期刊
CELL
卷 138, 期 3, 页码 537-548出版社
CELL PRESS
DOI: 10.1016/j.cell.2009.05.030
关键词
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资金
- Research Grants Council of Hong Kong [HKUST6419/05M, 6442/06M, 663407, 663808, CA07/08.SC01, AoE/B-15/01-II, 660708, PolyU5641/08M]
- Hong Kong Jockey Club
Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.
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