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Phosphorylation of serine 468 by GSK-3beta negatively regulates basal p65 NF-kappaB activity.

The Journal of biological chemistry - 26 Nov 2004

Buss Holger, Dörrie Anneke, Schmitz M Lienhard, Frank Ronald, Livingstone Mark, Resch Klaus, Kracht Michael

Abstract excerpt

The activity of NF-kappaB is controlled at several levels including the phosphorylation of the strongly transactivating p65 (RelA) subunit. However, the overall number of phosphorylation sites, the signaling pathways and protein kinases that target p65 NF-kappaB and the functional role of these phosphorylations are still being uncovered. Using a combination of peptide arrays with in vitro kinase assays we...

Topics

Down-Regulation
Glycogen Synthase Kinase 3
Glycogen Synthase Kinase 3 beta
HeLa Cells
Humans
Interleukin-1
Mutation
NF-kappa B
Phosphorylation
Serine
Transcription Factor RelA

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 15465828
DOI: 10.1074/jbc.C400442200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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Phosphorylation of serine 468 by GSK-3beta negatively regulates basal p65 NF-kappaB activity.PMID 15465828Read ↗

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