Nature Cell Biology7, 235 - 245 (2005)
Published online: 20 February 2005; | doi:10.1038/ncb1222
Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase
Vito Mennella1, Gregory C. Rogers1, Stephen L. Rogers2, Daniel W. Buster1, Ronald D. Vale2
& David J. Sharp1
1
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
2
Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, California 94107, USA.
Regulation of microtubule polymerization and depolymerization is required for proper cell development. Here, we report that two proteins of the Drosophila melanogaster kinesin-13 family, KLP10A and KLP59C, cooperate to drive microtubule depolymerization in interphase cells. Analyses of microtubule dynamics in S2 cells depleted of these proteins indicate that both proteins stimulate depolymerization, but alter distinct parameters of dynamic instability; KLP10A stimulates catastrophe (a switch from growth to shrinkage) whereas KLP59C suppresses rescue (a switch from shrinkage to growth). Moreover, immunofluorescence and live analyses of cells expressing tagged kinesins reveal that KLP10A and KLP59C target to polymerizing and depolymerizing microtubule plus ends, respectively. Our data also suggest that KLP10A is deposited on microtubules by the plus-end tracking protein, EB1. Our findings support a model in which these two members of the kinesin-13 family divide the labour of microtubule depolymerization.
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