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  Functional characterization of the N-terminal region of myosin-2

Fujita-Becker, S., Tsiavaliaris, G., Ohkura, R., Shimada, T., Manstein, D. J., & Sutoh, K. (2006). Functional characterization of the N-terminal region of myosin-2. The Journal of Biological Chemistry, 281(47), 36102-36109. doi:10.1074/jbc.M605171200.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-DDFB-C Version Permalink: http://hdl.handle.net/21.11116/0000-0001-DDFC-B
Genre: Journal Article

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JBiolChem_281_2006_36102.pdf (Any fulltext), 440KB
 
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 Creators:
Fujita-Becker, Setsuko1, Author              
Tsiavaliaris, Georgios1, Author              
Ohkura, Reiko, Author
Shimada, Takashi, Author
Manstein, Dietmar J.1, Author              
Sutoh, Kazuo, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: All class 2 myosins contain an N-terminal extension of approximately 80 residues that includes an Src homology 3 (SH3)-like subdomain. To explore the functional importance of this region, which is also present in most other myosin classes, we generated truncated constructs of Dictyostelium discoideum myosin-2. Truncation at position 80 resulted in the complete loss of myosin-2 function in vivo. Actin affinity was more than 80-fold, and the rate of ADP release approximately 40-fold decreased in this mutant. In contrast, a myosin construct that lacks only the SH3-like subdomain, corresponding to residues 33-79, displayed much smaller functional defects. In complementation experiments with myosin-2 null cells, this construct rescued myosin-2-dependent processes such as cytokinesis, fruiting body formation, and sporogenesis. An 8-fold reduction in motile activity and changes of similar extent in the affinity for ADP and filamentous actin indicate the importance of the SH3-like subdomain for correct communication between the functional regions within the myosin motor domain and suggest that local perturbations in this region can play a role in modulating myosin-2 motor activity.

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Language(s): eng - English
 Dates: 2006-08-252006-05-302006-09-172006-11-24
 Publication Status: Published in print
 Pages: 8
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 Table of Contents: -
 Rev. Method: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 281 (47) Sequence Number: - Start / End Page: 36102 - 36109 Identifier: ISSN: 0021-9258
CoNE: /journals/resource/954925410826_1