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

doi:10.1083/jcb.147.4.791

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Article

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

The Journal of cell biology - 15 Nov 1999

Schott D, Ho J, Pruyne D, Bretscher A

Abstract excerpt

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...

Topics

Alleles
Amino Acid Sequence
Amino Acid Substitution
Animals
Cell Polarity
Consensus Sequence
Cytoplasmic Granules
Dictyostelium
Evolution, Molecular
Fungal Proteins
Genotype

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutagenesis, Site-Directed

Myosin Heavy Chains

Myosin Type II

Myosin Type V

Myosins

Phylogeny

Source

Open in PubMed Open full text

Identifiers

PMID: 10562281
DOI: 10.1083/jcb.147.4.791
PMCID: PMC2156159

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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The COOH-terminal domain of Myo2p, a yeast myosin V, has a direct role in secretory vesicle targeting.PMID 10562281Read ↗

The tail of a yeast class V myosin, myo2p, functions as a localization domain.Semantic proximity Read ↗

Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes.Semantic proximity Read ↗

The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles.Semantic proximity Read ↗

Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae.Semantic proximity Read ↗

Regulated phosphorylation of budding yeast's essential myosin V heavy chain, Myo2p.Semantic proximity Read ↗

Head-to-tail regulation is critical for the in vivo function of myosin V.Semantic proximity Read ↗

Myosin V attachment to cargo requires the tight association of two functional subdomains.Semantic proximity Read ↗

The yeast kinesin-related protein Smy1p exerts its effects on the class V myosin Myo2p via a physical interaction.Semantic proximity Read ↗

Myosin-V is activated by binding secretory cargo and released in coordination with Rab/exocyst function.Semantic proximity Read ↗

Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p.Semantic proximity Read ↗

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