PMID:16982629

Citation	Fujita-Becker, S, Tsiavaliaris, G, Ohkura, R, Shimada, T, Manstein, DJ and Sutoh, K (2006) Functional characterization of the N-terminal region of myosin-2. J. Biol. Chem. 281:36102-9
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.
Links	PubMed Online version:10.1074/jbc.M605171200
Keywords	Actins/chemistry; Adenosine Diphosphate/chemistry; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Animals; Cytokinesis; Dictyostelium/metabolism; Genetic Complementation Test; Molecular Sequence Data; Myosin Type II/chemistry; Myosin Type II/metabolism; Myosins/chemistry; Protein Structure, Tertiary; Sequence Homology, Amino Acid; src Homology Domains
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