2022
DOI: 10.1021/acschembio.2c00678
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Site-Selective Tyrosine Phosphorylation in the Activation of the p50 Subunit of NF-κB for DNA Binding and Transcription

Abstract: The family of NF-κB transcriptional activators controls the expression of many genes, including those involved in cell survival and development. The family consists of homo-and heterodimers constituted by combinations of five subunits. Subunit p50 includes 13 tyrosine residues, but the relationship between specific tyrosine phosphorylations and p50 function is not well understood. Subunits of p50 and p65 prepared in vitro formed a heterodimer, but this NF-κB would not bind to the interleukin-2 (IL-2) promoter … Show more

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Cited by 4 publications
(6 citation statements)
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“…Weakly fluorescent thiazole dipeptidomimetic 5 , and several congeners, exhibits dramatic alteration of its photophysical properties when positioned within structured domains of proteins. ,, Finally, by the introduction of phosphotyrosine (pTyr) ( 6 ) at a single position of inhibitory protein IκB-α, we have identified a possible new property of this protein in regulating DNA strand exchange by NF-κB . Additionally, the introduction of 6 at discrete positions of NF-κB has enabled the regulation of DNA promoter binding and gene transcription/translation in experimental systems. , In the aggregate, these and related amino acid analogues have been incorporated into numerous proteins and peptides, and their incorporation has been studied by multiple analytical techniques including mass spectrometry.…”
Section: Results and Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Weakly fluorescent thiazole dipeptidomimetic 5 , and several congeners, exhibits dramatic alteration of its photophysical properties when positioned within structured domains of proteins. ,, Finally, by the introduction of phosphotyrosine (pTyr) ( 6 ) at a single position of inhibitory protein IκB-α, we have identified a possible new property of this protein in regulating DNA strand exchange by NF-κB . Additionally, the introduction of 6 at discrete positions of NF-κB has enabled the regulation of DNA promoter binding and gene transcription/translation in experimental systems. , In the aggregate, these and related amino acid analogues have been incorporated into numerous proteins and peptides, and their incorporation has been studied by multiple analytical techniques including mass spectrometry.…”
Section: Results and Discussionmentioning
confidence: 99%
“…44 Additionally, the introduction of 6 at discrete positions of NF-κB has enabled the regulation of DNA promoter binding and gene transcription/translation in experimental systems. 52,53 In the aggregate, these and related amino acid analogues have been incorporated into numerous proteins and peptides, and their incorporation has been studied by multiple analytical techniques including mass spectrometry.…”
Section: ■ Results and Discussionmentioning
confidence: 99%
“…Then, in 2021, Chen et al 281 encoded pTyr into the p50 subunit of NF-κB at positions Y60 and Y82, revealing that phosphorylation at these sites facilitated its binding to the CD40 promoter, resulting in increased CD40 expression. But interestingly, in 2023, 272 Chen et al showed this same phosphorylated form of NF-κB (with the p50 subunit phosphorylated at Y60) did not bind the IL-2 promoter, revealing how phosphorylation can tune which genes NF-κB activates for transcription. Instead, binding to the IL-2 promoter could be achieved if NF-κB was first phosphorylated at Y60 in the p50 subunit and after that was further phosphorylated by an unknown kinase in Jurkat cell extract.…”
Section: Expression Host Considerations For Ptyrmentioning
confidence: 99%
“…Using the cell-free encoding system with the modified 23S rRNA, Chen et al. ,, in a series of three studies sought to understand how Tyr phosphorylation of the IκB-α/NF-κB complex regulated gene transcription. When unmodified, IκB-α binds to the heterodimeric transcription factor NF-κB, masking the nuclear localization sequence of NF-κB and inhibiting its ability to bind promoter DNA.…”
Section: Development and Applications Of Phosphoamino Acid Gce Systemsmentioning
confidence: 99%
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