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http://purl.uniprot.org/citations/21687988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21687988http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21687988http://www.w3.org/2000/01/rdf-schema#comment"Myosin-7a participates in auditory and visual processes. Defects in MYO7A, the gene encoding the myosin-7a heavy chain, are causative for Usher syndrome 1B, the most frequent cause of deaf-blindness in humans. In the present study, we performed a detailed kinetic and functional characterization of the isolated human myosin-7a motor domain to elucidate the details of chemomechanical coupling and the regulation of motor function. A rate-limiting, slow ADP release step causes long lifetimes of strong actin-binding intermediates and results in a high duty ratio. Moreover, our results reveal a Mg(2+)-sensitive regulatory mechanism tuning the kinetic and mechanical properties of the myosin-7a motor domain. We obtained direct evidence that changes in the concentration of free Mg(2+) ions affect the motor properties of human myosin-7a using an in vitro motility assay system. Our results suggest that in a cellular environment, compartment-specific fluctuations in free Mg(2+) ions can mediate the conditional switching of myosin-7a between cargo moving and tension bearing modes."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.org/dc/terms/identifier"doi:10.1007/s00018-011-0749-8"xsd:string
http://purl.uniprot.org/citations/21687988http://purl.org/dc/terms/identifier"doi:10.1007/s00018-011-0749-8"xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/author"Manstein D.J."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/author"Manstein D.J."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/author"Heissler S.M."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/author"Heissler S.M."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/name"Cell. Mol. Life Sci."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/name"Cell. Mol. Life Sci."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/pages"299-311"xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/pages"299-311"xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/title"Functional characterization of the human myosin-7a motor domain."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/title"Functional characterization of the human myosin-7a motor domain."xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/volume"69"xsd:string
http://purl.uniprot.org/citations/21687988http://purl.uniprot.org/core/volume"69"xsd:string
http://purl.uniprot.org/citations/21687988http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21687988
http://purl.uniprot.org/citations/21687988http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21687988
http://purl.uniprot.org/citations/21687988http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21687988
http://purl.uniprot.org/citations/21687988http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21687988
http://purl.uniprot.org/uniprot/Q13402http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/21687988
http://purl.uniprot.org/uniprot/Q13402#attribution-3657AE0A49AB5100D314CF852185D72Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21687988