Transcriptional activation of the NF‐κB p65 subunit by mitogen‐ and stress‐activated protein kinase‐1 (MSK1)

By L. Vermeulen, G. de Wilde, P. Van Damme, W. Vanden Berghe, G. Haegeman. EMBO Journal, 2003

831 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7396ba4dc54547d68ce2fd88ab8ecd79962d4d55

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Citations in the corpus

IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300 (2006, background): “The recruitment of HAT activity is governed by phosphorylation of RelA/p65 within the Rel homology domain (RHD) at S276 by the catalytic protein kinase A subunit or by mitogen and stress-activated protein kinase 1 and at S311 by the protein kinase C (20, 63, 72).”
MAPK signalling pathways as molecular targets for anti-inflammatory therapy--from molecular mechanisms to therapeutic benefits. (2005, background): “p38 MAPK can increase the expression, or regulate by phosphorylation, several transcription factors, including activating transcription factor-2 (ATF-2 is a possible partner of c-Jun in the AP-1 complex), GADD153, myocyte enhancer factor 2C (MEF 2C), C/EBP homologous protein 1 [31,49,50], and NF-nB ”
NF-κB RelA Phosphorylation Regulates RelA Acetylation (2005, methodology): “Phosphorylation of RelA at serine 276 enhances the recruitment of coactivator p300/CBP, leading to increased transcriptional activation involving acetylation of histones surrounding NF-Bresponsive genes ( 29 , 34, 35).”
TNF and MAP kinase signaling pathways (2014, positive): “Moreover, p38α MAP kinase increases NF-κB expression [103] and may mark promoters for increased NF-κB recruitment by p38α MAP kinase-dependent histone H3 phosphorylation of selected chromatin targets [104]. p38α MAP kinase (in cooperation with ERK) was also shown to regulate NF-κB by activating MSK1”
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase (2004, background): “RelA/p65 has been shown to be phosphorylated at serine 276 by the catalytic protein kinase A subunit or the mitogen and stress-activate protein kinase-1, and at serine 311 by the protein kinase C z (Duran et al, 2003; Vermeulen et al, 2003).”
The interplay between the glucocorticoid receptor and nuclear factor-kappaB or activator protein-1: molecular mechanisms for gene repression. (2003, background): “Since we reported on the crucial role of p38 and ERK MAPK in TNFdependent NF- B transactivation (83, 554, 711), we have tested whether the p38 and ERK MAPK inhibitors SB20358 and PD098059 affect GR inhibition of NF- B.”
Inhibiting NF-κB Activation by Small Molecules As a Therapeutic Strategy (2010, neutral): “stress-activated protein kinase-1 (MSK-1) [52], MAP3K NIK[53], Tpl2, PKC-θ [54], PI3K, Akt [55–57], p38 MAPK [58], protein tyrosine kinase, PKC-δ [59], RHO-kinase 2 [60], Mitogen activated protein kinase kinase 3 (MEKK3) [61], and receptor tyrosine kinases such as epidermal growth factor receptor, h”
Transient and Selective NF-κB p65 Serine 536 Phosphorylation Induced by T Cell Costimulation Is Mediated by IκB Kinase β and Controls the Kinetics of p65 Nuclear Import 1 (2004, background): “Serine 276 can be phosphorylated by protein kinase A catalytic subunit (24) or mitogen- and stress-activated protein kinase 1 (25).”
IKKβ phosphorylates p65 at S468 in transactivaton domain 2 (2005, background): “On the other hand, phosphorylation of p65 in the Rel homology domain at S276 and S311 has consistently been reported to be required for association with CBP and NF-κB transcriptional activity (9, 11, 26, 32).”