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http://purl.uniprot.org/citations/11973348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11973348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11973348http://www.w3.org/2000/01/rdf-schema#comment"In this report we have characterized a novel, ubiquitously expressed kinase, Clik1, that is predominantly nuclear and undergoes autophosphorylation. Yeast two-hybrid analysis indicated a highly specific association between Clik1 and CLP-36, which was identified in 36 out of 37 Clik1-interacting clones. CLP-36 is a PDZ-LIM protein that localizes to actin stress fibers in nonmuscle cells and associates with alpha-actinin via its PDZ-domain. The association of CLP-36 with Clik1, in turn, is mediated by the C-terminal part of CLP-36 containing the LIM domain, and association was not noted with the closely related ALP PDZ-LIM protein. Interestingly, the association with CLP-36 led to relocalization of the otherwise nuclear Clik1 kinase to actin stress fibers, where it disrupted the periodic staining pattern of CLP-36. Taken together these results establish the CLP-36 PDZ-LIM protein as an adapter, recruiting the Clik1 kinase to actin stress fibers in nonmuscle cells, and suggest that Clik1 represents a novel regulator of actin stress fibers."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.org/dc/terms/identifier"doi:10.1242/jcs.115.10.2067"xsd:string
http://purl.uniprot.org/citations/11973348http://purl.org/dc/terms/identifier"doi:10.1242/jcs.115.10.2067"xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/author"Maekelae T.P."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/author"Maekelae T.P."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/author"Vallenius T."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/author"Vallenius T."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/pages"2067-2073"xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/pages"2067-2073"xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/title"Clik1: a novel kinase targeted to actin stress fibers by the CLP-36 PDZ-LIM protein."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/title"Clik1: a novel kinase targeted to actin stress fibers by the CLP-36 PDZ-LIM protein."xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/volume"115"xsd:string
http://purl.uniprot.org/citations/11973348http://purl.uniprot.org/core/volume"115"xsd:string
http://purl.uniprot.org/citations/11973348http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11973348
http://purl.uniprot.org/citations/11973348http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11973348
http://purl.uniprot.org/citations/11973348http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11973348
http://purl.uniprot.org/citations/11973348http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11973348
http://purl.uniprot.org/uniprot/Q8TDR2http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11973348
http://purl.uniprot.org/uniprot/Q8TDR2#attribution-A30DB523B9E93C432F9B15DE9E703B24http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/11973348