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Proc Natl Acad Sci U S A
2010 Jul 06;10727:12151-6. doi: 10.1073/pnas.1004736107.
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Kinesin-1 heavy chain mediates microtubule sliding to drive changes in cell shape.
Jolly AL
,
Kim H
,
Srinivasan D
,
Lakonishok M
,
Larson AG
,
Gelfand VI
.
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Microtubules are typically observed to buckle and loop during interphase in cultured cells by an unknown mechanism. We show that lateralmicrotubule movement and looping is a result of microtubules sliding against one another in interphase Drosophila S2 cells. RNAi of the kinesin-1 heavy chain (KHC), but not dynein or the kinesin-1 light chain, eliminates these movements. KHC-dependent microtubule sliding powers the formation of cellular processes filled with parallel microtubule bundles. The growth of these cellular processes is independent of the actin cytoskeleton. We further observe cytoplasmic microtubule sliding in Xenopus and Ptk2 cells, and show that antibody inhibition of KHC in mammalian cells prevents sliding. We therefore propose that, in addition to its well established role in organelle transport, an important universal function of kinesin-1 is to mediate cytoplasmic microtubule-microtubule sliding. This provides the cell with a dedicated mechanism to transport long and short microtubule filaments and drive changes in cell shape.
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