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http://purl.uniprot.org/citations/9490638http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9490638http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9490638http://www.w3.org/2000/01/rdf-schema#comment"The heavy chains of the class IX myosins, rat myr5 and human myosin-IXb, contain within their tail domains a region with sequence homology to GTPase activating proteins for the rho family of G proteins. Because low levels of myosin-IXb expression preclude purification by conventional means, we have employed an immunoadsorption strategy to purify myosin-IXb, enabling us to characterize the mechanochemical and rho-GTPase activation properties of the native protein. In this report we have examined the light chain content, actin binding properties, in vitro motility and rho-GTPase activity of human myosin-IXb purified from leukocytes. The results presented here indicate that myosin-IXb contains calmodulin as a light chain and that it binds to actin with high affinity in both the absence and presence of ATP. Myosin-IXb is an active motor which, like other calmodulin-containing myosins, exhibits maximal velocity of actin filaments (15 nm/second) in the absence of Ca2+. Native myosin-IXb exhibits GAP activity on rho. Class IX myosins may be an important link between rho and rho-dependent remodeling of the actin cytoskeleton."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.org/dc/terms/identifier"doi:10.1242/jcs.111.7.941"xsd:string
http://purl.uniprot.org/citations/9490638http://purl.org/dc/terms/identifier"doi:10.1242/jcs.111.7.941"xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/author"Bokoch G.M."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/author"Bokoch G.M."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/author"Mooseker M.S."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/author"Mooseker M.S."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/author"Post P.L."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/author"Post P.L."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/pages"941-950"xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/pages"941-950"xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/title"Human myosin-IXb is a mechanochemically active motor and a GAP for rho."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/title"Human myosin-IXb is a mechanochemically active motor and a GAP for rho."xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/volume"111"xsd:string
http://purl.uniprot.org/citations/9490638http://purl.uniprot.org/core/volume"111"xsd:string
http://purl.uniprot.org/citations/9490638http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9490638
http://purl.uniprot.org/citations/9490638http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9490638
http://purl.uniprot.org/citations/9490638http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9490638
http://purl.uniprot.org/citations/9490638http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9490638