Evidence map›Paper›PMID 32581155›Full record

ArticleCell structure and function2020

Internalization of AMPA-type Glutamate Receptor in the MIN6 Pancreatic β-cell Line.

The Mon La, Hiroshi Yamada, Sayaka Seiriki, Shun-Ai Li, Kenshiro Fujise, Natsuho Katsumi, Tadashi Abe, Masami Watanabe, Kohji Takei

Open access · goldAbstract read
In one paragraph

Article in Cell structure and function, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. 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

9 authors at 2 institutions in 1 country.

The Mon LaDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
Hiroshi YamadaDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
Sayaka SeirikiDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
Shun-Ai LiCenter for Innovative Clinical Medicine, Okayama University Hospital.
Kenshiro FujiseDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
Natsuho KatsumiDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
Tadashi AbeDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
Masami WatanabeCenter for Innovative Clinical Medicine, Okayama University Hospital.
Kohji TakeiDepartment of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences.
Okayama University · JPOkayama University Hospital · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of AMPA-type glutamate receptor is involved in insulin release from pancreatic β-cells. However, the mechanism and dynamics that underlie AMPA receptor-mediated insulin release in β-cells is largely unknown. Here, we show that AMPA induces internalization of glutamate receptor 2/3 (GluR2/3), AMPA receptor subtype, in the mouse β-cell line MIN6. Immunofluorescence experiments showed that GluR2/3 appeared as fine dots that were distributed throughout MIN6 cells. Intracellular GluR2/3 co-localized with AP2 and clathrin, markers for clathrin-coated pits and vesicles. Immunoelectron microscopy revealed that GluR2/3 was also localized at plasma membrane. Surface biotinylation and immunofluorescence measurements showed that addition of AMPA caused an approximate 1.8-fold increase in GluR2/3 internalization under low-glucose conditions. Furthermore, internalized GluR2 largely co-localized with EEA1, an early endosome marker. In addition, GluR2/3 co-immunoprecipitated with cortactin, a F-actin binding protein. Depletion of cortactin by RNAi in MIN6 cells altered the intracellular distribution of GluR2/3, suggesting that cortactin is involved in internalization of GluR2/3 in MIN6 cells. Taken together, our results suggest that pancreatic β-cells adjust the amount of AMPA-type GluR2/3 on the cell surface to regulate the receptive capability of the cell for glutamate.Key words: endocytosis, GluR2, AMPA, cortactin, MIN6.

Indexed as

Cell LineClathrinFatty Acid-Binding ProteinsGlutamic AcidHumansInsulin-Secreting CellsReceptors, AMPAClathrinFABP4 protein, humanFatty Acid-Binding Proteinsglutamate receptor ionotropic, AMPA 3Glutamic AcidReceptors, AMPAAMPAcortactinendocytosisGluR2MIN6

Identifiers

PMID32581155
PMCPMC10511061
OpenAlexW3037845967

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.