ArticleBMC biochemistry2002
Calmodulin binding to recombinant myosin-1c and myosin-1c IQ peptides.
Article in BMC biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed.
- Non-Canonical Localization of Cardiac Troponins: Expanding Functions or Causing Pathologies?International journal of molecular sciences · 2024Review
- How Transmembrane Inner Ear (TMIE) plays role in the auditory system: A mystery to us.Journal of cellular and molecular medicine · 2021Review
- The regulatory protein 14-3-3β binds to the IQ motifs of myosin-IC independent of phosphorylation.The Journal of biological chemistry · 2020Article
- Calcium and Nuclear Signaling in Prostate Cancer.International journal of molecular sciences · 2018Review
- Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling.Nature structural & molecular biology · 2015Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- Specific nuclear localizing sequence directs two myosin isoforms to the cell nucleus in calmodulin-sensitive manner.PloS one · 2012Article
- Leveraging the membrane - cytoskeleton interface with myosin-1.Trends in cell biology · 2010Review
- Modification of loop 1 affects the nucleotide binding properties of Myo1c, the adaptation motor in the inner ear.Biochemistry · 2010Article
- IQ motif selectivity in human IQGAP1: binding of myosin essential light chain and S100B.Molecular and cellular biochemistry · 2008Article
- Calcium sensitivity of the cross-bridge cycle of Myo1c, the adaptation motor in the inner ear.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Calcium regulation of calmodulin binding to and dissociation from the myo1c regulatory domain.Biochemistry · 2007Article
- CIB1 and CaBP1 bind to the myo1c regulatory domain.Journal of muscle research and cell motility · 2007Article
- Stereociliary myosin-1c receptors are sensitive to calcium chelation and absent from cadherin 23 mutant mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- A signal transduction pathway model prototype II: Application to Ca2+-calmodulin signaling and myosin light chain phosphorylation.Biophysical journal · 2004Article
- Effect of O-4-ethoxyl-butyl-berbamine in combination with pegylated liposomal doxorubicin on advanced hepatoma in mice.World journal of gastroenterology · 2004Article
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2 authors.
Funding
Abstract
backgroundBullfrog myosin-1c contains three previously recognized calmodulin-binding IQ domains (IQ1, IQ2, and IQ3) in its neck region; we identified a fourth IQ domain (IQ4), located immediately adjacent to IQ3. How calmodulin binds to these IQ domains is the subject of this report.
resultsIn the presence of EGTA, calmodulin bound to synthetic peptides corresponding to IQ1, IQ2, and IQ3 with Kd values of 2-4 microM at normal ionic strength; the interaction with an IQ4 peptide was much weaker. Ca2+ substantially weakened the calmodulin-peptide affinity for all of the IQ peptides except IQ3. To reveal how calmodulin bound to the linearly arranged IQ domains of the myosin-1c neck, we used hydrodynamic measurements to determine the stoichiometry of complexes of calmodulin and myosin-1c. Purified myosin-1c and T701-Myo1c (a myosin-1c fragment with all four IQ domains and the C-terminal tail) each bound 2-3 calmodulin molecules. At a physiologically relevant temperature (25 degrees C) and under low-Ca2+ conditions, T701-Myo1c bound two calmodulins in the absence and three calmodulins in the presence of 5 microM free calmodulin. Ca2+ dissociated nearly all calmodulins from T701-Myo1c at 25 degrees C; one calmodulin was retained if 5 microM free calmodulin was present.
conclusionsWe inferred from these data that at 25 degrees C and normal cellular concentrations of calmodulin, calmodulin is bound to IQ1, IQ2, and IQ3 of myosin-1c when Ca2+ is low. The calmodulin bound to one of these IQ domains, probably IQ2, is only weakly associated. Upon Ca2+ elevation, all calmodulin except that bound to IQ3 should dissociate.
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