ArticleScientific reports2015
Melanophilin Stimulates Myosin-5a Motor Function by Allosterically Inhibiting the Interaction between the Head and Tail of Myosin-5a.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 34 citations in OpenAlex.
- Determination of Dissociation Constants for the Interaction of Myosin-5a with its Cargo Protein Using Microscale Thermophoresis (MST).Bio-protocol · 2025Article
- Article
- DietaryFrontiers in immunology · 2023Article
- Autoinhibition and activation mechanisms revealed by the triangular-shaped structure of myosin Va.Science advances · 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
- 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
- Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.Small GTPases · 2018Review
- Myosin-Driven Intracellular Transport.Cold Spring Harbor perspectives in biology · 2018Review
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- Myosin Va's adaptor protein melanophilin enforces track selection on the microtubule and actin networks in vitro.Proceedings of the National Academy of Sciences of the United States of America · 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
- Identification of the Isoform-specific Interactions between the Tail and the Head of Class V Myosin.The Journal of biological chemistry · 2016Article
- Dynamic multimerization of Dab2-Myosin VI complexes regulates cargo processivity while minimizing cortical actin reorganization.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tail-inhibition model is generally accepted for the regulation of myosin-5a motor function. Inhibited myosin-5a is in a folded conformation in which its globular tail domain (GTD) interacts with its head and inhibits its motor function, and high Ca(2+) or cargo binding may reduce the interaction between the GTD and the head of myosin-5a, thus activating motor activity. Although it is well established that myosin-5a motor function is regulated by Ca(2+), little is known about the effects of cargo binding. We previously reported that melanophilin (Mlph), a myosin-5a cargo-binding protein, is capable of activating myosin-5a motor function. Here, we report that Mlph-GTBDP, a 26 amino-acid-long peptide of Mlph, is sufficient for activating myosin-5a motor function. We demonstrate that Mlph-GTBDP abolishes the interaction between the head and GTD of myosin-5a, thereby inducing a folded-to-extended conformation transition for myosin-5a and activating its motor function. Mutagenesis of the GTD shows that the GTD uses two distinct, non-overlapping regions to interact with Mlph-GTBDP and the head of myosin-5a. We propose that the GTD is an allosteric protein and that Mlph allosterically inhibits the interaction between the GTD and head of myosin-5a, thereby activating myosin-5a motor function.
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.