ArticleProceedings of the National Academy of Sciences of the United States of America2008
The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 45 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
45 citing papers in PubMed, 76 citations in OpenAlex.
- MYO5A-mediated stabilization promotes the acquisition of fusion competence in sealed autophagosomes.The EMBO journal · 2026Article
- Article
- Autoinhibition and activation mechanisms revealed by the triangular-shaped structure of myosin Va.Science advances · 2022Article
- Mitochondria-associated myosin 19 processively transports mitochondria on actin tracks in living cells.The Journal of biological chemistry · 2022Article
- Human deafness-associated variants alter the dynamics of key molecules in hair cell stereocilia F-actin cores.Human genetics · 2022Review
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Effects of Mutations in the Phenamacril-Binding Site ofACS omega · 2020Article
- Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- The cargo adaptor proteins RILPL2 and melanophilin co-regulate myosin-5a motor activity.The Journal of biological chemistry · 2019Article
- Regulation of Myosin-5b by Rab11a and the Rab11 family interacting protein 2.Bioscience reports · 2019Article
- Myosin-Driven Intracellular Transport.Cold Spring Harbor perspectives in biology · 2018Review
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- Human myosin VIIa is a very slow processive motor protein on various cellular actin structures.The Journal of biological chemistry · 2017Article
- The molecular motor Myosin Va interacts with the cilia-centrosomal protein RPGRIP1L.Scientific reports · 2017Article
- Calmodulin in complex with the first IQ motif of myosin-5a functions as an intact calcium sensor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Coordinated recruitment of Spir actin nucleators and myosin V motors to Rab11 vesicle membranes.eLife · 2016Article
- The Globular Tail Domain of Myosin-5a Functions as a Dimer in Regulating the Motor Activity.The Journal of biological chemistry · 2016Article
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
- Identification of the Isoform-specific Interactions between the Tail and the Head of Class V Myosin.The Journal of biological chemistry · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Myosin Va is a well known processive motor involved in transport of organelles. A tail-inhibition model is generally accepted for the regulation of myosin Va: inhibited myosin Va is in a folded conformation such that the tail domain interacts with and inhibits myosin Va motor activity. Recent studies indicate that it is the C-terminal globular tail domain (GTD) that directly inhibits the motor activity of myosin Va. In the present study, we identified a conserved acidic residue in the motor domain (Asp-136) and two conserved basic residues in the GTD (Lys-1706 and Lys-1779) as critical residues for this regulation. Alanine mutations of these conserved charged residues not only abolished the inhibition of motor activity by the GTD but also prevented myosin Va from forming a folded conformation. We propose that Asp-136 forms ionic interactions with Lys-1706 and Lys-1779. This assignment locates the GTD-binding site in a pocket of the motor domain, formed by the N-terminal domain, converter, and the calmodulin in the first IQ motif. We propose that binding of the GTD to the motor domain prevents the movement of the converter/lever arm during ATP hydrolysis cycle, thus inhibiting the chemical cycle of the motor domain.
Indexed as
Identifiers
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.