UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae

Chia Wen Ho, Hung Ta Chen, Jaulang Hwang

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)21826-21834
Number of pages9
JournalJournal of Biological Chemistry
Issue number24
Publication statusPublished - Jun 17 2011
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology


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