bei Google ScholarTitelangaben
Kurat, Christoph F. ; Wolinski, Heimo ; Petschnigg, Julia ; Kaluarachchi, Supipi ; Andrews, Brenda ; Natter, Klaus ; Kohlwein, Sepp D.:
Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression.
In: Molecular Cell.
Bd. 33
(2009)
Heft 1
.
- S. 53-63.
ISSN 1097-4164
DOI: https://doi.org/10.1016/j.molcel.2008.12.019
Abstract
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.
Weitere Angaben
| Publikationsform: | Artikel in einer Zeitschrift |
|---|---|
| Begutachteter Beitrag: | Ja |
| Institutionen der Universität: | Fakultäten > Fakultät für Biologie, Chemie und Geowissenschaften > Fachgruppe Biologie |
| Titel an der UBT entstanden: | Nein |
| Themengebiete aus DDC: | 500 Naturwissenschaften und Mathematik > 500 Naturwissenschaften |
| Eingestellt am: | 06 Aug 2026 07:31 |
| Letzte Änderung: | 06 Aug 2026 07:31 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/99222 |