ArticleThe EMBO journal2006
Structural basis for myosin V discrimination between distinct cargoes.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
73 citing papers in PubMed, 132 citations in OpenAlex.
- Cargo adaptors use a handhold mechanism to engage with myosin V for organelle transport.The Journal of cell biology · 2025Article
- Review
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- Actin- and microtubule-based motors contribute to clathrin-independent endocytosis in yeast.Molecular biology of the cell · 2023Article
- The type V myosin-containing complex HUM is a RAB11 effector powering movement of secretory vesicles.iScience · 2022Article
- Myosin-II proteins are involved in the growth, morphogenesis, and virulence of the human pathogenic fungusFrontiers in cellular and infection microbiology · 2022Article
- Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP reveals role for regulation of Vps4 ATPase.Molecular biology of the cell · 2021Article
- Type V myosin focuses the polarisome and shapes the tip of yeast cells.The Journal of cell biology · 2021Article
- Rab-E and its interaction with myosin XI are essential for polarised cell growth.The New phytologist · 2021Article
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Extranuclear Structural Components that Mediate Dynamic Chromosome Movements in Yeast Meiosis.Current biology : CB · 2020Article
- Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2.The Journal of biological chemistry · 2019Article
- Exposing the Elusive Exocyst Structure.Trends in biochemical sciences · 2018Review
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- Fusion, fission, and transport control asymmetric inheritance of mitochondria and protein aggregates.The Journal of cell biology · 2017Article
- Distinct Roles for the N- and C-terminal Regions of M-Sec in Plasma Membrane Deformation during Tunneling Nanotube Formation.Scientific reports · 2016Article
- Identification of the Isoform-specific Interactions between the Tail and the Head of Class V Myosin.The Journal of biological chemistry · 2016Article
- Melanophilin Stimulates Myosin-5a Motor Function by Allosterically Inhibiting the Interaction between the Head and Tail of Myosin-5a.Scientific reports · 2015Article
- Head-to-tail regulation is critical for the in vivo function of myosin V.The Journal of cell biology · 2015Article
- Myosin vc interacts with Rab32 and Rab38 proteins and works in the biogenesis and secretion of melanosomes.The Journal of biological chemistry · 2014Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin V molecular motors move cargoes on actin filaments. A myosin V may move multiple cargoes to distinct places at different times. The cargoes attach to the globular tail of myosin V via cargo-specific receptors. Here we report the crystal structure at 2.2 A of the myosin V globular tail. The overall tertiary structure has not been previously observed. There are several patches of highly conserved regions distributed on the surface of the tail. These are candidate attachment sites for cargo-specific receptors. Indeed, we identified a region of five conserved surface residues that are solely required for vacuole inheritance. Likewise, we identified a region of five conserved surface residues that are required for secretory vesicle movement, but not vacuole movement. These two regions are at opposite ends of the oblong-shaped cargo-binding domain, and moreover are offset by 180 degrees. The fact that the cargo-binding areas are distant from each other and simultaneously exposed on the surface of the globular tail suggests that major targets for the regulation of cargo attachment are organelle-specific myosin V receptors.
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What OpenQuestion holds
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.