| Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression. | |
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MedLine Citation:
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PMID: 19150427 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Christoph F Kurat; Heimo Wolinski; Julia Petschnigg; Supipi Kaluarachchi; Brenda Andrews; Klaus Natter; Sepp D Kohlwein |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular cell Volume: 33 ISSN: 1097-4164 ISO Abbreviation: Mol. Cell Publication Date: 2009 Jan |
Date Detail:
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Created Date: 2009-01-19 Completed Date: 2009-02-04 Revised Date: 2011-09-15 |
Medline Journal Info:
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Nlm Unique ID: 9802571 Medline TA: Mol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 53-63 Citation Subset: IM |
Affiliation:
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Institute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/II, A8010 Graz, Austria. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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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:
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F 3005-B19//Austrian Science Fund FWF; W 901-B12//Austrian Science Fund FWF |
| Chemical | |
Reg. No./Substance:
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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:
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Mol Cell. 2009 Jan 30;33(2):143-4
[PMID:
19187756
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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