IKKbeta phosphorylates p65 at S468 in transactivaton domain 2.

doi:10.1096/fj.05-3736fje

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Topics Community

Back to search

Article

IKKbeta phosphorylates p65 at S468 in transactivaton domain 2.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Oct 2005

Schwabe Robert F, Sakurai Hiroaki

Abstract excerpt

The transcription factor nuclear factor-kappa B (NF-kappaB) subunit p65 is phosphorylated by IkappaB kinase (IKK) at S536 in transactivation domain (TAD) 1. In this study, we investigate the presence of IKK sites in TAD2 of p65. Recombinant IKKbeta, but not IKKalpha, phosphorylated a GST-p65 substrate in which TAD1 was deleted. Mutational analysis revealed S468 as the only IKK site in TAD2. S468 phosphorylation...

Topics

Active Transport, Cell Nucleus
Animals
Binding Sites
Blotting, Western
Cell Line
Cell Line, Tumor
Cells, Cultured
DNA Mutational Analysis
Fibroblasts
Genes, Dominant
Genes, Reporter

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

HeLa Cells

Humans

I-kappa B Kinase

Immunoprecipitation

Inflammation

Interleukin-1

Leukocytes, Mononuclear

Source

Open in PubMed

Identifiers

PMID: 16046471
DOI: 10.1096/fj.05-3736fje

Genes

Provenance

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

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

IKKbeta phosphorylates p65 at S468 in transactivaton domain 2.PMID 16046471Read ↗

Constitutive and interleukin-1-inducible phosphorylation of p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription.Semantic proximity Read ↗

Tumor necrosis factor-alpha-induced IKK phosphorylation of NF-kappaB p65 on serine 536 is mediated through the TRAF2, TRAF5, and TAK1 signaling pathway.Semantic proximity Read ↗

Phosphorylation of RelA/p65 on serine 536 defines an I{kappa}B{alpha}-independent NF-{kappa}B pathway.Semantic proximity Read ↗

Insufficient p65 phosphorylation at S536 specifically contributes to the lack of NF-kappaB activation and transformation in resistant JB6 cells.Semantic proximity Read ↗

Thr435 phosphorylation regulates RelA (p65) NF-kappaB subunit transactivation.Semantic proximity Read ↗

Suppression of p65 phosphorylation coincides with inhibition of IkappaBalpha polyubiquitination and degradation.Semantic proximity Read ↗

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

A phosphomimetic mutant of RelA/p65 at Ser536 induces apoptosis and senescence: An implication for tumor-suppressive role of Ser536 phosphorylation.Semantic proximity Read ↗

A RelA(p65) Thr505 phospho-site mutation reveals an important mechanism regulating NF-κB-dependent liver regeneration and cancer.Semantic proximity Read ↗

Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1).Semantic proximity Read ↗

Specification of the NF-kappaB transcriptional response by p65 phosphorylation and TNF-induced nuclear translocation of IKK epsilon.Semantic proximity Read ↗

A novel NF-kappaB pathway involving IKKbeta and p65/RelA Ser-536 phosphorylation results in p53 Inhibition in the absence of NF-kappaB transcriptional activity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.