ArticleScience advances2022
Autoinhibition and activation mechanisms revealed by the triangular-shaped structure of myosin Va.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Plasmodium falciparum PfMyoF contains a Rab-like tail domain and associates with perinuclear membrane trafficking proteins.Communications biology · 2026Article
- The unconventional regulation of non-muscle myosins.Biophysical reviews · 2026Article
- Research progress on the interaction mechanisms and functions between exosomes and the cytoskeleton.Frontiers in cell and developmental biology · 2026Review
- Cargo adaptors use a handhold mechanism to engage with myosin V for organelle transport.The Journal of cell biology · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Autoinhibition and relief mechanisms for MICAL monooxygenases in F-actin disassembly.Nature communications · 2024Article
- A de novo designed coiled coil-based switch regulates the microtubule motor kinesin-1.Nature chemical biology · 2024Article
- Article
- The Dilute domain in Canoe is not essential for linking cell junctions to the cytoskeleton but supports morphogenesis robustness.Journal of cell science · 2024Article
- Autoinhibition and activation of myosin VI revealed by its cryo-EM structure.Nature communications · 2024Article
- Motor properties of Myosin 5c are modulated by tropomyosin isoforms and inhibited by pentabromopseudilin.Frontiers in physiology · 2024Article
- How myosin VI traps its off-state, is activated and dimerizes.Nature communications · 2023Article
- The Dilute domain of Canoe is not essential for Canoe's role in linking adherens junctions to the cytoskeleton but contributes to robustness of morphogenesis.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As the prototype of unconventional myosin motor family, myosin Va (MyoVa) transport cellular cargos along actin filaments in diverse cellular processes. The off-duty MyoVa adopts a closed and autoinhibited state, which can be relieved by cargo binding. The molecular mechanisms governing the autoinhibition and activation of MyoVa remain unclear. Here, we report the cryo-electron microscopy structure of the two full-length, closed MyoVa heavy chains in complex with 12 calmodulin light chains at 4.78-Å resolution. The MyoVa adopts a triangular structure with multiple intra- and interpolypeptide chain interactions in establishing the closed state with cargo binding and adenosine triphosphatase activity inhibited. Structural, biochemical, and cellular analyses uncover an asymmetric autoinhibition mechanism, in which the cargo-binding sites in the two MyoVa heavy chains are differently protected. Thus, specific and efficient MyoVa activation requires coincident binding of multiple cargo adaptors, revealing an intricate and elegant activity regulation of the motor in response to cargos.
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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.