ArticleStructure (London, England : 1993)2010
Formation of salt bridges mediates internal dimerization of myosin VI medial tail domain.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 35 citations in OpenAlex.
- 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
- Emergent conformational and aggregation properties of synergistic antimicrobial peptide combinations.Nanoscale · 2024Article
- How myosin VI traps its off-state, is activated and dimerizes.Nature communications · 2023Article
- Constructing atomic structural models into cryo-EM densities using molecular dynamics - Pros and cons.Journal of structural biology · 2018Article
- NDP52 activates nuclear myosin VI to enhance RNA polymerase II transcription.Nature communications · 2017Article
- Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2.Scientific reports · 2017Article
- Kinematics of the lever arm swing in myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Advances in the molecular dynamics flexible fitting method for cryo-EM modeling.Methods (San Diego, Calif.) · 2016Article
- Myosin VI must dimerize and deploy its unusual lever arm in order to perform its cellular roles.Cell reports · 2014Article
- Membrane-induced lever arm expansion allows myosin VI to walk with large and variable step sizes.The Journal of biological chemistry · 2012Article
- Cryo-electron microscopy modeling by the molecular dynamics flexible fitting method.Biopolymers · 2012Article
- How myosin motors power cellular functions: an exciting journey from structure to function: based on a lecture delivered at the 34th FEBS Congress in Prague, Czech Republic, July 2009.The FEBS journal · 2012Article
- A conformational transition in the myosin VI converter contributes to the variable step size.Biophysical journal · 2011Article
- Myosin-X: a MyTH-FERM myosin at the tips of filopodia.Journal of cell science · 2011Review
- Oligomerization state of photosynthetic core complexes is correlated with the dimerization affinity of a transmembrane helix.Journal of the American Chemical Society · 2011Article
- Extension of a three-helix bundle domain of myosin VI and key role of calmodulins.Biophysical journal · 2011Article
- Applications of the molecular dynamics flexible fitting method.Journal of structural biology · 2011Article
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5 authors at 1 institution in 1 country.
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Abstract
The unconventional motor protein, myosin VI, is known to dimerize upon cargo binding to its C-terminal end. It has been shown that one of its tail domains, called the medial tail domain, is a dimerization region. The domain contains an unusual pattern of alternating charged residues and a few hydrophobic residues. To reveal the unknown dimerization mechanism of the medial tail domain, we employed molecular dynamics and single-molecule experimental techniques. Both techniques suggest that the formation of electrostatic-based interhelical salt bridges between oppositely charged residues is a key dimerization factor. For the dimerization to occur, the two identical helices within the dimer do not bind in a symmetric fashion, but rather with an offset of about one helical repeat. Calculations of the dimer-dissociation energy find the contribution of hydrophobic residues to the dimerization process to be minor; they also find that the asymmetric homodimer state is energetically favorable over a state of separate helices.
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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.