Evidence map›Paper›PMID 33931009›Full record

ArticleCellular & molecular biology letters2021

Effect of the glycine-rich domain in GAREM2 on its unique subcellular localization upon EGF stimulation.

Tasuku Nishino, Tsuyoshi Oshika, Moriatsu Kyan, Hiroaki Konishi

Open access · goldAbstract readLetter
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular & molecular biology letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Review
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

4 authors at 2 institutions in 1 country.

Tasuku NishinoFaculty of Life and Environmental Sciences, Prefectural University of Hiroshima, Shobara, Hiroshima, 727-0023, Japan.
Tsuyoshi OshikaDivision of Bioscience and Biotechnology Department of Agricultural and Life Sciences, Faculty of Agriculture, Shinshu University, 8304 Minamiminowa, Nagano, 399-4598, Japan.
Moriatsu KyanDivision of Bioscience and Biotechnology Department of Agricultural and Life Sciences, Faculty of Agriculture, Shinshu University, 8304 Minamiminowa, Nagano, 399-4598, Japan.
Hiroaki KonishiDivision of Bioscience and Biotechnology Department of Agricultural and Life Sciences, Faculty of Agriculture, Shinshu University, 8304 Minamiminowa, Nagano, 399-4598, Japan. hkonishi@shinshu-u.ac.jp.ORCID http://orcid.org/0000-0003-2875-3816
Shinshu University · JPPrefectural University of Hiroshima · JP

Funding

Japan Society for the Promotion of Science 17K07341Japan Society for the Promotion of Science Grant No. 20K06548
6 · The paper itself

Abstract

backgroundIn mammals, there are two subtypes of Grb2-associated regulator of Erk/MAPK (GAREM), an adaptor protein that functions downstream of the cell growth factor receptor. GAREM1 is ubiquitously expressed, whereas GAREM2 is mainly expressed in the brain. However, the precise mechanism of the translocation of each GAREM subtype in growth factor-stimulated cells is still unclear.

methodsIn this study, immunofluorescence staining with specific antibodies against each GAREM subtype and time-lapse analysis using GFP fusion proteins were used to analyze the subcellular localization of each GAREM subtype in a cell growth stimulus-dependent manner. We also biochemically analyzed the correlation between its subcellular localization and tyrosine phosphorylation of GAREM2.

resultsWe found that endogenously and exogenously expressed GAREM2 specifically aggregated and formed granules in NGF-stimulated PC-12 cells and in EGF-stimulated COS-7 cells. Based on the observed subcellular localizations of chimeric GAREM1 and GAREM2 proteins, a glycine-rich region, which is present only in GAREM2, is required for the observed granule formation. This region also regulates the degree of EGF-stimulation-dependent tyrosine phosphorylation of GAREM2.

conclusionsOur results, showing that aggregation of GAREM2 in response to EGF stimulation is dependent on a glycine-rich region, suggest that GAREM2 aggregation may be involved in neurodegenerative diseases.

Indexed as

AnimalsApoptosisChlorocebus aethiopsCOS CellsEpidermal Growth FactorGRB2 Adaptor ProteinHumansPhosphorylationProtein AggregatesProtein DomainsTime-Lapse ImagingEpidermal Growth FactorGAREM1 protein, humanGAREM2 protein, humanGRB2 Adaptor ProteinProtein AggregatesAdaptor proteinEGF receptorGlycine-richProtein aggregationTyrosine phosphorylation

Identifiers

PMID33931009
PMCPMC8086153
OpenAlexW3158164340

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.