ArticleCellular and molecular life sciences : CMLS2011
Myo1c mutations associated with hearing loss cause defects in the interaction with nucleotide and actin.
Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment.Cell communication and signaling : CCS · 2025Article
- The Allosteric Inhibitor Pentachloropseudilin Inhibits Myosin 1C ATPase Activity and Recapitulates Retinitis Pigmentosa Phenotypes in Mice.ACS omega · 2025Article
- Motility Assay to Probe the Calcium Sensitivity of Myosin and Regulated Thin Filaments.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The role of motor proteins in photoreceptor protein transport and visual function.Ophthalmic genetics · 2022Article
- Loss of Motor Protein MYO1C Causes Rhodopsin Mislocalization and Results in Impaired Visual Function.Cells · 2021Article
- Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021Review
- Dilated cardiomyopathy myosin mutants have reduced force-generating capacity.The Journal of biological chemistry · 2018Article
- The hypertrophic cardiomyopathy myosin mutation R453C alters ATP binding and hydrolysis of human cardiac β-myosin.The Journal of biological chemistry · 2014Article
- The duplication 17p13.3 phenotype: analysis of 21 families delineates developmental, behavioral and brain abnormalities, and rare variant phenotypes.American journal of medical genetics. Part A · 2013Article
- A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity.Biochemistry · 2011Article
- Mechanochemical properties of human myosin-1C are modulated by isoform-specific differences in the N-terminal extension.The Journal of biological chemistryArticle
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Three heterozygous missense mutations in the motor domain of myosin 1c (Myo1c), which mediates adaptation in the inner ear, are associated with bilateral sensorineural hearing loss in humans. With transient kinetic analyses, steady-state ATPase and motility assays, and homology modeling, we studied the interaction of these mutants with nucleotide and actin using a truncated construct, Myo1c(1IQ-SAH), which includes an artificial lever arm. Results indicate that mutation R156W, near switch 1, affects the nucleotide-binding pocket and the calcium binding by disrupting switch 1 movement. Mutation V252A, in the K helix of the upper 50 kDa domain, showed reduced actin affinity consistent with disruption of communication between the actin- and nucleotide-binding sites. T380M, in a Myo1c-specific insert in the HO linker, displayed aberrant changes in most kinetic parameters and uncoupling of the ATPase from motility. These data allow for an interpretation of how these mutations might affect adaptation.
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Registered trials
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.