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Sumoylation regulates diverse biological processes 总被引:8,自引:0,他引:8
Zhao J 《Cellular and molecular life sciences : CMLS》2007,64(23):3017-3033
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.
Received 19 March 2007; received after version 16 July 2007; accepted 1 August 2007 相似文献
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