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http://purl.uniprot.org/citations/9565595http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9565595http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9565595http://www.w3.org/2000/01/rdf-schema#comment"We found that vimentin, the most widely expressed intermediate filament protein, served as an excellent substrate for Rho-associated kinase (Rho-kinase) and that vimentin phosphorylated by Rho-kinase lost its ability to form filaments in vitro. Two amino-terminal sites on vimentin, Ser38 and Ser71, were identified as the major phosphorylation sites for Rho-kinase, and Ser71 was the most favored and unique phosphorylation site for Rho-kinase in vitro. To analyze the vimentin phosphorylation by Rho-kinase in vivo, we prepared an antibody GK71 that specifically recognizes the phosphorylation of vimentin-Ser71. Ectopic expression of constitutively active Rho-kinase in COS-7 cells induced phosphorylation of vimentin at Ser71, followed by the reorganization of vimentin filament networks. During the cell cycle, the phosphorylation of vimentin-Ser71 occurred only at the cleavage furrow in late mitotic cells but not in interphase or early mitotic cells. This cleavage furrow-specific phosphorylation of vimentin-Ser71 was observed in the various types of cells we examined. All these accumulating observations increase the possibility that Rho-kinase may have a definite role in governing regulatory processes in assembly-disassembly and turnover of vimentin filaments at the cleavage furrow during cytokinesis."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.19.11728"xsd:string
http://purl.uniprot.org/citations/9565595http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.19.11728"xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Amano M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Amano M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Goto H."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Goto H."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Kaibuchi K."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Kaibuchi K."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Inagaki M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Inagaki M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Sakurai M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Sakurai M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Tanabe K."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Tanabe K."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Yanagida M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Yanagida M."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Kosako H."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/author"Kosako H."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9565595http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string