| RRC ID |
72853
|
| 著者 |
Nakatsukasa K, Fujisawa M, Yang X, Kawarasaki T, Okumura F, Kamura T.
|
| タイトル |
Triacylglycerol lipase Tgl4 is a stable protein and its dephosphorylation is regulated in a cell cycle-dependent manner in Saccharomyces cerevisiae.
|
| ジャーナル |
Biochem Biophys Res Commun
|
| Abstract |
Triacylglycerols (TGs) serve as reservoirs for diacylglycerols and fatty acids, which play important roles in synthesizing energy and membrane lipids that are required for cell cycle progression. In the yeast, Saccharomyces cerevisiae, Tgl4, the functional ortholog of murine adipose triacylglycerol lipase (ATGL), is activated by Cdk1/Cdc28-mediated phosphorylation and facilitates the G1/S transition. However, little is known about how Tgl4 is inactivated during the cell cycle. To monitor the phosphorylation status and the stability of endogenous Tgl4, we raised a specific antibody against Tgl4. We found that in contrast to the previous suggestion, Tgl4 was a stable protein throughout the cell cycle. We also showed that Tgl4 was dephosphorylated upon entry into G1 phase. These results suggest that Tgl4 is a stable protein and is inactivated during G1 phase by dephosphorylation.
|
| 巻・号 |
626
|
| ページ |
85-91
|
| 公開日 |
2022-10-20
|
| DOI |
10.1016/j.bbrc.2022.08.022
|
| PII |
S0006-291X(22)01135-4
|
| PMID |
35981421
|
| MeSH |
Animals
Cell Cycle
Lipase / genetics
Lipase / metabolism
Mice
Phosphorylation
Saccharomyces cerevisiae* / metabolism
Saccharomyces cerevisiae Proteins* / metabolism
Triglycerides / metabolism
|
| IF |
2.985
|
| リソース情報 |
| 酵母 |
BY22800, BY8258 |
