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• W2059607522 startingPage "693" @default.
• W2059607522 abstract "Myosin V molecular motors move cargoes on actin filaments. A myosin V may move multiple cargoes to distinct places at different times. The cargoes attach to the globular tail of myosin V via cargo-specific receptors. Here we report the crystal structure at 2.2 A of the myosin V globular tail. The overall tertiary structure has not been previously observed. There are several patches of highly conserved regions distributed on the surface of the tail. These are candidate attachment sites for cargo-specific receptors. Indeed, we identified a region of five conserved surface residues that are solely required for vacuole inheritance. Likewise, we identified a region of five conserved surface residues that are required for secretory vesicle movement, but not vacuole movement. These two regions are at opposite ends of the oblong-shaped cargo-binding domain, and moreover are offset by 180 degrees. The fact that the cargo-binding areas are distant from each other and simultaneously exposed on the surface of the globular tail suggests that major targets for the regulation of cargo attachment are organelle-specific myosin V receptors." @default.
• W2059607522 created "2016-06-24" @default.
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• W2059607522 creator A5066989398 @default.
• W2059607522 creator A5081220025 @default.
• W2059607522 date "2006-01-26" @default.
• W2059607522 modified "2023-09-24" @default.
• W2059607522 title "Structural basis for myosin V discrimination between distinct cargoes" @default.
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• W2059607522 doi "https://doi.org/10.1038/sj.emboj.7600965" @default.
• W2059607522 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1383548" @default.
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• W2059607522 hasPublicationYear "2006" @default.
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