ArticlePloS one2013
Structural insights into the globular tails of the human type v myosins Myo5a, Myo5b, And Myo5c.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Comprehensive Analysis of SLC17A9 and Its Prognostic Value in Hepatocellular Carcinoma.Frontiers in oncology · 2022Article
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Integrated miRNA-mRNA transcriptomic analysis reveals epigenetic-mediated embryonic muscle growth differences between Wuzhishan and Landrace pigs1.Journal of animal science · 2019Article
- MYO5B, STX3, and STXBP2 mutations reveal a common disease mechanism that unifies a subset of congenital diarrheal disorders: A mutation update.Human mutation · 2018Review
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- Loss of Myosin Vb in colorectal cancer is a strong prognostic factor for disease recurrence.British journal of cancer · 2017Article
- Crystal structure of Sec10, a subunit of the exocyst complex.Scientific reports · 2017Article
- The Globular Tail Domain of Myosin-5a Functions as a Dimer in Regulating the Motor Activity.The Journal of biological chemistry · 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
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vertebrate type V myosins (MyoV) Myo5a, Myo5b, and Myo5c mediate transport of several different cargoes. All MyoV paralogs bind to cargo complexes mainly by their C-terminal globular domains. In absence of cargo, the globular domain of Myo5a inhibits its motor domain. Here, we report low-resolution SAXS models for the globular domains from human Myo5a, Myo5b, and Myo5c, which suggest very similar overall shapes of all three paralogs. We determined the crystal structures of globular domains from Myo5a and Myo5b, and provide a homology model for human Myo5c. When we docked the Myo5a crystal structure into a previously published electron microscopy density of the autoinhibited full-length Myo5a, only one domain orientation resulted in a good fit. This structural arrangement suggests the participation of additional region of the globular domain in autoinhibition. Quantification of the interaction of the Myo5a globular domain with its motor complex revealed a tight binding with dissociation half-life in the order of minutes, suggesting a rather slow transition between the active and inactive states.
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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.