ArticleProceedings of the National Academy of Sciences of the United States of America1998
The terminal tail region of a yeast myosin-V mediates its attachment to vacuole membranes and sites of polarized growth.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 138 citations in OpenAlex.
- Cargo adaptors use a handhold mechanism to engage with myosin V for organelle transport.The Journal of cell biology · 2025Article
- Actin- and microtubule-based motors contribute to clathrin-independent endocytosis in yeast.Molecular biology of the cell · 2023Article
- Bur1 functions with TORC1 for vacuole-mediated cell cycle progression.EMBO reports · 2022Article
- Let it go: mechanisms that detach myosin V from the yeast vacuole.Current genetics · 2021Review
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Cargo Release from Myosin V Requires the Convergence of Parallel Pathways that Phosphorylate and Ubiquitylate the Cargo Adaptor.Current biology : CB · 2020Article
- Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables.Molecular biology of the cell · 2018Article
- The tail domain of theJournal of cell science · 2018Article
- Fusion, fission, and transport control asymmetric inheritance of mitochondria and protein aggregates.The Journal of cell biology · 2017Article
- Live-cell single-molecule labeling and analysis of myosin motors with quantum dots.Molecular biology of the cell · 2017Article
- Review
- Article
- Coupling of two non-processive myosin 5c dimers enables processive stepping along actin filaments.Scientific reports · 2014Article
- Yeast vacuoles fragment in an asymmetrical two-phase process with distinct protein requirements.Molecular biology of the cell · 2012Article
- Overlap of cargo binding sites on myosin V coordinates the inheritance of diverse cargoes.The Journal of cell biology · 2012Article
- Article
- The myosin-related motor protein Myo2 is an essential mediator of bud-directed mitochondrial movement in yeast.The Journal of cell biology · 2011Article
- Yeast homologues of lethal giant larvae and type V myosin cooperate in the regulation of Rab-dependent vesicle clustering and polarized exocytosis.Molecular biology of the cell · 2011Article
- Molecular mechanisms of organelle inheritance: lessons from peroxisomes in yeast.Nature reviews. Molecular cell biology · 2010Review
- A nonprocessive class V myosin drives cargo processively when a kinesin- related protein is a passenger.Current biology : CB · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae myosin-V, Myo2p, has been implicated in the polarized movement of several organelles and is essential for yeast viability. We have shown previously that Myo2p is required for the movement of a portion of the lysosome (vacuole) into the bud and consequently for proper inheritance of this organelle during cell division. Class V myosins have a globular carboxyl terminal tail domain that is proposed to mediate localization of the myosin, possibly through interaction with organelle-specific receptors. Here we describe a myo2 allele whose phenotypes support this hypothesis. vac15-1/myo2-2 has a single mutation in this globular tail domain, causing defects in vacuole movement and inheritance. Although a portion of wild-type Myo2p fractionates with the vacuole, the myo2-2 gene product does not. In addition, the mutant protein does not concentrate at sites of active growth, the predominant location of wild-type Myo2p. Although deletion of the tail domain is lethal, the myo2-2 gene product retains the essential functions of Myo2p. Moreover, myo2-2 does not cause the growth defects and lethal genetic interactions seen in myo2-66, a mutant defective in the actin-binding domain. These observations suggest that the myo2-2 mutation specifically disrupts interactions with selected myosin receptors, namely those on the vacuole membrane and those at sites of polarized growth.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.