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Article

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

Molecular biology of the cell - 1 Aug 2016

Lwin Kyaw Myo, Li Donghao, Bretscher Anthony

Abstract excerpt

The mechanisms by which molecular motors associate with specific cargo is a central problem in cell organization. The kinesin-like protein Smy1 of budding yeast was originally identified by the ability of elevated levels to suppress a conditional myosin-V mutation (myo2-66), but its function with Myo2 remained mysterious. Subsequently, Myo2 was found to provide an essential role in delivery of secretory vesicles...

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

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Source

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Identifiers

PMID: 27307583
DOI: 10.1091/mbc.E16-03-0185
PMCID: PMC4966985

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

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Research trail→

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Kinesin-related Smy1 enhances the Rab-dependent association of myosin-V with secretory cargo.PMID 27307583Read ↗

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

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

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

Smy1p, a kinesin-related protein that does not require microtubules.Semantic proximity Read ↗

Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.Semantic proximity Read ↗

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

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

PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast.Semantic proximity Read ↗

Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis.Semantic proximity Read ↗

Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis.Semantic proximity Read ↗

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