Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1

Martín-García, Rebeca and Mulvihill, Daniel P. (2009) Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1. Journal of Cell Science, 122 (21). pp. 3862-3872. ISSN 0021-9533 . (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1242/jcs.054460

Abstract

Coordination between microtubule and actin cytoskeletons plays a crucial role during the establishment of cell polarity. In fission yeast, the microtubule cytoskeleton regulates the distribution of actin assembly at the new growing end during the monopolar-to-bipolar growth transition. Here, we describe a novel mechanism in which a myosin V modulates the spatial coordination of proteolysis and microtubule dynamics. In cells lacking a functional copy of the class V myosin, Myo52, the plus ends of microtubules fail to undergo catastrophe on contacting the cell end and continue to grow, curling around the end of the cell. We show that this actin-associated motor regulates the efficient ubiquitin-dependent proteolysis of the Schizosaccharomyces pombe CLIP-170 homologue, Tip1. Myo52 facilitates microtubule catastrophe by enhancing Tip1 removal from the plus end of growing microtubules at the cell tips. There, Myo52 and the ubiquitin receptor, Dph1, work in concert to target Tip1 for degradation.

Item Type: Article
Additional information: Research Article
Uncontrolled keywords: CLIP-170, Dph1, Schizosaccharomyces pombe, Class V myosin, Ubiquitin-dependent proteolysis
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH426 Genetics
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Dan Mulvihill
Date Deposited: 23 Oct 2009 14:58
Last Modified: 02 Jun 2014 14:01
Resource URI: http://kar.kent.ac.uk/id/eprint/23030 (The current URI for this page, for reference purposes)
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