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PMID: 11704852 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

SUMO: of branched proteins and nuclear bodies.

Oncogene ·Vol. 20 ·No. 49 ·2001-10-29 ·Pages 7243-9

Seeler JS, Dejean A

Abstract

SUMO belongs to a growing number of ubiquitin-like proteins that covalently modify their target proteins. Although some evidence supports a role of SUMO modification in regulating protein stability, most studied examples support a model by which SUMO alters the interaction properties of its targets, often affecting their subcellular localization behavior. Examination of the PML nuclear bodies, whose principal components are SUMO-modified, has revealed this modification to be essential for their structural and functional integrity. This and other examples thus support the view that SUMO regulates the stability not of individual proteins, but rather that of entire multiprotein complexes.

MeSH Terms
Animals Antigens, Nuclear Autoantigens/metabolism Cell Nucleus Structures/metabolism DNA Virus Infections/metabolism Humans Macromolecular Substances Neoplasm Proteins/metabolism Nuclear Proteins/metabolism Organelles/metabolism Promyelocytic Leukemia Protein Protein Binding Protein Processing, Post-Translational/physiology SUMO-1 Protein/metabolism Transcription Factors/metabolism Tumor Suppressor Proteins
Chemicals
Antigens, Nuclear Autoantigens Macromolecular Substances Neoplasm Proteins Nuclear Proteins Promyelocytic Leukemia Protein SUMO-1 Protein Transcription Factors Tumor Suppressor Proteins Sp100 protein, human PML protein, human
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Seeler J S
Unité de Recombinaison et Expression Génétique, INSERM U 163, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France.
Dejean A
Article Info
Journal
Oncogene
Abbr.
Oncogene
ISSN
0950-9232
Published
2001-10-29
Pages
7243-9
Language
English
Region
England
NLM ID
8711562
Subset
IM
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