The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting.

ABSTRACT: MYO2 encodes a type V myosin heavy chain needed for the targeting of vacuoles and secretory vesicles to the growing bud of yeast. Here we describe new myo2 alleles containing conditional lethal mutations in the COOH-terminal tail domain. Within 5 min of shifting to the restrictive temperature, the polarized distribution of secretory vesicles is abolished without affecting the distribution of actin or the mutant Myo2p, showing that the tail has a direct role in vesicle targeting. We also show that the actin cable-dependent translocation of Myo2p to growth sites does not require secretory vesicle cargo. Although a fusion protein containing the Myo2p tail also concentrates at growth sites, this accumulation depends on the polarized delivery of secretory vesicles, implying that the Myo2p tail

SUBMITTER: Schott D 

PROVIDER: S-EPMC2156159 | biostudies-literature | 1999 Nov

REPOSITORIES: biostudies-literature