Myosin VI Undergoes Cargo-Mediated Dimerization

Cong Yu, Wei Feng, Zhiyi Wei, Yohei Miyanoiri, Wenyu Wen, Yanxiang Zhao, Mingjie Zhang

Research output: Journal article publicationJournal articleAcademic researchpeer-review

108 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)537-548
Number of pages12
Issue number3
Publication statusPublished - 7 Aug 2009



ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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