An additional role for SUMO in ubiquitin-mediated proteolysis

Marie-Claude Geoffroy; Ronald T. Hay

doi:10.1038/nrm2707

An additional role for SUMO in ubiquitin-mediated proteolysis

Marie-Claude Geoffroy, Ronald T. Hay

Research output: Contribution to journal › Review article › peer-review

226 Citations (Scopus)

Abstract

Although the post-translational modification of proteins with small ubiquitin-like modifier (SUMO) has a role in many biological processes, it was thought that SUMO, unlike ubiquitin, does not target proteins for degradation. However, these views need to be revised, as recent findings in yeast and human cells indicate that SUMO can act as a signal for the recruitment of E3 ubiquitin ligases, which leads to the ubiquitylation and degradation of the modified protein.

Original language	English
Pages (from-to)	564-568
Number of pages	5
Journal	Nature Reviews Molecular Cell Biology
Volume	10
Issue number	8
DOIs	https://doi.org/10.1038/nrm2707
Publication status	Published - Aug 2009

Keywords

ACUTE PROMYELOCYTIC LEUKEMIA
TRIOXIDE-INDUCED APOPTOSIS
NUCLEAR-PORE COMPLEX
RAR-ALPHA
SACCHAROMYCES-CEREVISIAE
IN-VITRO
PML
PROTEIN
RNF4
LIGASE

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title = "An additional role for SUMO in ubiquitin-mediated proteolysis",

abstract = "Although the post-translational modification of proteins with small ubiquitin-like modifier (SUMO) has a role in many biological processes, it was thought that SUMO, unlike ubiquitin, does not target proteins for degradation. However, these views need to be revised, as recent findings in yeast and human cells indicate that SUMO can act as a signal for the recruitment of E3 ubiquitin ligases, which leads to the ubiquitylation and degradation of the modified protein.",

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author = "Marie-Claude Geoffroy and Hay, {Ronald T.}",

year = "2009",

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doi = "10.1038/nrm2707",

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AU - Geoffroy, Marie-Claude

AU - Hay, Ronald T.

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N2 - Although the post-translational modification of proteins with small ubiquitin-like modifier (SUMO) has a role in many biological processes, it was thought that SUMO, unlike ubiquitin, does not target proteins for degradation. However, these views need to be revised, as recent findings in yeast and human cells indicate that SUMO can act as a signal for the recruitment of E3 ubiquitin ligases, which leads to the ubiquitylation and degradation of the modified protein.

AB - Although the post-translational modification of proteins with small ubiquitin-like modifier (SUMO) has a role in many biological processes, it was thought that SUMO, unlike ubiquitin, does not target proteins for degradation. However, these views need to be revised, as recent findings in yeast and human cells indicate that SUMO can act as a signal for the recruitment of E3 ubiquitin ligases, which leads to the ubiquitylation and degradation of the modified protein.

KW - ACUTE PROMYELOCYTIC LEUKEMIA

KW - TRIOXIDE-INDUCED APOPTOSIS

KW - NUCLEAR-PORE COMPLEX

KW - RAR-ALPHA

KW - SACCHAROMYCES-CEREVISIAE

KW - IN-VITRO

KW - PML

KW - PROTEIN

KW - RNF4

KW - LIGASE

U2 - 10.1038/nrm2707

DO - 10.1038/nrm2707

M3 - Review article

C2 - 19474794

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SP - 564

EP - 568

JO - Nature Reviews Molecular Cell Biology

JF - Nature Reviews Molecular Cell Biology

IS - 8

ER -

An additional role for SUMO in ubiquitin-mediated proteolysis

Abstract

Keywords

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