| Literature DB >> 11792540 |
Abstract
The past several years have seen major advances in our understanding of the mechanisms of microtubule destabilization by oncoprotein18/stathmin (Op18/stathmin) and related proteins. New structural information has clearly shown how members of the Op18/stathmin protein family bind tubulin dimers and suggests models for how these proteins stimulate catastrophe, the transition from microtubule growth to shortening. Regulation of Op18/stathmin by phosphorylation continues to capture much attention. Studies suggest that phosphorylation occurs in a localized fashion, resulting in decreased microtubule destabilizing activity near chromatin or microtubule polymer. A spatial gradient of inactive Op18/stathmin associated with chromatin or microtubules could contribute significantly to mitotic spindle assembly.Entities:
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Year: 2002 PMID: 11792540 DOI: 10.1016/s0955-0674(01)00289-7
Source DB: PubMed Journal: Curr Opin Cell Biol ISSN: 0955-0674 Impact factor: 8.382