The oncoprotein 18/stathmin family of microtubule destabilizers.
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.
Cassimeris
Lynne
L
Department of Biological Sciences, 111 Research Drive, Lehigh University, Bethlehem, PA18015, USA. lc07@lehigh.edu
D000818:Animals; D006801:Humans; D008868:Microtubule Proteins; D008870:Microtubules / Q000378:metabolism*; D008958:Models, Molecular; D010063:Ovum / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry / Q000502:physiology*; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D050777:Stathmin; D014404:Tubulin / Q000378:metabolism
D008868:Microtubule Proteins; D010750:Phosphoproteins; C493995:STMN1 protein, human; D050777:Stathmin; D014404:Tubulin