ArticleProceedings of the National Academy of Sciences of the United States of America2004
The unique insert in myosin VI is a structural calcium-calmodulin binding site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 79 citations in OpenAlex.
- Direct Observation of Nanometer-Sized Steps of Single Myosin VI Molecules in Living Cells.Nano letters · 2026Article
- Neurogranin-MYH9 interaction regulates cytoskeletal remodeling in cerebral vasculature.Fluids and barriers of the CNS · 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
- Hydrogen/Deuterium Exchange Mass Spectrometry Provides Insights into the Role of Drosophila Testis-Specific Myosin VI Light Chain AndroCaM.Biochemistry · 2024Article
- Myosins, an Underestimated Player in the Infectious Cycle of Pathogenic Bacteria.International journal of molecular sciences · 2021Review
- Strain Mediated Adaptation Is Key for Myosin Mechanochemistry: Discovering General Rules for Motor Activity.PLoS computational biology · 2016Article
- Calcium can mobilize and activate myosin-VI.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Myosin VI deafness mutation prevents the initiation of processive runs on actin.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- The cortical acto-Myosin network: from diffusion barrier to functional gateway in the transport of neurosecretory vesicles to the plasma membrane.Frontiers in endocrinology · 2013Review
- Myosin VI has a one track mind versus myosin Va when moving on actin bundles or at an intersection.Traffic (Copenhagen, Denmark) · 2013Article
- Structure of androcam supports specialized interactions with myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.Investigative ophthalmology & visual science · 2011Article
- Actin filament dynamics in the actomyosin VI complex is regulated allosterically by calcium-calmodulin light chain.Journal of molecular biology · 2011Article
- Myosin Va and myosin VI coordinate their steps while engaged in an in vitro tug of war during cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI.Biophysical journal · 2011Article
- Formation of salt bridges mediates internal dimerization of myosin VI medial tail domain.Structure (London, England : 1993) · 2010Article
- Head of myosin IX binds calmodulin and moves processively toward the plus-end of actin filaments.The Journal of biological chemistry · 2010Article
- Myosin VI: an innovative motor that challenged the swinging lever arm hypothesis.Nature reviews. Molecular cell biology · 2010Review
- Reverse conformational changes of the light chain-binding domain of myosin V and VI processive motor heads during and after hydrolysis of ATP by small-angle X-ray solution scattering.Journal of molecular biology · 2009Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
Myosin VI contains an inserted sequence that is unique among myosin superfamily members and has been suggested to be a determinant of the reverse directionality and unusual motility of the motor. It is thought that each head of a two-headed myosin VI molecule binds one calmodulin (CaM) by means of a single "IQ motif". Using truncations of the myosin VI protein and electrospray ionization(ESI)-MS, we demonstrate that in fact each myosin VI head binds two CaMs. One CaM binds to a conventional IQ motif either with or without calcium and likely plays a regulatory role when calcium binds to its N-terminal lobe. The second CaM binds to a unique insertion between the converter region and IQ motif. This unusual CaM-binding site normally binds CaM with four Ca2+ and can bind only if the C-terminal lobe of CaM is occupied by calcium. Regions of the MD outside of the insert peptide contribute to the Ca(2+)-CaM binding, as truncations that eliminate elements of the MD alter CaM binding and allow calcium dissociation. We suggest that the Ca(2+)-CaM bound to the unique insert represents a structural CaM, and not a calcium sensor or regulatory component of the motor. This structure is likely an integral part of the myosin VI "converter" region and repositions the myosin VI "lever arm" to allow reverse direction (minus-end) motility on actin.
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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.