Myosin V attachment to cargo requires the tight association of two functional subdomains.

The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdomains that have ...
distinct functions, namely, vacuole-specific and secretory vesicle-specific movement. Biochemical and genetic analyses demonstrate that subdomain I tightly associates with subdomain II, and that the interaction does not require additional proteins. Importantly, although neither subdomain alone is functional, simultaneous expression of the separate subdomains produces a functional complex in vivo. Our results suggest a model whereby intramolecular interactions between the globular tail subdomains help to coordinate the transport of multiple distinct cargoes by myosin V.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Biological Transport, Cytoplasmic Vesicles, Escherichia coli, Gene Expression, Microtubule-Associated Proteins, Models, Biological, Molecular Sequence Data, Mutation, Myosin Heavy Chains, Myosin Type V, Nuclear Proteins, Peptide Fragments, Protein Binding, Receptors, Cell Surface, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Secretory Vesicles, Transfection, Trypsin, Two-Hybrid System Techniques, Vacuoles, Vesicular Transport Proteins
J. Cell Biol.
Date: Jan. 31, 2005
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