Identification of an organelle-specific myosin V receptor.

J Cell Biol 2003 Mar;160(6):887-97

Dept. of Biochemistry, The University of Iowa, Iowa City, IA 52242, USA.

Class V myosins are widely distributed among diverse organisms and move cargo along actin filaments. Some myosin Vs move multiple types of cargo, where the timing of movement and the destinations of selected cargoes are unique. Here, we report the discovery of an organelle-specific myosin V receptor. Vac17p, a novel protein, is a component of the vacuole-specific receptor for Myo2p, a Saccharomyces cerevisiae myosin V. Vac17p interacts with the Myo2p cargo-binding domain, but not with vacuole inheritance-defective myo2 mutants that have single amino acid changes within this region. Moreover, a region of the Myo2p tail required specifically for secretory vesicle transport is neither required for vacuole inheritance nor for Vac17p-Myo2p interactions. Vac17p is localized on the vacuole membrane, and vacuole-associated Myo2p increases in proportion with an increase in Vac17p. Furthermore, Vac17p is not required for movement of other cargo moved by Myo2p. These findings demonstrate that Vac17p is a component of a vacuole-specific receptor for Myo2p. Organelle-specific receptors such as Vac17p provide a mechanism whereby a single type of myosin V can move diverse cargoes to distinct destinations at different times.

Download full-text PDF

Source
http://dx.doi.org/10.1083/jcb.200210139DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173761PMC
March 2003

Publication Analysis

Top Keywords

vacuole-specific receptor
8
myosin receptor
8
receptor myo2p
8
organelle-specific myosin
8
component vacuole-specific
8
myosin move
8
vac17p
7
myo2p
6
myosin
5
interactions vac17p
4
required secretory
4
tail required
4
region myo2p
4
myo2p tail
4
secretory vesicle
4
vesicle transport
4
vacuole inheritance
4
inheritance vac17p-myo2p
4
vac17p-myo2p interactions
4
transport required
4

Similar Publications