Ste20-kinase-dependent TEDS-site phosphorylation modulates the dynamic localisation and endocytic function of the fission yeast class I myosin, Myo1

Attanapola, Sheran L. and Alexander, Christopher J. and Mulvihill, Daniel P. (2009) Ste20-kinase-dependent TEDS-site phosphorylation modulates the dynamic localisation and endocytic function of the fission yeast class I myosin, Myo1. Journal of Cell Science, 122 (21). pp. 3856-3861. 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.053959

Abstract

Type I myosins are monomeric motors involved in a range of motile and sensory activities in different cell types. In simple unicellular eukaryotes, motor activity of class I myosins is regulated by phosphorylation of a conserved 'TEDS site' residue within the motor domain. The mechanism by which this phosphorylation event affects the cellular function of each myosin I remains unclear. The fission yeast myosin I, Myo1, activates Arp2/3-dependent polymerisation of cortical actin patches and also regulates endocytosis. Using mutants and Myo1-specific antibodies, we show that the phosphorylation of the Myo1 TEDS site (serine 361) plays a crucial role in regulating this protein's dynamic localisation and cellular function. We conclude that although phosphorylation of serine 361 does not affect the ability of this motor protein to promote actin polymerisation, it is required for Myo1 to recruit to sites of endocytosis and function during this process.

Item Type: Article
Uncontrolled keywords: Schizosaccharomyces pombe, Type I myosin, TEDS site, Endocytosis, Myo1, Fission yeast
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 > Cell & Developmental Biology Group
Depositing User: Dan Mulvihill
Date Deposited: 26 Oct 2009 15:48
Last Modified: 08 Apr 2014 13:43
Resource URI: http://kar.kent.ac.uk/id/eprint/23029 (The current URI for this page, for reference purposes)
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