Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB

By Lin-Feng Chen, Y. Mu, W. Greene. EMBO Journal, 2002

894 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/4ec788824955a86580361f7aeac5afccb6f9e47c

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 Immunology

Citations in the corpus

Inhibiting NF-κB Activation by Small Molecules As a Therapeutic Strategy (2010, neutral): “The K221 and K310 acetylation are associated with increased NF-κB target gene transcription [112] and are required for p65 activation [24], which is supported by the observations that SIRT driven deacetylation at K310 inhibits NF-κB target gene transcription [113].”
IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300 (2006, background): “p300-induced acetylation of RelA/p65 at K310 is associated with full NF- B transcriptional activity, suggesting that acetylation within the RHD of RelA/p65 is required for NF- B-mediated enhanceasome activity (16, 17, 69).”
Persistently-activated Stat3 maintains constitutive NF-κB activity in tumors (2009, positive): “We cotransfected Stat3C into Stat3 / MEFs with vectors encoding WT RelA, RelA-K221R (221), RelA-K310R (310), or RelA-K218/221/ 310R (K/R) mutants, all of which have been reported to have markedly reduced acetylation (Chen et al., 2002).”
Shaping the nuclear action of NF-κB (2004, background): “Three main acetylation sites have been identified within RELA — lysines 218, 221 and 310 (Ref”
Dangerous liaisons: STAT3 and NF-κB collaboration and crosstalk in cancer (2009, background): “Acetylated RelA interacts only weakly with I-kBa, and its deacetylation by histone deacetylases (HDACs)markedly increases IkBa binding, and therefore results in its nuclear export and deactivation [64].”
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase (2004, methodology): “In addition, data obtained from site-directed RelA/p65 mutants, 1–317(K310R) and 1–317 (K314R), con- curred with previous studies (Chen et al, 2002) that p300- mediated acetylation occurred predominantly at lysine 310 on the RelA/p65 protein.”
Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, background): “Lys-221 acetylation enhances RelA DNA binding, and in conjunction with Lys-218 acetylation, inhibits the association of RelA with newly synthesized IkBa, which otherwise could act to relocate NF-kB complexes to the cytoplasm (Chen et al., 2002).”
NF-κB RelA Phosphorylation Regulates RelA Acetylation (2005, methodology): “Deacetylation of lysine 310 by histone deacetylase 3 (HDAC3) or SIRT1 inhibits the transcriptional activity of RelA and augments cellular apoptosis in response to TNF- ( 6 , 32).”
NF-κB activation as a pathological mechanism of septic shock and inflammation (2006, neutral): “Acetylation at Lys221 enhances p65 DNA binding, impairs its assembly with I- B , and reduces NF- B dimer nuclear exportation, resulting increased NF- B activity (42).”