Format

Send to

Choose Destination
See comment in PubMed Commons below
Cell Mol Life Sci. 2007 Dec;64(23):3017-33.

Sumoylation regulates diverse biological processes.

Author information

1
Center for Cell Biology and Cancer Research, Albany Medical College, 47 New Scotland Avenue, MC-165, Albany, New York 12208, USA. zhaojh@mail.amc.edu

Abstract

Ten years after its discovery, the small ubiquitin-like protein modifier (SUMO) has emerged as a key regulator of proteins. While early studies indicated that sumoylation takes place mainly in the nucleus, an increasing number of non-nuclear substrates have recently been identified, suggesting a wider stage for sumoylation in the cell. Unlike ubiquitylation, which primarily targets a substrate for degradation, sumoylation regulates a substrate's functions mainly by altering the intracellular localization, protein-protein interactions or other types of post-translational modifications. These changes in turn affect gene expression, genomic and chromosomal stability and integrity, and signal transduction. Sumoylation is counter-balanced by desumoylation, and well-balanced sumoylation is essential for normal cellular behaviors. Loss of the balance has been associated with a number of diseases. This paper reviews recent progress in the study of SUMO pathways, substrates, and cellular functions and highlights important findings that have accelerated advances in this study field and link sumoylation to human diseases.

PMID:
17763827
DOI:
10.1007/s00018-007-7137-4
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center