Evidence map›Paper›PMID 28689659›Full record

ArticleMolecular cell2017

Bcl3 Phosphorylation by Akt, Erk2, and IKK Is Required for Its Transcriptional Activity.

Vivien Ya-Fan Wang, Yidan Li, Daniel Kim, Xiangyang Zhong, Qian Du, Majid Ghassemian, Gourisankar Ghosh

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Unveiling the multifaceted roles of BCL3: biological functions and disease implications.Apoptosis : an international journal on programmed cell death · 2026
    Review
  3. Article
  4. Review
  5. Regulation and Function of the Atypical IκBs-Bcl-3, IκBEuropean journal of immunology · 2025
    Review
  6. Article
  7. Article
  8. Review
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  11. Review
  12. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 2 countries.

Vivien Ya-Fan WangFaculty of Health Sciences, University of Macau, Avenida da Universidade, Taipa, Macau SAR, China; Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, USA.
Yidan LiDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, USA.
Daniel KimDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, USA.
Xiangyang ZhongDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, USA.
Qian DuDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, USA.
Majid GhassemianDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, USA.
Gourisankar GhoshDepartment of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA, USA. Electronic address: gghosh@ucsd.edu.
University of California, San Diego · US

Funding

Investigation of Gene Regulation by NF-kappaB Transcription factorsR01GM085490 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GHOSH, GOURISANKAR · 2009 to 2023
$3.8M
Processing of NF-kB2/P100R01AI064326 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GHOSH, GOURISANKAR · 2005 to 2015
$3.2M
IKK:Biophysical basis of dynamic regulationR01CA141722 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GHOSH, GOURISANKAR, HOFFMANN, ALEXANDER · 2009 to 2013
$2.7M
NCI NIH HHS R01 CA141722NIAID NIH HHS R01 AI064326NIGMS NIH HHS R01 GM085490
6 · The paper itself

Abstract

Unlike prototypical IκB proteins, which are inhibitors of NF-κB RelA, cRel, and RelB dimers, the atypical IκB protein Bcl3 is primarily a transcriptional coregulator of p52 and p50 homodimers. Bcl3 exists as phospho-protein in many cancer cells. Unphosphorylated Bcl3 acts as a classical IκB-like inhibitor and removes p50 and p52 from bound DNA. Neither the phosphorylation site(s) nor the kinase(s) phosphorylating Bcl3 is known. Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. Cells expressing the S114A/S446A mutant have cellular proliferation and migration defects. This work links Akt and MAPK pathways to NF-κB through Bcl3 and provides mechanistic insight into how Bcl3 functions as an oncoprotein through collaboration with IKK1/2, Akt, and Erk2.

Indexed as

Transcription, GeneticActive Transport, Cell NucleusAnimalsB-Cell Lymphoma 3 ProteinCell MovementCell ProliferationHEK293 CellsHeLa CellsHumansI-kappa B KinaseMiceMitogen-Activated Protein Kinase 1MutationNF-kappa B p50 SubunitNF-kappa B p52 SubunitPhosphorylationAKT2 protein, humanB-Cell Lymphoma 3 ProteinBCL3 protein, humanBcl3 protein, mouseCHUK protein, humanI-kappa B KinaseIKBKB protein, humanMAPK1 protein, humanMitogen-Activated Protein Kinase 1NF-kappa B p50 SubunitNF-kappa B p52 SubunitNFKB1 protein, humanNFKB2 protein, humanProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSerineTranscription FactorsAktBcl3Erk2IKKNF-κBphosphorylation

Identifiers

PMID28689659
PMCPMC6571149
OpenAlexW2734281802

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.