Podosome-regulating kinesin KIF1C translocates to the cell periphery in a CLASP-dependent manner.

Nadia Efimova, Ashley Grimaldi, Alice Bachmann, Keyada Frye, Xiaodong Zhu, Alexander Feoktistov, Anne Straube, Irina Kaverina

Index: J. Cell Sci. 127(24) , 5179-88, (2014)

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Abstract

The kinesin KIF1C is known to regulate podosomes, actin-rich adhesion structures that remodel the extracellular matrix during physiological processes. Here, we show that KIF1C is a player in the podosome-inducing signaling cascade. Upon induction of podosome formation by protein kinase C (PKC), KIF1C translocation to the cell periphery intensifies and KIF1C accumulates both in the proximity of peripheral microtubules that show enrichment for the plus-tip-associated proteins CLASPs and around podosomes. Importantly, without CLASPs, both KIF1C trafficking and podosome formation are suppressed. Moreover, chimeric mitochondrially targeted CLASP2 recruits KIF1C, suggesting a transient CLASP-KIF1C association. We propose that CLASPs create preferred microtubule tracks for KIF1C to promote podosome induction downstream of PKC. © 2014. Published by The Company of Biologists Ltd.