Essential role of RelA Ser311 phosphorylation by ζPKC in NF‐κB transcriptional activation

By A. Duran, M. Diaz-Meco, J. Moscat. 2003

329 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a38c64ae32b4bb9989d0a5bf0c9085e019b795de

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Citations in the corpus

IKKβ phosphorylates p65 at S468 in transactivaton domain 2 (2005, background): “p65 has been shown to be phosphorylated by PKAc and MSK1 at S276 (9, 10), by PKCζ at S311 ( 11 ), by GSK-3β at S468 (12), by casein kinase at S529 (13, 14), and by calmodulindependent kinase IV at S535 (15).”
NF-κB RelA Phosphorylation Regulates RelA Acetylation (2005, background): “In addition to serines 276 and 536, RelA is also phosphorylated at serine 311 by protein kinase C ( 10 ) and at serine 529 by casein kinase II (30).”
The complexity of NF-κB signaling in inflammation and cancer (2013, unknown): “PKCζ S311 stimulates transcriptional activity [59]”
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 311 can be inducibly phosphorylated by PKC , which is important for coactivator binding and recruitment to their target promoters (27).”
The Regulation of NF-κB Subunits by Phosphorylation (2016, background): “S281 unknown transactivation [73,76] S311 PKCζ K310 acetylation, transactivation [79–82] S316 unknown transactivation [83] T435 unknown (CK2, PLK1?) transactivation [101,102]”
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).”
Shaping the nuclear action of NF-κB (2004, background): “pl?Q05513">PKCζ , and this modification similarly enhances the overall transcriptional respons”
Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, background): “Ser-311, which also lies within the RelA transactivation domain, but close to the junction with the RHD, is inducibly phosphorylated by the atypical protein kinase C, PKCz, in response to TNF stimulation (Duran et al., 2003).”
IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300 (2006, background): “Therefore, in agreement with previously published work (17, 20, 72), it is likely that phosphorylation of RelA/p65 at S276, S536, and possibly S311 and S529 activates RelA/p65 by first derepressing HDAC1 and SMRT-HDAC3 repression complexes, allowing subsequent recruitment of CBP/p300 and acetylation”