UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae

Chia Wen Ho, Hung Ta Chen, Jaulang Hwang

研究成果: 雜誌貢獻文章同行評審

17 引文 斯高帕斯(Scopus)

摘要

Sumoylation regulates a wide range of cellular processes. However, little is known about the regulation of the SUMO machinery. In this study, we demonstrate that two lysine residues (Lys-153 and Lys-157) in the C-terminal region of the yeast E2-conjugating enzyme Ubc9 are the major and minor autosumoylation sites, respectively. Surprisingly, mutation of Lys-157 (ubc9K157R) significantly stimulates the level of Ubc9 autosumoylation at Lys-153. The functional role of Ubc9 autosumoylation is exemplified in our findings that cell cycle-dependent sumoylation of cytoskeletal septin proteins is inversely correlated with the Ubc9 autosumoylation level and that mutation of the Ubc9 autosumoylation sites results in aberrant cell morphology. Our study elucidates a regulatory mechanism that utilizes automodification of the E2 enzyme of the sumoylation machinery to control substrate sumoylation.

原文英語
頁(從 - 到)21826-21834
頁數9
期刊Journal of Biological Chemistry
286
發行號24
DOIs
出版狀態已發佈 - 六月 17 2011
對外發佈

ASJC Scopus subject areas

  • 生物化學
  • 細胞生物學
  • 分子生物學

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