The University of Southampton
University of Southampton Institutional Repository

KLP10A and KLP59C: the dynamic duo of microtubule depolymerization

KLP10A and KLP59C: the dynamic duo of microtubule depolymerization
KLP10A and KLP59C: the dynamic duo of microtubule depolymerization

Kinesin-13s are important effectors of microtubule depolymerization in cells. In a recent series of studies, we examined the roles played by kinesin-13s throughout the cell cycle in Drosophila. Our findings have revealed remarkable coordination between two family members, KLP10A and KLP59C, in which alterations in the relative targeting of these proteins allows them to participate in markedly different tasks at distinct points in the cell cycle. During mitosis, KLP10A and KLP59C function in parallel by targeting to and depolymerizing the opposite ends of kinetochore-associated microtubules, thereby driving poleward chromatid motility by a Pacman-Flux mechanism. Alternatively, during interphase, both proteins target to the same end of the microtubule but act in series to divide the labor of microtubule depolymerization. KLP10A initiates depolymerization while KLP59C perpetuates depolymerization after its initiation. Below, we detail these findings and examine some of their implications.

Animals, Drosophila Proteins/physiology, Drosophila melanogaster/cytology, Humans, Kinesin/physiology, Polymers/chemistry
1538-4101
1482-1485
Sharp, David J
0e701ea9-7d32-4884-a57c-51b927c76ba3
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Buster, Daniel W
8618c713-96b5-4bda-bc32-88cc7a793b46
Sharp, David J
0e701ea9-7d32-4884-a57c-51b927c76ba3
Mennella, Vito
43c60e29-c0a7-4ab8-8e5c-fcb59f70a28a
Buster, Daniel W
8618c713-96b5-4bda-bc32-88cc7a793b46

Sharp, David J, Mennella, Vito and Buster, Daniel W (2005) KLP10A and KLP59C: the dynamic duo of microtubule depolymerization. Cell Cycle, 4 (11), 1482-1485. (doi:10.4161/cc.4.11.2116).

Record type: Review

Abstract

Kinesin-13s are important effectors of microtubule depolymerization in cells. In a recent series of studies, we examined the roles played by kinesin-13s throughout the cell cycle in Drosophila. Our findings have revealed remarkable coordination between two family members, KLP10A and KLP59C, in which alterations in the relative targeting of these proteins allows them to participate in markedly different tasks at distinct points in the cell cycle. During mitosis, KLP10A and KLP59C function in parallel by targeting to and depolymerizing the opposite ends of kinetochore-associated microtubules, thereby driving poleward chromatid motility by a Pacman-Flux mechanism. Alternatively, during interphase, both proteins target to the same end of the microtubule but act in series to divide the labor of microtubule depolymerization. KLP10A initiates depolymerization while KLP59C perpetuates depolymerization after its initiation. Below, we detail these findings and examine some of their implications.

This record has no associated files available for download.

More information

Accepted/In Press date: 22 August 2005
Published date: November 2005
Keywords: Animals, Drosophila Proteins/physiology, Drosophila melanogaster/cytology, Humans, Kinesin/physiology, Polymers/chemistry

Identifiers

Local EPrints ID: 434035
URI: http://eprints.soton.ac.uk/id/eprint/434035
ISSN: 1538-4101
PURE UUID: 036037a5-acc6-42db-8e59-013f3a7d10b7
ORCID for Vito Mennella: ORCID iD orcid.org/0000-0002-4842-9012

Catalogue record

Date deposited: 11 Sep 2019 16:30
Last modified: 16 Mar 2024 04:04

Export record

Altmetrics

Contributors

Author: David J Sharp
Author: Vito Mennella ORCID iD
Author: Daniel W Buster

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×