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Article

Myosin V attachment to cargo requires the tight association of two functional subdomains.

The Journal of cell biology - 31 Jan 2005

Pashkova Natasha, Catlett Natalie L, Novak Jennifer L, Wu Guanming, Lu Renne, Cohen Robert E, Weisman Lois S

Abstract excerpt

The myosin V carboxyl-terminal globular tail domain is essential for the attachment of myosin V to all known cargoes. Previously, the globular tail was viewed as a single, functional entity. Here, we show that the globular tail of the yeast myosin Va homologue, Myo2p, contains two structural subdomains that have distinct functions, namely, vacuole-specific and secretory vesicle-specific movement. Biochemical and...

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Share to Cytoplasmic Vesicles
Share to Myosin Heavy Chains

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Myosin Type V

Share to Secretory Vesicles

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Share to Two-Hybrid System Techniques

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Source

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Identifiers

PMID: 15684027
DOI: 10.1083/jcb.200407146
PMCID: PMC2171732

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Myosin V attachment to cargo requires the tight association of two functional subdomains.PMID 15684027Read ↗

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

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

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

Structural basis of cargo recognitions for class V myosins.Semantic proximity Read ↗

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

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

Kinesin-related Smy1 enhances the Rab-dependent association of myosin-V with secretory cargo.Semantic proximity Read ↗

Direct interaction between a myosin V motor and the Rab GTPases Ypt31/32 is required for polarized secretion.Semantic proximity Read ↗

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

Beyond Static Tethering at Membrane Contact Sites: Structural Dynamics and Functional Implications of VAP ProteinsSemantic proximity Read ↗

Complex formation with Ypt11p, a rab-type small GTPase, is essential to facilitate the function of Myo2p, a class V myosin, in mitochondrial distribution in Saccharomyces cerevisiae.Semantic proximity Read ↗

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