ArticleBiochemistry2008
Impacts of Usher syndrome type IB mutations on human myosin VIIa motor function.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- The Logistical Backbone of Photoreceptor Cell Function: Complementary Mechanisms of Dietary Vitamin A Receptors and Rhodopsin Transporters.International journal of molecular sciences · 2024Review
- The dynamics of actin protrusions can be controlled by tip-localized myosin motors.The Journal of biological chemistry · 2024Article
- Unraveling the genetic complexities of combined retinal dystrophy and hearing impairment.Human genetics · 2022Article
- Screening Consanguineous Families for Hearing Loss Using the MiamiOtoGenes Panel.Genetic testing and molecular biomarkers · 2020Article
- Human myosin VIIa is a very slow processive motor protein on various cellular actin structures.The Journal of biological chemistry · 2017Article
- Usher syndrome in Denmark: mutation spectrum and some clinical observations.Molecular genetics & genomic medicine · 2016Article
- Functional characterization of the human myosin-7a motor domain.Cellular and molecular life sciences : CMLS · 2012Article
- Cargo binding activates myosin VIIA motor function in cells.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The kinetic mechanism of mouse myosin VIIA.The Journal of biological chemistry · 2011Article
- Molecular epidemiology of Usher syndrome in Italy.Molecular vision · 2011Article
- Reinforcement of a minor alternative splicing event in MYO7A due to a missense mutation results in a mild form of retinopathy and deafness.Molecular vision · 2010Article
- A novel allele of myosin VIIa reveals a critical function for the C-terminal FERM domain for melanosome transport in retinal pigment epithelial cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- The tail binds to the head-neck domain, inhibiting ATPase activity of myosin VIIA.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Usher syndrome (USH) is a human hereditary disorder characterized by profound congenital deafness, retinitis pigmentosa, and vestibular dysfunction. Myosin VIIa has been identified as the responsible gene for USH type 1B, and a number of missense mutations have been identified in the affected families. However, the molecular basis of the dysfunction of USH gene, myosin VIIa, in the affected families is unknown to date. Here we clarified the effects of USH1B mutations on human myosin VIIa motor function for the first time. The missense mutations of USH1B significantly inhibited the actin activation of ATPase activity of myosin VIIa. G25R, R212C, A397D, and E450Q mutations abolished the actin-activated ATPase activity completely. P503L mutation increased the basal ATPase activity for 2-3-fold but reduced the actin-activated ATPase activity to 50% of the wild type. While all of the mutations examined, except for R302H, reduced the affinity for actin and the ATP hydrolysis cycling rate, they did not largely decrease the rate of ADP release from actomyosin, suggesting that the mutations reduce the duty ratio of myosin VIIa. Taken together, the results suggest that the mutations responsible for USH1B cause the complete loss of the actin-activated ATPase activity or the reduction of duty ratio of myosin VIIa.
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