RPS6KA5 & RELA Protein Protein Interaction Antibody Pair
- Known as:
- RPS6KA5 & RELA Protein Protein Interaction Antibody Pair
- Catalog number:
- DI0553
- Product Quantity:
- 1 Set
- Category:
- -
- Supplier:
- Abno
- Gene target:
- RPS6KA5 & RELA Protein Interaction Antibody Pair
Related genes to: RPS6KA5 & RELA Protein Protein Interaction Antibody Pair
- Gene:
- RELA NIH gene
- Name:
- RELA proto-oncogene, NF-kB subunit
- Previous symbol:
- NFKB3
- Synonyms:
- p65
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1991-11-14
- Date modifiied:
- 2016-10-05
- Gene:
- RPS6KA5 NIH gene
- Name:
- ribosomal protein S6 kinase A5
- Previous symbol:
- -
- Synonyms:
- MSK1, RLPK
- Chromosome:
- 14q32.11
- Locus Type:
- gene with protein product
- Date approved:
- 1999-03-10
- Date modifiied:
- 2016-03-01
Related products to: RPS6KA5 & RELA Protein Protein Interaction Antibody Pair
Related articles to: RPS6KA5 & RELA Protein Protein Interaction Antibody Pair
- Interleukin-1β (IL-1β) is a central proinflammatory cytokine implicated in osteoarthritis (OA), but its precise role in chondrocyte apoptosis remains to be fully elucidated. In this study, we demonstrate that IL-1β triggers mitophagy in chondrocytes by promoting Parkin translocation and p62 recruitment to damaged mitochondria, thereby reducing mitochondrial dysfunction and apoptosis. Loss of p62 resulted in impaired mitophagy, excessive mitochondrial superoxide accumulation, and increased cell death. Mechanistically, IL-1β enhanced NF-κB (RelA) phosphorylation at Ser276 and Ser536, accompanied by elevated Mitogen and stress-activated kinase-1 (MSK1) expression. Inhibition of MSK1 selectively suppressed Ser276 phosphorylation without affecting Ser536, leading to reduced p62 expression and disrupted mitophagy. These findings reveal a previously unrecognized intrinsic regulatory mechanism by which IL-1β limits its own apoptosis-promoting effect through activation of the NF-κB (RelA) Ser276-p62-mitophagy axis. This pathway facilitates the clearance of damaged mitochondria and preserves chondrocyte viability, offering potential therapeutic insight into inflammation-associated cartilage degeneration in OA. - Source: PubMed
Hu JunzhengZhang WeituoZhao Zhe - The mitogen- and stress-activated protein kinases (MSK) are epigenetic modifiers that regulate gene expression in normal and disease cell states. MSK1 and 2 are involved in a chain of signal transduction events bringing signals from the external environment of a cell to specific sites in the genome. MSK1/2 phosphorylate histone H3 at multiple sites, resulting in chromatin remodeling at regulatory elements of target genes and the induction of gene expression. Several transcription factors (RELA of NF-κB and CREB) are also phosphorylated by MSK1/2 and contribute to induction of gene expression. In response to signal transduction pathways, MSK1/2 can stimulate genes involved in cell proliferation, inflammation, innate immunity, neuronal function, and neoplastic transformation. Abrogation of the MSK-involved signaling pathway is among the mechanisms by which pathogenic bacteria subdue the host's innate immunity. Depending on the signal transduction pathways in play and the MSK-targeted genes, MSK may promote or hinder metastasis. Thus, depending on the type of cancer and genes involved, MSK overexpression may be a good or poor prognostic factor. In this review, we focus on mechanisms by which MSK1/2 regulate gene expression, and recent studies on their roles in normal and diseased cells. - Source: PubMed
Publication date: 2023/02/22
Sattarifard HediehSafaei AkramKhazeeva EnzheRastegar MojganDavie James R - Microglial cells are essential mediators of neuroinflammatory processes involved in several pathologies. Moreover, the chemokine fractalkine (CX3CL1) is essential in the crosstalk between neurons and microglia. However, the exact roles of CX3CL1, CX3CL1 receptor (CX3CR1) and microglia signalling are not fully understood in neuroinflammation. In addition, the findings reported on this subject are controversial. In this work, we investigated whether CX3CL1 induced pro-inflammatory signalling activation through NF-κB pathway. We were able to show that CX3CL1 activates the pro-inflammatory pathway mediated by the transcription factor NF-κB as an early response in microglial cells. On the other side, CX3CR1-deficient microglia showed impaired NF-κB axis. Phospho-kinase assay proteome profiles indicated that CX3CL1 induced several kinases such as MAPK's (ERK and JNK), SRC-family tyrosine kinases (YES, FGR, LCK and LYN) and most interesting and also related to NF-κB, the mitogen- and stress-activated kinase-1 (MSK1). Knockdown of MSK1 with short interfering RNAs decreased partially MSK1 protein levels (about 50%), enough to decrease the mRNA levels of Il-1β, Tnf-α and iNos triggered by stimulation with CX3CL1. These results indicate the relevance of CX3CL1 in the activation of the pro-inflammatory NF-κB signalling pathway through MSK1 in microglial cells. - Source: PubMed
Publication date: 2019/03/04
Galán-Ganga MarcosGarcía-Yagüe Ángel JLastres-Becker Isabel - Airway inflammation plays a major role in the pathophysiology of lung inflammatory diseases such as asthma. Thrombin, a serine protease, is known to mediate central functions in thrombosis and hemostasis and also plays a critical role in lung inflammation via producing chemokine release including interleukin (IL)-8/CXCL8. Our previous studies showed that c-Src- and Rac-dependent nuclear factor (NF)-κB signaling pathways participate in thrombin-induced IL-8/CXCL8 release in human lung epithelial cells. In this study, we further investigated the role of casein kinase 2 (CK2)/mitogen stress-activated protein kinase 1 (MSK1)-dependent p65 phosphorylation in thrombin-induced NF-κB activation and IL-8/CXCL8 release. Thrombin-induced IL-8/CXCL8 release was inhibited by CK2 inhibitors (apigenin and tetrabromobenzotriazole, TBB), small interfering RNA of CK2β (CK2β siRNA), and MSK1 siRNA. Treatment of cells with thrombin caused increases in CK2β phosphorylation at Ser209, which was inhibited by a protein kinase C α (PKCα) inhibitor (Ro-32-0432). Thrombin-induced MSK1 phosphorylation at Ser581 and Akt phosphorylation at Ser473 were inhibited by apigenin. Moreover, the thrombin-induced increase in IL-8/CXCL8 release was attenuated by p65 siRNA. Stimulation of cells with thrombin resulted in an increase in p65 phosphorylation at Ser276, which was inhibited by apigenin and MSK1 siRNA. Thrombin-induced κB-luciferase activity was also inhibited by apigenin and MSK1 siRNA. Taken together, these results show that thrombin activates the PKCα/CK2/MSK1 signaling pathways, which in turn initiates p65 phosphorylation and NF-κB activation, and ultimately induces IL-8/CXCL8 release in human lung epithelial cells. - Source: PubMed
Publication date: 2015/10/14
Lin Chien-HuangShih Chung-HungChen Bing-Chang - The influence of ultraviolet B (UVB) radiation on transglutaminase 1 (TGase 1), a major factor that regulates skin keratinization, has not been sufficiently characterized especially at the gene or protein level. Thus, we determined whether UVB affects the expression of TGase 1 in human keratinocytes and clarified the intracellular stress signaling mechanism(s) involved. Exposure of human keratinocytes to UVB significantly up-regulated the expression of TGase 1 at the gene and protein levels. Treatment with inhibitors of p38, MEK, JNK or NFκB significantly abolished the UVB-stimulated protein expression of TGase 1. Treatment with astaxanthin immediately after UVB irradiation did not attenuate the increased phosphorylation of Ser536/Ser468NFκBp65, c-Jun, ATK-2 and CK2, and did not abrogate the increased or diminished protein levels of c-Jun/c-Fos or I-κBα, respectively. However, the same treatment with astaxanthin significantly abolished the UVB-stimulated expression of TGase 1 protein, which was accompanied by the attenuated phosphorylation of Thr565/Ser376/Ser360MSK1, Ser276NFκBp65 and Ser133CREB. The MSK1 inhibitor H89 significantly down-regulated the increased protein expression of TGase 1 in UVB-exposed human keratinocytes, which was accompanied by an abrogating effect on the increased phosphorylation of Ser276NFκBp65 and Ser133CREB but not Thr565/Ser376/Ser360MSK1. Transfection of human keratinocytes with MSK1 siRNA suppressed the UVB-stimulated protein expression of TGase 1. These findings suggest that the UVB-stimulated expression of TGase 1 is mediated predominantly via the NFκB pathway and can be attenuated through a specific interruption of the p38/MSK1/NFκBp65Ser276 axis. - Source: PubMed
Publication date: 2015/08/25
Terazawa ShukoMori ShingoNakajima HiroakiYasuda MichitakaImokawa Genji