ArticleThe Journal of biological chemistry2016
The Globular Tail Domain of Myosin-5a Functions as a Dimer in Regulating the Motor Activity.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Myosin-5a facilitates stress granule formation by interacting with G3BP1.Cellular and molecular life sciences : CMLS · 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
- 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
- Autoinhibition and activation mechanisms revealed by the triangular-shaped structure of myosin Va.Science advances · 2022Article
- Roles of Myosin-Mediated Membrane Trafficking in TGF-β Signaling.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
- Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2.The Journal of biological chemistry · 2019Article
- MYH9 Aggregation Induced by Direct Interaction With PRRSV GP5 Ectodomain Facilitates Viral Internalization by Permissive Cells.Frontiers in microbiology · 2019Article
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- 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
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin-5a contains two heavy chains, which are dimerized via the coiled-coil regions. Thus, myosin-5a comprises two heads and two globular tail domains (GTDs). The GTD is the inhibitory domain that binds to the head and inhibits its motor function. Although the two-headed structure is essential for the processive movement of myosin-5a along actin filaments, little is known about the role of GTD dimerization. Here, we investigated the effect of GTD dimerization on its inhibitory activity. We found that the potent inhibitory activity of the GTD is dependent on its dimerization by the preceding coiled-coil regions, indicating synergistic interactions between the two GTDs and the two heads of myosin-5a. Moreover, we found that alanine mutations of the two conserved basic residues at N-terminal extension of the GTD not only weaken the inhibitory activity of the GTD but also enhance the activation of myosin-5a by its cargo-binding protein melanophilin (Mlph). These results are consistent with the GTD forming a head to head dimer, in which the N-terminal extension of the GTD interacts with the Mlph-binding site in the counterpart GTD. The Mlph-binding site at the GTD-GTD interface must be exposed prior to the binding of Mlph. We therefore propose that the inhibited Myo5a is equilibrated between the folded state, in which the Mlph-binding site is buried, and the preactivated state, in which the Mlph-binding site is exposed, and that Mlph is able to bind to the Myo5a in preactivated state and activates its motor function.
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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.