:  MEDLINE    
Synthesis, degradation, and metabolism of fatty acids are strictly coordinated to meet the nutritional and energetic needs of cells and organisms. In the absence of exogenous fatty acids, proliferation and growth of the yeast Saccharomyces cerevisiae depends on endogenous synthesis of fatty acids, which is catalysed by fatty acid synthase. In the present study, we have used quantitative proteomics to examine the cellular response to inhibition of fatty acid synthesis in Saccharomyces cerevisiae. We have identified approximately 2000 phosphorylation sites of which more than 400 have been identified as being regulated in a temporal manner in response to inhibition of fatty acid synthesis by cerulenin. By bioinformatic analysis of these phosphorylation events, we have identified the cell cycle kinases Cdc28 and Pho85, the PAK kinase Ste20 as well as the protein kinase Sch9 as central mediators of the cellular response to inhibition of fatty acid synthesis.
Dennis Pultz; Martin V Bennetzen; Steven Vestergaard Rødkær; Christine Zimmermann; Jorrit M Enserink; Jens S Andersen; Nils J Færgeman
Related Documents :
18960127 - The stability constants of tar and par complexes.
18173227 - Pegylated dendrimers with core functionality for biological applications.
23643917 - Conjugation of succinic acid to non-ionogenic amphiphilic polymers modulates their inte...
15835147 - Chemically transformable configurations of mercaptohexadecanoic acid self-assembled mon...
7073957 - The effect of culture media on the production and measurement of luminol-dependent chem...
12798497 - First synthesis of phosphonobile acids and preliminary studies on their aggregation pro...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-01-04
Journal Detail:
Title:  Molecular bioSystems     Volume:  8     ISSN:  1742-2051     ISO Abbreviation:  Mol Biosyst     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-02-07     Completed Date:  2012-06-27     Revised Date:  2012-07-03    
Medline Journal Info:
Nlm Unique ID:  101251620     Medline TA:  Mol Biosyst     Country:  England    
Other Details:
Languages:  eng     Pagination:  796-803     Citation Subset:  IM    
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
CDC28 Protein Kinase, S cerevisiae / chemistry,  metabolism*
Cyclin-Dependent Kinases / chemistry,  genetics,  metabolism*
Fatty Acids / metabolism*
Intracellular Signaling Peptides and Proteins / chemistry,  metabolism*
MAP Kinase Kinase Kinases / chemistry,  metabolism*
Protein Kinases / chemistry,  metabolism*
Protein-Serine-Threonine Kinases / chemistry,  metabolism*
Proteomics / methods
Saccharomyces cerevisiae / enzymology*,  metabolism*
Saccharomyces cerevisiae Proteins / chemistry,  metabolism*
Reg. No./Substance:
0/Fatty Acids; 0/Intracellular Signaling Peptides and Proteins; 0/Saccharomyces cerevisiae Proteins; EC 2.7.-/Protein Kinases; EC 2.7.1.-/SCH9 protein kinase; EC Kinases; EC protein, S cerevisiae; EC Protein Kinase, S cerevisiae; EC Kinases; EC protein, S cerevisiae; EC Kinase Kinase Kinases; EC protein, S cerevisiae

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Treatment of neuromyelitis optica: an evidence based review.
Next Document:  Differential effects of 20 non-dioxin-like PCBs on basal and depolarisation-evoked intracellular cal...