Evidence map›Paper›PMID 35064188›Full record

ArticleExperimental & molecular medicine2022

SENP2 regulates mitochondrial function and insulin secretion in pancreatic β cells.

Jinyan Nan, Ji Seon Lee, Joon Ho Moon, Seung-Ah Lee, Young Joo Park, Dong-Sup Lee, Sung Soo Chung, Kyong Soo Park

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

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  13. Mitochondrial Dynamics and Insulin Secretion.International journal of molecular sciences · 2023
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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 2 institutions in 2 countries.

Jinyan NanDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, Korea.
Ji Seon LeeDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, Korea.
Joon Ho MoonDepartment of Internal Medicine, Seoul National University College of Medicine, Seoul, Korea.
Seung-Ah LeeGenomic Medicine Institute, Seoul National University Medical Research Center, Seoul, Korea.
Young Joo ParkDepartment of Internal Medicine, Seoul National University College of Medicine, Seoul, Korea.ORCID http://orcid.org/0000-0002-3671-6364
Dong-Sup LeeDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, Korea.
Sung Soo ChungBiomedical Research Institute, Seoul National University Hospital, Seoul, Korea. suschung@snu.ac.kr.
Kyong Soo ParkDepartment of Internal Medicine, Seoul National University College of Medicine, Seoul, Korea. kspark@snu.ac.kr.ORCID http://orcid.org/0000-0003-3597-342X
Seoul National University · KRSeoul National University Hospital · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Increasing evidence has shown that small ubiquitin-like modifier (SUMO) modification plays an important role in metabolic regulation. We previously demonstrated that SUMO-specific protease 2 (SENP2) is involved in lipid metabolism in skeletal muscle and adipogenesis. In this study, we investigated the function of SENP2 in pancreatic β cells by generating a β cell-specific knockout (Senp2-βKO) mouse model. Glucose tolerance and insulin secretion were significantly impaired in the Senp2-βKO mice. In addition, glucose-stimulated insulin secretion (GSIS) was decreased in the islets of the Senp2-βKO mice without a significant change in insulin synthesis. Furthermore, islets of the Senp2-βKO mice exhibited enlarged mitochondria and lower oxygen consumption rates, accompanied by lower levels of S616 phosphorylated DRP1 (an active form of DRP1), a mitochondrial fission protein. Using a cell culture system of NIT-1, an islet β cell line, we found that increased SUMO2/3 conjugation to DRP1 due to SENP2 deficiency suppresses the phosphorylation of DRP1, which possibly induces mitochondrial dysfunction. In addition, SENP2 overexpression restored GSIS impairment induced by DRP1 knockdown and increased DRP1 phosphorylation. Furthermore, palmitate treatment decreased phosphorylated DRP1 and GSIS in β cells, which was rescued by SENP2 overexpression. These results suggest that SENP2 regulates mitochondrial function and insulin secretion at least in part by modulating the phosphorylation of DRP1 in pancreatic β cells.

Indexed as

Insulin-Secreting CellsAnimalsCysteine EndopeptidasesGlucoseInsulinInsulin SecretionMiceMitochondriaMitochondrial ProteinsPeptide HydrolasesCysteine EndopeptidasesGlucoseInsulinMitochondrial ProteinsPeptide HydrolasesSenp2 protein, mouse

Identifiers

PMID35064188
PMCPMC8814193
OpenAlexW4205260910

What OpenQuestion holds

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LicenceCC BY
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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.