The Phosphorylation Status of Nuclear NF-ΚB Determines Its Association with CBP/p300 or HDAC-1

By H. Zhong, M. May, E. Jimi, S. Ghosh. 2002

918 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/5d17c97ef7194abc4b0438156d2923c7968d1524

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

In Molecular Biology

In Oncology

Citations in the corpus

NF-κB RelA Phosphorylation Regulates RelA Acetylation (2005, background): “Phosphorylation of serine 276 also enhances the recruitment of coactivator p300/CBP to and displaces transcriptionally repressive p50-HDAC complexes from the promoter region of several NF-B target genes, thereby facilitating the acetylation of histones surrounding the gene (29, 33 , 35).”
NF-kappaB/p65 antagonizes Nrf2-ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK. (2008, background): “In nucleus, p65 concerts gene transcription by recruiting either coactivators, such as CREB binding protein (CBP) [3,4], or corepressors, such as histone deacetylases (HDACs), to target gene [5–8].”
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): “Phosphorylation of this site enhances p65 DNA binding and interaction with the transcriptional coactivator CBP/p300 (26).”
The interplay between the glucocorticoid receptor and nuclear factor-kappaB or activator protein-1: molecular mechanisms for gene repression. (2003, background): “Besides HDAC-2, association of NF- B with HDAC-1 and HDAC-3 has also been observed recently (77, 467, 468).”
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase (2004, background): “HDAC1, HDAC2, and HDAC3 deacetylate RelA/p65, resulting in increased IkBa association or loss of transactivation potential of the protein (Ashburner et al, 2001; Chen et al, 2001; Zhong et al, 2002).”
Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, background): “…subunit of protein kinase A (PKAc), which is in a complex with IkBa, suggesting coordinate IkB phosphorylation/degradation and RelA modification (Zhong et al., 1998, 2002) (Figure 3; Table 4). p50 and c-Rel are also modified by PKAc at Ser-337 and Ser-267, respectively, the equivalent sites to…”