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http://purl.uniprot.org/citations/19166925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19166925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19166925http://www.w3.org/2000/01/rdf-schema#comment"Mitogen-activated protein kinase (MAPK) pathways can play a role in F-actin dynamics. In particular, the p38 MAPK/MAPK-activated protein kinase 2 (MK2)/heat shock protein 27 (Hsp27) pathway is involved in F-actin alternations. Previously, we showed that MK5 is implicated in F-actin rearrangement induced by the cAMP/cAMP-dependent protein kinase pathway in PC12 cells, while others found Hsp27 to be a good in vitro MK5 substrate. Here we demonstrate that MK5 can specifically interact with Hsp27 in vivo and can induce phosphorylation at serine residues 78 and 82 in cells. siRNA-mediated depletion of Hsp27 protein levels, as well as overexpression of the non-phosphorylatable Hsp27-3A mutant prevented forskolin-induced F-actin reorganization. While ectopic expression of a constitutive active MK5 mutant was sufficient to induce F-actin rearrangement in PC12 cells, co-expression of Hsp27-3A could ablate this process. Our results imply that MK5 is involved in Hsp27-controlled F-actin dynamics in response to activation of the cAMP-dependent protein kinase pathway. These findings render the MK5/Hsp27 connection into a putative therapeutic target for conditions with aberrant Hsp27 phosphorylation such as metastasis, cardiovascular diseases, muscle atrophy, autoimmune skin disease and neuropathology."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.org/dc/terms/identifier"doi:10.1016/j.cellsig.2009.01.009"xsd:string
http://purl.uniprot.org/citations/19166925http://purl.org/dc/terms/identifier"doi:10.1016/j.cellsig.2009.01.009"xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/author"Johannessen M."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/author"Johannessen M."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/author"Moens U."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/author"Moens U."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/author"Kostenko S."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/author"Kostenko S."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/name"Cell. Signal."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/name"Cell. Signal."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/pages"712-718"xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/pages"712-718"xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/title"PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/title"PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5."xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/19166925http://purl.uniprot.org/core/volume"21"xsd:string
http://purl.uniprot.org/citations/19166925http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19166925
http://purl.uniprot.org/citations/19166925http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19166925
http://purl.uniprot.org/citations/19166925http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19166925
http://purl.uniprot.org/citations/19166925http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19166925