UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae

Chia Wen Ho, Hung Ta Chen, Jaulang Hwang

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

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
Volume286
Issue number24
DOIs
Publication statusPublished - Jun 17 2011
Externally publishedYes

Fingerprint

Septins
Sumoylation
Yeast
Machinery
Saccharomyces cerevisiae
Enzymes
Lysine
Cells
Mutation
Cytoskeletal Proteins
Substrates
Cell Cycle
Proteins
Yeasts

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae. / Ho, Chia Wen; Chen, Hung Ta; Hwang, Jaulang.

In: Journal of Biological Chemistry, Vol. 286, No. 24, 17.06.2011, p. 21826-21834.

Research output: Contribution to journalArticle

Ho, Chia Wen ; Chen, Hung Ta ; Hwang, Jaulang. / UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae. In: Journal of Biological Chemistry. 2011 ; Vol. 286, No. 24. pp. 21826-21834.
@article{6b1fcdaa5fb140b8837f9f3a070782fb,
title = "UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae",
abstract = "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.",
author = "Ho, {Chia Wen} and Chen, {Hung Ta} and Jaulang Hwang",
year = "2011",
month = "6",
day = "17",
doi = "10.1074/jbc.M111.234914",
language = "English",
volume = "286",
pages = "21826--21834",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "24",

}

TY - JOUR

T1 - UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae

AU - Ho, Chia Wen

AU - Chen, Hung Ta

AU - Hwang, Jaulang

PY - 2011/6/17

Y1 - 2011/6/17

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=79958753032&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79958753032&partnerID=8YFLogxK

U2 - 10.1074/jbc.M111.234914

DO - 10.1074/jbc.M111.234914

M3 - Article

VL - 286

SP - 21826

EP - 21834

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 24

ER -