| http://purl.uniprot.org/citations/26247921 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26247921 | http://www.w3.org/2000/01/rdf-schema#comment | "Nuclear factor-κB (NF-κB) is an inducible transcription factor that mediates immune and inflammatory responses. NF-κB pathways are also involved in cell adhesion, differentiation, proliferation, autophagy, senescence, and protection against apoptosis. The deregulation of NF-κB activity is found in a number of disease states, including cancer, arthritis, chronic inflammation, asthma, neurodegenerative diseases, and heart disease. The 90 kDa ribosomal S6 kinase (p90RSK) family, which is serine/threonine kinases, is phosphorylated by extracellular signal-regulated kinase1/2 (ERK1/2) and is related to NF-κB pathways. Our previous studies revealed that Sec6, a component of the exocyst complex, plays specific roles in cell-cell adhesion and cell cycle arrest. However, the mechanism by which Sec6 regulates the NF-κB signaling pathway is unknown. We demonstrated that Sec6 knockdown inhibited the degradation of IκBα and delayed the nucleus-cytoplasm translocation of p65 in HeLa cells transfected with Sec6 siRNAs after treatment with tumor necrosis factor alpha (TNF-α). Furthermore, the binding of p65 and cAMP response element binding protein (CREB) binding protein (CBP) or p300 decreased and NF-κB related genes which were inhibitors of NF-κB alpha (IκBα), A20, B cell lymphoma protein 2 (Bcl-2), and monocyte chemoattractant protein-1 (MCP-1) were low in cells transfected with Sec6 siRNAs in response to TNF-α stimulation. Sec6 knockdown decreased the expression of p90RSKs and the phosphorylation of ERK or p90RSK1 at Ser380 or IκBα at Ser32. The present study suggests that Sec6 regulates NF-κB transcriptional activity via the control of the phosphorylation of IκBα, p90RSK1, and ERK."xsd:string |
| http://purl.uniprot.org/citations/26247921 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcp.25122"xsd:string |
| http://purl.uniprot.org/citations/26247921 | http://purl.uniprot.org/core/author | "Tanaka T."xsd:string |
| http://purl.uniprot.org/citations/26247921 | http://purl.uniprot.org/core/author | "Iino M."xsd:string |
| http://purl.uniprot.org/citations/26247921 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/26247921 | http://purl.uniprot.org/core/name | "J Cell Physiol"xsd:string |
| http://purl.uniprot.org/citations/26247921 | http://purl.uniprot.org/core/pages | "719-730"xsd:string |
| http://purl.uniprot.org/citations/26247921 | http://purl.uniprot.org/core/title | "Nuclear Translocation of p65 is Controlled by Sec6 via the Degradation of IkappaBalpha."xsd:string |
| http://purl.uniprot.org/citations/26247921 | http://purl.uniprot.org/core/volume | "231"xsd:string |
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