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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons92982

Fujita-Becker,  Setsuko
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95711

Tsiavaliaris,  Georgios
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons94215

Manstein,  Dietmar J.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-9A3F-F
Abstract
All class 2 myosins contain an N−terminal extension of 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 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 forADPand 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