期刊
JOURNAL OF CELL SCIENCE
卷 132, 期 21, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.232389
关键词
SIRT2; Golgi; Acetylation; GRASP55; Golgi assembly; Cell cycle
类别
资金
- National Institutes of Health [GM112786, GM105920, GM130331]
- MCubed and the Fast Forward Protein Folding Disease Initiative of the University of Michigan
- Vienna Science and Technology Fund (WWTF) [LS14-001]
- Max Perutz Labs (MFPL) start-up
Sirtuin 2 (SIRT2) is an NAD-dependent sirtuin deacetylase that regulates microtubule and chromatin dynamics, gene expression and cell cycle progression, aswell as nuclear envelope reassembly. Recent proteomic analyses have identifiedGolgi proteins as SIRT2 interactors, indicating that SIRT2 may also play a role in Golgi structure formation. Here, we show that SIRT2 depletion causes Golgi fragmentation and impairsGolgi reassembly at the end of mitosis. SIRT2 interacts with the Golgi reassembly stacking protein GRASP55 (also known as GORASP2) in mitosis when GRASP55 is highly acetylated on K50. Expression of wild-type and the K50R acetylation-deficient mutant of GRASP55, but not the K50Qacetylation-mimetic mutant, inGRASP55 and GRASP65 (also known as GORASP1) double-knockout cells, rescued the Golgi structure and post-mitotic Golgi reassembly. Acetylation-deficient GRASP55 exhibited a higher self-interaction efficiency, a property required for Golgi structure formation. These results demonstrate that SIRT2 regulates Golgi structure bymodulating GRASP55 acetylation levels.
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