ArticleProceedings of the National Academy of Sciences of the United States of America2005
Structure of the light chain-binding domain of myosin V.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Ageing alters cysteine oxidation-regulated redox signalling in skeletal muscle: Integrative omics and AI-based structural predictions.Experimental physiology · 2026Article
- Functional characterization of calmodulin-like proteins, CML13 and CML14, as novel light chains of Arabidopsis class VIII myosins.Journal of experimental botany · 2024Article
- Ensembles of human myosin-19 bound to calmodulin and regulatory light chain RLC12B drive multimicron transport.The Journal of biological chemistry · 2023Article
- Inferring Conformational State of Myosin Motor in an Atomic Force Microscopy ImageFrontiers in molecular biosciences · 2022Article
- A tunable LIC1-adaptor interaction modulates dynein activity in a cargo-specific manner.Nature communications · 2020Article
- Regulation of class V myosin.Cellular and molecular life sciences : CMLS · 2018Review
- Structure of the Single-lobe Myosin Light Chain C in Complex with the Light Chain-binding Domains of Myosin-1C Provides Insights into Divergent IQ Motif Recognition.The Journal of biological chemistry · 2016Article
- 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
- Surface dynamics in allosteric regulation of protein-protein interactions: modulation of calmodulin functions by Ca2+.PLoS computational biology · 2013Article
- Structure of androcam supports specialized interactions with myosin VI.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Calmodulin bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a.The Journal of biological chemistry · 2012Article
- The azimuthal path of myosin V and its dependence on lever-arm length.The Journal of general physiology · 2012Article
- A conformational transition in the myosin VI converter contributes to the variable step size.Biophysical journal · 2011Article
- IQ-motif selectivity in human IQGAP2 and IQGAP3: binding of calmodulin and myosin essential light chain.Bioscience reports · 2011Article
- Lever-arm mechanics of processive myosins.Biophysical journal · 2011Review
- Moving into the cell: single-molecule studies of molecular motors in complex environments.Nature reviews. Molecular cell biology · 2011Review
- Nucleotide-dependent shape changes in the reverse direction motor, myosin VI.Biophysical journal · 2010Article
- Calmodulin dissociation regulates Myo5 recruitment and function at endocytic sites.The EMBO journal · 2010Article
- Head of myosin IX binds calmodulin and moves processively toward the plus-end of actin filaments.The Journal of biological chemistry · 2010Article
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5 authors.
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Abstract
Myosin V is a double-headed molecular motor involved in organelle transport. Two distinctive features of this motor, processivity and the ability to take extended linear steps of approximately 36 nm along the actin helical track, depend on its unusually long light chain-binding domain (LCBD). The LCBD of myosin V consists of six tandem IQ motifs, which constitute the binding sites for calmodulin (CaM) and CaM-like light chains. Here, we report the 2-A resolution crystal structure of myosin light chain 1 (Mlc1p) bound to the IQ2-IQ3 fragment of Myo2p, a myosin V from Saccharomyces cerevisiae. This structure, combined with FRET distance measurements between probes in various CaM-IQ complexes, comparative sequence analysis, and the previously determined structures of Mlc1p-IQ2 and Mlc1p-IQ4, allowed building a model of the LCBD of myosin V. The IQs of myosin V are distributed into three pairs. There appear to be specific cooperative interactions between light chains within each IQ pair, but little or no interaction between pairs, providing flexibility at their junctions. The second and third IQ pairs each present a light chain, whether CaM or a CaM-related molecule, bound in a noncanonical extended conformation in which the N-lobe does not interact with the IQ motif. The resulting free N-lobes may engage in protein-protein interactions. The extended conformation is characteristic of the single IQ of myosin VI and is common throughout the myosin superfamily. The model points to a prominent role of the LCBD in the function, regulation, and molecular interactions of myosin V.
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