Sumoylation
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Accession number;05A0630946
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| Title;Sumoylation |
| Author;
KIKUCHI YOSHIKO
(Univ. Tokyo, Graduate School of Sci., JPN)
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Journal Title;Seikagaku
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Journal Code:G0184A
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ISSN:0037-1017
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VOL.77;NO.6;PAGE.545-551(2005)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;SUMO, a ubiquitin-like protein, is a protein modifier that reversibly binds with a target protein as ubiquitin does. As SUMO-modifications of proteins involved in intranuclear transportation, transcription control, chromosome separation, and the like have been reported one after another, SUMO-modifications have been noted for their importance in control mechanism. SUMO pathway involves factors similar to ubiquitinase but is independent from the ubiquitination pathway. As SUMO ligase closest to the substrate was identified recently, it has become possible to analyze the control mechanism by SUMO-modification. A target protein bound with SUMO obtains new functions; it is altered in localization and affinity to DNA or binds with a new factor. In addition, there are cases where SUNO-modification competes with ubiquitination and acetylation, contributes to the stabilization of a target protein, or plays a role in controlling a switch for functional changes. (Author's abstract). |
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