ArticleProtein science : a publication of the Protein Society2002
Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 41 citations in OpenAlex.
- The co-occurrence of homozygous variants in GUCY2D and MYO7A in Leber congenital amaurosis associated with deafness: clinical, molecular, and in silico investigation.Molecular biology reports · 2026Article
- Oncogenic ASPM Is a Regulatory Hub of Developmental and Stemness Signaling in Cancers.Cancer research · 2023Article
- Direct m6A recognition by IMP1 underlays an alternative model of target selection for non-canonical methyl-readers.Nucleic acids research · 2023Article
- Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaBiophysical chemistry · 2017Article
- Self-organization of actin networks by a monomeric myosin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Detecting stoichiometry of macromolecular complexes in live cells using FRET.Nature communications · 2016Article
- Calcium can mobilize and activate myosin-VI.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin.Protein science : a publication of the Protein Society · 2014Article
- Calmodulin regulates dimerization, motility, and lipid binding of Leishmania myosin XXI.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Myosin light chains: Teaching old dogs new tricks.Bioarchitecture · 2014Review
- The microtubule-associated protein ASPM regulates spindle assembly and meiotic progression in mouse oocytes.PloS one · 2012Article
- Kinetic analysis reveals differences in the binding mechanism of calmodulin and calmodulin-like protein to the IQ motifs of myosin-10.Biochemistry · 2010Article
- The globular tail domain puts on the brake to stop the ATPase cycle of myosin Va.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A molecular dynamics study and free energy analysis of complexes between the Mlc1p protein and two IQ motif peptides.Biophysical journal · 2006Article
- New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.Protein science : a publication of the Protein Society · 2006Article
- Biochemical properties of V91G calmodulin: A calmodulin point mutation that deregulates muscle contraction in Drosophila.Protein science : a publication of the Protein Society · 2004Article
- Time-resolved fluorescence anisotropy studies show domain-specific interactions of calmodulin with IQ target sequences of myosin V.European biophysics journal : EBJ · 2003Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Apo-Calmodulin acts as the light chain for unconventional myosin V, and treatment with Ca(2+) can cause dissociation of calmodulin from the 6IQ region of the myosin heavy chain. The effects of Ca(2+) on the stoichiometry and affinity of interactions of calmodulin and its two domains with two myosin-V peptides (IQ3 and IQ4) have therefore been quantified in vitro, using fluorescence and near- and far-UV CD. The results with separate domains show their differential affinity in interactions with the IQ motif, with the apo-N domain interacting surprisingly weakly. Contrary to expectations, the effect of Ca(2+) on the interactions of either peptide with either isolated domain is to increase affinity, reducing the K(d) at physiological ionic strengths by >200-fold to approximately 75 nM for the N domain, and approximately 10-fold to approximately 15 nM for the C domain. Under suitable conditions, intact (holo- or apo-) calmodulin can bind up to two IQ-target sequences. Interactions of apo- and holo-calmodulin with the double-length, concatenated sequence (IQ34) can result in complex stoichiometries. Strikingly, holo-calmodulin forms a high-affinity 1:1 complex with IQ34 in a novel mode of interaction, as a "bridged" structure wherein two calmodulin domains interact with adjacent IQ motifs. This apparently imposes a steric requirement for the alpha-helical target sequence to be discontinuous, possibly in the central region, and a model structure is illustrated. Such a mode of interaction could account for the Ca(2+)-dependent regulation of myosin V in vitro motility, by changing the structure of the regulatory complex, and paradoxically causing calmodulin dissociation through a change in stoichiometry, rather than a Ca(2+)-dependent reduction in affinity.
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