ArticleThe Journal of biological chemistry2015
Structure and Regulation of the Movement of Human Myosin VIIA.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- A novel duplication mutation in the MYO7A gene associated with autosomal recessive hearing loss in a Chinese family.Genes & genomics · 2026Article
- Single-molecule fluorescence microscopy reveals regulatory mechanisms of MYO7A-driven cargo transport in stereocilia of live inner ear hair cells.Nature communications · 2025Article
- Influence of Myosin Regulatory Light Chain and Myosin Light Chain Kinase on the Physiological Function of Inner Ear Hair Cells.Journal of the Association for Research in Otolaryngology : JARO · 2025Article
- Select autosomal dominant DFNA11 deafness variants activate Myo7A targeting in epithelial cells.Journal of cell science · 2025Article
- Myosin motors in sensory hair bundle assembly.Current opinion in cell biology · 2022Review
- Novel compound heterozygous synonymous and missense variants in the MYO7A gene identified by next-generation sequencing in a Chinese family with nonsyndromic hearing loss.Journal of clinical laboratory analysis · 2022Article
- Mitochondria-associated myosin 19 processively transports mitochondria on actin tracks in living cells.The Journal of biological chemistry · 2022Article
- Clinical Heterogeneity Associated withBiomedicines · 2022Article
- Comparative analysis of the MyTH4-FERM myosins reveals insights into the determinants of actin track selection in polarized epithelia.Molecular biology of the cell · 2021Article
- The many roles of myosins in filopodia, microvilli and stereocilia.Current biology : CB · 2021Review
- Spectrum ofGenes · 2021Article
- A binding protein regulates myosin-7a dimerization and actin bundle assembly.Nature communications · 2021Article
- Homology modeling and global computational mutagenesis of human myosin VIIa.Journal of analytical & pharmaceutical research · 2021Article
- A new light chain for myosin-7.The Journal of biological chemistry · 2020Article
- The small EF-hand protein CALML4 functions as a critical myosin light chain within the intermicrovillar adhesion complex.The Journal of biological chemistry · 2020Article
- Myosin VIIa Supports Spermatid/Organelle Transport and Cell Adhesion During Spermatogenesis in the Rat Testis.Endocrinology · 2019Article
- Globular-shaped variable lymphocyte receptors B antibody multimerized by a hydrophobic clustering in hagfish.Scientific reports · 2018Article
- Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Role of glutamine and interlinked asparagine metabolism in vessel formation.The EMBO journal · 2017Article
- Human myosin VIIa is a very slow processive motor protein on various cellular actin structures.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Human myosin VIIA (HM7A) is responsible for human Usher syndrome type 1B, which causes hearing and visual loss in humans. Here we studied the regulation of HM7A. The actin-activated ATPase activity of full-length HM7A (HM7AFull) was lower than that of tail-truncated HM7A (HM7AΔTail). Deletion of the C-terminal 40 amino acids and mutation of the basic residues in this region (R2176A or K2179A) abolished the inhibition. Electron microscopy revealed that HM7AFull is a monomer in which the tail domain bends back toward the head-neck domain to form a compact structure. This compact structure is extended at high ionic strength or in the presence of Ca(2+). Although myosin VIIA has five isoleucine-glutamine (IQ) motifs, the neck length seems to be shorter than the expected length of five bound calmodulins. Supporting this observation, the IQ domain bound only three calmodulins in Ca(2+), and the first IQ motif failed to bind calmodulin in EGTA. These results suggest that the unique IQ domain of HM7A is important for the tail-neck interaction and, therefore, regulation. Cellular studies revealed that dimer formation of HM7A is critical for its translocation to filopodial tips and that the tail domain (HM7ATail) markedly reduced the filopodial tip localization of the HM7AΔTail dimer, suggesting that the tail-inhibition mechanism is operating in vivo. The translocation of the HM7AFull dimer was significantly less than that of the HM7AΔTail dimer, and R2176A/R2179A mutation rescued the filopodial tip translocation. These results suggest that HM7A can transport its cargo molecules, such as USH1 proteins, upon release of the tail-dependent inhibition.
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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.