Journal
EMBO JOURNAL
Volume 25, Issue 4, Pages 693-700Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.emboj.7600965
Keywords
cargo-binding domain; membrane transport; myosin V; Myo2p
Categories
Funding
- NIGMS NIH HHS [GM62261, GM62904, R01 GM062904, R01 GM062261, R37 GM062261] Funding Source: Medline
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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 angstrom 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.
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