In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain

Grallert, Agnes and Martín-García, Rebeca and Bagley, Steve and Mulvihill, Daniel P. (2007) In vivo movement of the type V myosin Myo52 requires dimerisation but is independent of the neck domain. Journal of Cell Science, 120 (23). pp. 4093-4098. ISSN 0021-9533 . (The full text of this publication is not available from this repository)

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Abstract

Intracellular movement is a fundamental property of all cell types. Many organelles and molecules are actively transported throughout the cytoplasm by molecular motors, such as the dimeric type V myosins. These possess a long neck, which contains an IQ motif, that allow it to make 36-nm steps along the actin polymer. Live cell imaging of the fission yeast type V myosin Myo52 reveals that the protein moves rapidly throughout the cytoplasm. Here, we describe analysis of this movement and have established that Myo52 moves long distances on actin filaments in an ATP-dependent manner at approximately 0.5 mum/second. Myo51 and the microtubule cytoskeleton have no discernable role in modulating Myo52 movements, whereas rigour mutations in Myo52 abrogated its movement. We go on to show that, although dimerisation is required for Myo52 movement, deleting its neck has no discernable affect on Myo52 function or velocity in vivo.

Item Type: Article
Additional information: 0021-9533 (Print) Journal Article
Uncontrolled keywords: Schizosaccharomyces pombe; myosin V; IQ domains
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Cell & Developmental Biology Group
Depositing User: Dan Mulvihill
Date Deposited: 08 Jul 2008 13:05
Last Modified: 02 Jun 2014 14:01
Resource URI: http://kar.kent.ac.uk/id/eprint/6071 (The current URI for this page, for reference purposes)
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