Evidence map›Paper›PMID 37612136›Full record

ArticleGenes & development2023

Histidine N1-position-specific methyltransferase CARNMT1 targets C3H zinc finger proteins and modulates RNA metabolism.

Tadahiro Shimazu, Rei Yoshimoto, Kaoru Kotoshiba, Takehiro Suzuki, Shogo Matoba, Michiko Hirose, Mai Akakabe, Yoshihiro Sohtome, Mikiko Sodeoka, Atsuo Ogura and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Substrate selectivity of human histidine methyltransferase METTL9.Protein science : a publication of the Protein Society · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 2 countries.

Tadahiro Shimazu *Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama 351-0198, Japan; yshinkai@riken.jp tshimazu@riken.jp.
Rei Yoshimoto *Department of Applied Biological Sciences, Faculty of Agriculture, Setsunan University, Hirakata, Osaka 573-0101, Japan.
Kaoru KotoshibaCellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama 351-0198, Japan.
Takehiro SuzukiBiomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Shogo MatobaBioresource Engineering Division, RIKEN Bioresource Research Center, Tsukuba, Ibaraki 305-0074, Japan.ORCID 0000-0003-0474-232X
Michiko HiroseBioresource Engineering Division, RIKEN Bioresource Research Center, Tsukuba, Ibaraki 305-0074, Japan.
Mai AkakabeSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama 351-0198, Japan.
Yoshihiro SohtomeSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama 351-0198, Japan.
Mikiko SodeokaSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama 351-0198, Japan.
Atsuo OguraBioresource Engineering Division, RIKEN Bioresource Research Center, Tsukuba, Ibaraki 305-0074, Japan.
Naoshi DohmaeBiomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Yoichi ShinkaiCellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama 351-0198, Japan; yshinkai@riken.jp tshimazu@riken.jp.ORCID 0000-0002-6051-2484
RIKEN Center for Sustainable Resource Science · JPRIKEN BioResource Research Center · JPPioneer (United States) · USPioneer (Japan) · JPSetsunan University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histidine (His) residues are methylated in various proteins, but their roles and regulation mechanisms remain unknown. Here, we show that carnosine N-methyltransferase 1 (CARNMT1), a known His methyltransferase of dipeptide carnosine (βAla-His), is a major His N1-position-specific methyltransferase. We found that 52 His sites in 20 proteins underwent CARNMT1-mediated methylation. The consensus methylation site for CARNMT1 was identified as Cx(F/Y)xH, a C3H zinc finger (C3H ZF) motif. CARNMT1-deficient and catalytically inactive mutant mice showed embryonic lethality. Among the CARNMT1 target C3H ZF proteins, RNA degradation mediated by Roquin and tristetraprolin (TTP) was affected by CARNMT1 and its enzymatic activity. Furthermore, the recognition of the 3' splice site of the CARNMT1 target C3H ZF protein U2AF1 was perturbed, and pre-mRNA alternative splicing (AS) was affected by CARNMT1 deficiency. These findings indicate that CARNMT1-mediated protein His methylation, which is essential for embryogenesis, plays roles in diverse aspects of RNA metabolism by targeting C3H ZF-type RNA-binding proteins and modulating their functions, including pre-mRNA AS and mRNA degradation regulation.

Indexed as

CarnosineProtein MethyltransferasesAnimalsHistidineMiceMice, Inbred C3HRNA PrecursorsRNA Splice SitesZinc FingersCarnmt1 protein, mouseCarnosineHistidineProtein MethyltransferasesRNA PrecursorsRNA Splice SitesCARNMT1degradationembryonic developmentembryonic lethalityhistidinemethylationmethyltransferasemRNAsplicingU2AF1zinc finger protein

Identifiers

PMID37612136
PMCPMC10546975
OpenAlexW4386086067

What Socratic holds

Textmetadata
LicenceCC BY-NC
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.