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Student Authors
Minakshi GuhaUMass Chan Affiliations
Department of PhysiologyDocument Type
Journal ArticlePublication Date
2005-04-28Keywords
Actins; Animals; Calcium-Calmodulin-Dependent Protein Kinases; Cells, Cultured; Cytokinesis; Fluorescence Recovery After Photobleaching; Heterocyclic Compounds with 4 or More Rings; Myosin Type II; Protein Transport; Protozoan Proteins; Quinolinium Compounds; RatsCell and Developmental Biology
Life Sciences
Medicine and Health Sciences
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Show full item recordAbstract
The involvement of myosin II in cytokinesis has been demonstrated with microinjection, genetic, and pharmacological approaches; however, the exact role of myosin II in cell division remains poorly understood. To address this question, we treated dividing normal rat kidney (NRK) cells with blebbistatin, a potent inhibitor of the nonmuscle myosin II ATPase. Blebbistatin caused a strong inhibition of cytokinesis but no detectable effect on the equatorial localization of actin or myosin. However, whereas these filaments dissociated from the equator in control cells during late cytokinesis, they persisted in blebbistatin-treated cells over an extended period of time. The accumulation of equatorial actin was caused by the inhibition of actin filament turnover, as suggested by a 2-fold increase in recovery half-time after fluorescence photobleaching. Local release of blebbistatin at the equator caused localized accumulation of equatorial actin and inhibition of cytokinesis, consistent with the function of myosin II along the furrow. However, treatment of the polar region also caused a high frequency of abnormal cytokinesis, suggesting that myosin II may play a second, global role. Our observations indicate that myosin II ATPase is not required for the assembly of equatorial cortex during cytokinesis but is essential for its subsequent turnover and remodeling.Source
Curr Biol. 2005 Apr 26;15(8):732-6. Link to article on publisher's siteDOI
10.1016/j.cub.2005.03.042Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33791PubMed ID
15854905Related Resources
Link to article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.cub.2005.03.042