ArticleNature structural & molecular biology2008
Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI.
Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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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.
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Who cites it
80 citing papers in PubMed.
- Single-molecule fluorescence microscopy reveals regulatory mechanisms of MYO7A-driven cargo transport in stereocilia of live inner ear hair cells.Nature communications · 2025Article
- Cardiolipin membranes drive Myosin VI activation, oligomerization, and processive cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dynamic Interchange of Local Residue-Residue Interactions in the Largely Extended Single Alpha-Helix in Drebrin.The Biochemical journal · 2025Article
- Article
- Structural dynamics of the intrinsically disordered linker region of cardiac troponin T.bioRxiv : the preprint server for biology · 2024Article
- Autoinhibition and activation of myosin VI revealed by its cryo-EM structure.Nature communications · 2024Article
- Pathophysiology of human hearing loss associated with variants in myosins.Frontiers in physiology · 2024Review
- How myosin VI traps its off-state, is activated and dimerizes.Nature communications · 2023Article
- Pervasive, conserved secondary structure in highly charged protein regions.PLoS computational biology · 2023Article
- Exploitation of Engineered Light-Switchable Myosin XI for Nanotechnological Applications.ACS nano · 2023Article
- Engineering the Active Site Lid Dynamics to Improve the Catalytic Efficiency of Yeast Cytosine Deaminase.International journal of molecular sciences · 2023Article
- Landscape-Based View on the Stepping Movement of Myosin VI.The journal of physical chemistry. B · 2022Article
- Binding partners regulate unfolding of myosin VI to activate the molecular motor.The Biochemical journal · 2022Article
- Gene editing in a Myo6 semi-dominant mouse model rescues auditory function.Molecular therapy : the journal of the American Society of Gene Therapy · 2022Article
- Disentangling the complexity of low complexity proteins.Briefings in bioinformatics · 2020Review
- Modulating the Stiffness of the Myosin VI Single α-Helical Domain.Biophysical journal · 2020Article
- Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.Journal of the American Chemical Society · 2019Article
- Dynamic ion pair behavior stabilizes single α-helices in proteins.The Journal of biological chemistry · 2019Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take approximately 36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare single alpha-helix of approximately 10 nm, which is anchored to the calmodulin-bound IQ domain by a globular proximal tail. With the medial tail contributing to the approximately 36-nm step, rather than dimerizing as previously proposed, we show that the cargo binding domain is the dimerization interface. Furthermore, the cargo binding domain seems to be folded back in the presence of the catalytic head, constituting a potential regulatory mechanism that inhibits dimerization.
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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.