期刊
JOURNAL OF CELL BIOLOGY
卷 186, 期 2, 页码 193-200出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200905016
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资金
- National Science Foundation [MCB0444291, MCB049958P]
- Pittsburgh Supercomputer Center
- Association for International Cancer Research [AICR06-613]
- National Institutes of Health [GM080587]
Actin, a major component of the cytoplasm, is also abundant in the nucleus. Nuclear actin is involved in a variety of nuclear processes including transcription, chromatin remodeling, and intranuclear transport. Nevertheless, the regulation of nuclear actin by posttranslational modifications has not been investigated. We now show that nuclear actin is modified by SUMO2 and SUMO3 and that computational modeling and site-directed mutagenesis identified K68 and K284 as critical sites for SUMOylating actin. We also present a model for the actin-SUMO complex and show that SUMOylation is required for the nuclear localization of actin.
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