Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis

Durrwang, Ulrike and Fujita-Becker, Setsuko and Erent, Muriel and Kull, F. Jon and Tsiavaliaris, Georgios and Geeves, Michael A. and Manstein, Dietmar J. (2006) Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis. Journal of Cell Science, 119 (Pt 3). pp. 550-58. ISSN 0021-9533. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Class I myosins are single-headed motor proteins, implicated in various motile processes including organelle translocation, ion-channel gating, and cytoskeleton reorganization. Here we describe the cellular localization of myosin-IE and its role in the phagocytic uptake of solid particles and cells. A complete analysis of the kinetic and motor properties of Dictyostelium discoideum myosin-IE was achieved by the use of motor domain constructs with artificial lever arms. Class I myosins belonging to subclass IC like myosin-IE are thought to be tuned for tension maintenance or stress sensing. In contrast to this prediction, our results show myosin-IE to be a fast motor. Myosin-IE motor activity is regulated by myosin heavy chain phosphorylation, which increases the coupling efficiency between the actin and nucleotide binding sites tenfold and the motile activity more than fivefold. Changes in the level of free Mg(2+) ions, which are within the physiological range, are shown to modulate the motor activity of myosin-IE by inhibiting the release of adenosine diphosphate.

Item Type: Article
Additional information: 0021-9533 (Print) Journal Article
Uncontrolled keywords: Adenosine Diphosphate/metabolism Animals Dictyostelium/cytology/genetics/*metabolism Magnesium/metabolism Myosin Type I/genetics/*metabolism Phagocytosis/*physiology Phosphorylation Protein Processing, Post-Translational/physiology Research Support, Non-U.S. Gov't
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Michael Geeves
Date Deposited: 16 Mar 2009 16:28
Last Modified: 28 Apr 2014 14:09
Resource URI: https://kar.kent.ac.uk/id/eprint/13211 (The current URI for this page, for reference purposes)
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