Evidence map›Paper›PMID 37190106›Full record

ArticleCells2023

Fyn Phosphorylates Transglutaminase 2 (Tgm2) and Modulates Autophagy and p53 Expression in the Development of Diabetic Kidney Disease.

Ryota Uehara, Eijiro Yamada, Shuichi Okada, Claire C Bastie, Akito Maeshima, Hidekazu Ikeuchi, Kazuhiko Horiguchi, Masanobu Yamada

Open access · goldAbstract read
In one paragraph

Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-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

11 citing papers in PubMed, 9 citations in OpenAlex.

  1. Elucidating the therapeutic targets and multi-target mechanisms of salvianolic acid A for diabetic nephropathy.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
  2. Article
  3. Post‑translational modifications in diabetic kidney disease (Review).International journal of molecular medicine · 2026
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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

8 authors at 3 institutions in 2 countries.

Ryota UeharaDepartment of Internal Medicine, Division of Endocrinology and Metabolism, Gunma University Graduate School of Medicine, 3-39-15, Showa, Maebashi 371-8511, Japan.ORCID 0000-0002-0511-036X
Eijiro YamadaDepartment of Internal Medicine, Division of Endocrinology and Metabolism, Gunma University Graduate School of Medicine, 3-39-15, Showa, Maebashi 371-8511, Japan.ORCID 0000-0002-0332-8605
Shuichi OkadaDepartment of Internal Medicine, Division of Endocrinology and Metabolism, Gunma University Graduate School of Medicine, 3-39-15, Showa, Maebashi 371-8511, Japan.ORCID 0000-0003-1403-6840
Claire C BastieDivision of Biomedical Sciences, Warwick Medical School, Coventry CV4 7AL, UK.
Akito MaeshimaDepartment of Nephrology and Hypertension, Saitama Medical Center, Saitama Medical University, 1981 Kamoda, Kawagoe 350-1298, Japan.
Hidekazu IkeuchiDepartment of Nephrology and Rheumatology, Gunma University Graduate School of Medicine, Maebashi 371-8511, Japan.ORCID 0000-0002-0768-7090
Kazuhiko HoriguchiDepartment of Internal Medicine, Division of Endocrinology and Metabolism, Gunma University Graduate School of Medicine, 3-39-15, Showa, Maebashi 371-8511, Japan.
Masanobu YamadaDepartment of Internal Medicine, Division of Endocrinology and Metabolism, Gunma University Graduate School of Medicine, 3-39-15, Showa, Maebashi 371-8511, Japan.
Gunma University · JPSocial Insurance Saitama Chuo Hospital · JPUniversity of Warwick · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is involved in the development of diabetic kidney disease (DKD), the leading cause of end-stage renal disease. The Fyn tyrosine kinase (Fyn) suppresses autophagy in the muscle. However, its role in kidney autophagic processes is unclear. Here, we examined the role of Fyn kinase in autophagy in proximal renal tubules both in vivo and in vitro. Phospho-proteomic analysis revealed that transglutaminase 2 (Tgm2), a protein involved in the degradation of p53 in the autophagosome, is phosphorylated on tyrosine 369 (Y369) by Fyn. Interestingly, we found that Fyn-dependent phosphorylation of Tgm2 regulates autophagy in proximal renal tubules in vitro, and that p53 expression is decreased upon autophagy in Tgm2-knockdown proximal renal tubule cell models. Using streptozocin (STZ)-induced hyperglycemic mice, we confirmed that Fyn regulated autophagy and mediated p53 expression via Tgm2. Taken together, these data provide a molecular basis for the role of the Fyn-Tgm2-p53 axis in the development of DKD.

Indexed as

Diabetes MellitusDiabetic NephropathiesAnimalsAutophagyMiceProtein Glutamine gamma Glutamyltransferase 2ProteomicsTumor Suppressor Protein p53Protein Glutamine gamma Glutamyltransferase 2Tumor Suppressor Protein p53autophagydiabeticend-stage renal diseasehyperglycemiakidney

Identifiers

PMID37190106
PMCPMC10136856
OpenAlexW4366597778

What OpenQuestion 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 OpenQuestion graph.