Katanin inhibition prevents the redistribution of γ-tubulin at mitosis

DOI PDF 被引用文献2件
  • Dan Buster
    Section of Molecular and Cellular Biology, University of California,Davis, CA 95616, USA
  • Karen McNally
    Section of Molecular and Cellular Biology, University of California,Davis, CA 95616, USA
  • Francis J. McNally
    Section of Molecular and Cellular Biology, University of California,Davis, CA 95616, USA

書誌事項

公開日
2002-03-01
DOI
  • 10.1242/jcs.115.5.1083
公開者
The Company of Biologists

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説明

<jats:p>Katanin is a microtubule-severing protein that is concentrated at mitotic spindle poles but katanin's function in the mitotic spindle has not been previously reported. Inhibition of katanin with either of two dominant-negative proteins or a subunit-specific antibody prevented the redistribution of γ-tubulin from the centrosome to the spindle in prometaphase CV-1 cells as assayed by immunofluorescence microscopy. Becauseγ-tubulin complexes can bind to pre-existing microtubule minus ends,these results could be explained by a model in which the broad distribution ofγ-tubulin in the mitotic spindle is in part due to cytosolicγ-tubulin ring complexes binding to microtubule minus ends generated by katanin-mediated microtubule severing. Because microtubules depolymerize at their ends, we hypothesized that a greater number of microtubule ends generated by severing in the spindle would result in an increased rate of spindle disassembly when polymerization is blocked with nocodazole. Indeed,katanin inhibition slowed the rate of spindle microtubule disassembly in the presence of nocodazole. However, katanin inhibition did not affect the rate of exchange between polymerized and unpolymerized tubulin as assayed by fluorescence recovery after photobleaching. These results support a model in which katanin activity regulates the number of microtubule ends in the spindle.</jats:p>

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