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http://purl.uniprot.org/citations/25411248http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25411248http://www.w3.org/2000/01/rdf-schema#comment"Glomerular podocytes are highly specialized terminally differentiated cells that act as a filtration barrier in the kidney. Mutations in the actin-binding protein, α-actinin 4 (ACTN4), are linked to focal segmental glomerulosclerosis (FSGS), a chronic kidney disease characterized by proteinuria. Aberrant activation of NF-κB pathway in podocytes is implicated in glomerular diseases including proteinuria. We demonstrate here that stable knockdown of ACTN4 in podocytes significantly reduces TNFα-mediated induction of NF-κB target genes, including IL-1β and NPHS1, and activation of an NF-κB-driven reporter without interfering with p65 nuclear translocation. Overexpression of ACTN4 and an actin binding-defective variant increases the reporter activity. In contrast, an FSGS-linked ACTN4 mutant, K255E, which has increased actin binding activity and is predominantly cytoplasmic, fails to potentiate NF-κB activity. Mechanistically, IκBα blocks the association of ACTN4 and p65 in the cytosol. In response to TNFα, both NF-κB subunits p65 and p50 translocate to the nucleus, where they bind and recruit ACTN4 to their targeted promoters, IL-1β and IL-8. Taken together, our data identify ACTN4 as a novel coactivator for NF-κB transcription factors in podocytes. Importantly, this nuclear function of ACTN4 is independent of its actin binding activity in the cytoplasm."xsd:string
http://purl.uniprot.org/citations/25411248http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m114.597260"xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/author"Zhao X."xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/author"Lim J.H."xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/author"Bruggeman L.A."xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/author"Kao H.Y."xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/author"Hsu K.S."xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/pages"338-349"xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/title"alpha-Actinin 4 potentiates nuclear factor kappa-light-chain-enhancer of activated B-cell (NF-kappaB) activity in podocytes independent of its cytoplasmic actin binding function."xsd:string
http://purl.uniprot.org/citations/25411248http://purl.uniprot.org/core/volume"290"xsd:string
http://purl.uniprot.org/citations/25411248http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25411248
http://purl.uniprot.org/citations/25411248http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25411248
http://purl.uniprot.org/uniprot/O43707#attribution-5DDF56CB39DDB5B83A2EAD46CB7EF0C2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/O43707#attribution-DD1A3A42A0C63A2570BF713CBFE111C9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/Q8WUI4#attribution-5DDF56CB39DDB5B83A2EAD46CB7EF0C2http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/P19838#attribution-516DB50EFE0F847716AA155791CADE14http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/P19838#attribution-DD1A3A42A0C63A2570BF713CBFE111C9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/Q04206#attribution-516DB50EFE0F847716AA155791CADE14http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/Q04206#attribution-DD1A3A42A0C63A2570BF713CBFE111C9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/Q04207#attribution-516DB50EFE0F847716AA155791CADE14http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/#_A0A0G2JGK6-mappedCitation-25411248http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25411248
http://purl.uniprot.org/uniprot/#_A0A1L1SV25-mappedCitation-25411248http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25411248