Evidence map›Paper›PMID 39758820›Full record

ArticleiScience2025

Heme regulates protein interactions and phosphorylation of BACH2 intrinsically disordered region in humoral response.

Miki Watanabe-Matsui, Shun Kadoya, Kei Segawa, Hiroki Shima, Tadashi Nakagawa, Yuko Nagasawa, Shuichiro Hayashi, Mitsuyo Matsumoto, Mariko Ikeda, Akihiko Muto and 7 more

Abstract read
In one paragraph

Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
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

17 authors.

Miki Watanabe-MatsuiDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Shun KadoyaDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Kei SegawaPharmaceutical Discovery Research Laboratories, Teijin Pharma Limited, Tokyo, Japan.
Hiroki ShimaDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Tadashi NakagawaDivision of Cell Proliferation, ART, Tohoku University Graduate School of Medicine, Sendai, Japan.
Yuko NagasawaDivision of Cell Proliferation, ART, Tohoku University Graduate School of Medicine, Sendai, Japan.
Shuichiro HayashiDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Mitsuyo MatsumotoDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Mariko IkedaLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Akihiko MutoDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Kyoko OchiaiDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Long C NguyenDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Katsumi Doh-UraDepartment of Neurochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.
Mikako ShirouzuLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama, Japan.
Keiko NakayamaDivision of Cell Proliferation, ART, Tohoku University Graduate School of Medicine, Sendai, Japan.
Kazutaka MurayamaDivision of Biomedical Measurements and Diagnostics, Tohoku University Graduate School of Biomedical Engineering, Sendai, Japan.
Kazuhiko IgarashiDepartment of Biochemistry, Tohoku University Graduate School of Medicine, Sendai, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heme is known to bind to the intrinsically disordered region (IDR) to regulate protein function. The binding of heme to the IDR of transcription factor BACH2 promotes plasma cell differentiation, but the molecular basis is unknown. Heme was found to increase BACH2 IDR interaction with TANK-binding kinase 1 (TBK1). TBK1 inactivated BACH2 by phosphorylation of its IDR, whereas BACH2 repressed TBK1 gene expression. BACH2 phosphorylation by TBK1 inhibited its interaction with the co-repressor NCOR1 and promoted plasma cell differentiation. Heme also induced BACH2 binding to ubiquitin E3 ligase adaptor FBXO22, which polyubiquitinated BACH2 only in the presence of heme

Indexed as

BiochemistryStructural biology

Identifiers

PMID39758820
PMCPMC11699347

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.