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http://purl.uniprot.org/citations/15835906http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15835906http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15835906http://www.w3.org/2000/01/rdf-schema#comment"Myosin XVIII is the recently identified 18th class of myosins, and its members are composed of a unique N-terminal domain, a motor domain with an unusual sequence around the ATPase site, one IQ motif, a segmented coiled-coil region for dimerization, and a C-terminal globular tail. To gain insight into the functions of this unique myosin, we characterized its human homologue, MYO18A, focusing on the functional roles of the characteristic N-terminal domain that contains a PDZ module known to mediate protein-protein interaction. GFP-tagged full-length and C-terminally truncated MYO18A molecules that were expressed in HeLa cells exhibited colocalization with actin filaments. Chemical cross-linking of these molecules showed that they form stable dimers as expected from their putative coiled-coil tails. Cosedimentation of the various types of truncated MYO18A constructs with actin filaments indicated the presence of an ATP-insensitive actin-binding site in the N-terminal domain. Further studies on truncated constructs of the N-terminal domain indicated that this actin-binding site is located outside the PDZ module, but within the middle region of this domain, which does not show any homology with the known actin-binding motifs. These results imply that this dimeric myosin might stably cross-link actin filaments by two ATP-insensitive actin-binding sites at the N-terminal domains for higher-order organization of the actin cytoskeleton."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.org/dc/terms/identifier"doi:10.1021/bi0475931"xsd:string
http://purl.uniprot.org/citations/15835906http://purl.org/dc/terms/identifier"doi:10.1021/bi0475931"xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Inoue T."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Inoue T."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Kon T."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Kon T."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Ohara O."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Ohara O."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Sutoh K."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Sutoh K."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Yamakawa H."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Yamakawa H."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Ohkura R."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Ohkura R."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Isogawa Y."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/author"Isogawa Y."xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/pages"6190-6196"xsd:string
http://purl.uniprot.org/citations/15835906http://purl.uniprot.org/core/pages"6190-6196"xsd:string