Document Detail


Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression.
MedLine Citation:
PMID:  19150427     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Triacylglycerols (TGs) serve essential cellular functions as reservoirs for energy substrates (fatty acids) and membrane lipid precursors (diacylglycerols and fatty acids). Here we show that the major yeast TG lipase Tgl4, the functional ortholog of murine adipose TG lipase ATGL, is phosphorylated and activated by cyclin-dependent kinase 1 (Cdk1/Cdc28). Phospho-Tgl4-catalyzed lipolysis contributes to early bud formation in late G1 phase of the cell cycle. Conversely, lack of lipolysis delays bud formation and cell-cycle progression. In the absence of beta-oxidation, lipolysis-derived metabolites are thus required to support cellular growth. TG homeostasis is the only metabolic process identified as yet that is directly regulated by Cdk1/Cdc28-dependent phosphorylation of key anabolic and catabolic enzymes, highlighting the importance of FA storage and mobilization during the cell cycle. Our data provide evidence for a direct link between cell-cycle-regulatory kinases and TG degradation and suggest a general mechanism for coordinating membrane synthesis with cell-cycle progression.
Authors:
Christoph F Kurat; Heimo Wolinski; Julia Petschnigg; Supipi Kaluarachchi; Brenda Andrews; Klaus Natter; Sepp D Kohlwein
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular cell     Volume:  33     ISSN:  1097-4164     ISO Abbreviation:  Mol. Cell     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2009-01-19     Completed Date:  2009-02-04     Revised Date:  2011-09-15    
Medline Journal Info:
Nlm Unique ID:  9802571     Medline TA:  Mol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  53-63     Citation Subset:  IM    
Affiliation:
Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/II, A8010 Graz, Austria.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
CDC2 Protein Kinase / metabolism*
CDC28 Protein Kinase, S cerevisiae / metabolism*
Cell Cycle*
Enzyme Activation
Fatty Acids / biosynthesis
G1 Phase
Homeostasis
Lipase / chemistry,  metabolism*
Lipids
Lipolysis*
Molecular Sequence Data
Phosphorylation
Phosphoserine / metabolism
Phosphothreonine / metabolism
Saccharomyces cerevisiae / cytology*,  enzymology*
Saccharomyces cerevisiae Proteins / chemistry,  metabolism*
Triglycerides / metabolism
Grant Support
ID/Acronym/Agency:
F 3005-B19//Austrian Science Fund FWF; W 901-B12//Austrian Science Fund FWF
Chemical
Reg. No./Substance:
0/Fatty Acids; 0/Lipids; 0/Saccharomyces cerevisiae Proteins; 0/Triglycerides; 1114-81-4/Phosphothreonine; 17885-08-4/Phosphoserine; EC 2.7.11.22/CDC2 Protein Kinase; EC 2.7.11.22/CDC28 Protein Kinase, S cerevisiae; EC 3.1.1.3/Lipase; EC 3.1.1.3/Tgl4 protein, S cerevisiae
Comments/Corrections
Comment In:
Mol Cell. 2009 Jan 30;33(2):143-4   [PMID:  19187756 ]

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


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