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

Dürrwang, U., Fujita-Becker, S., Erent, M., Kull, F. J., Tsiavaliaris, G., Geeves, M. A., et al. (2006). Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis. Journal of Cell Science, 119, 550-558. doi:10.1242/jcs.02774.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-E743-F Version Permalink: http://hdl.handle.net/21.11116/0000-0001-E744-E
Genre: Journal Article

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JCellSci_119_2006_550.pdf (Any fulltext), 797KB
 
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 Creators:
Dürrwang, Ulrike1, Author              
Fujita-Becker, Setsuko1, Author              
Erent, Muriel1, Author              
Kull, F. Jon, Author
Tsiavaliaris, Georgios1, Author              
Geeves, Michael A., Author
Manstein, Dietmar J.1, Author              
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: Dictyostelium discoideum, Phagocytosis, Phosphorylation, TEDS, Mg2+ concentration
 Abstract: 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.

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Language(s): eng - English
 Dates: 2005-10-192006-02-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: Journal of Cell Science
Source Genre: Journal
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Publ. Info: Cambridge, U.K. : Co. of Biologists
Pages: - Volume / Issue: 119 Sequence Number: - Start / End Page: 550 - 558 Identifier: ISSN: 0021-9533
CoNE: /journals/resource/954925326678