Evidence map›Paper›PMID 27538481›Full record

ArticleScientific reports2016

Glucosidase II β-subunit, a novel substrate for caspase-3-like activity in rice, plays as a molecular switch between autophagy and programmed cell death.

Jing Cui, Bing Chen, Hongjuan Wang, Yue Han, Xi Chen, Wei Zhang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  5. Transcriptome-Wide NFrontiers in microbiology · 2021
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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

6 authors at 1 institution in 1 country.

Jing CuiDept. of Biochemistry &Molecular Biology, College of Life Science, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Bing ChenDept. of Biochemistry &Molecular Biology, College of Life Science, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Hongjuan WangDept. of Biochemistry &Molecular Biology, College of Life Science, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Yue HanDept. of Biochemistry &Molecular Biology, College of Life Science, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Xi ChenDept. of Biochemistry &Molecular Biology, College of Life Science, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Wei ZhangDept. of Biochemistry &Molecular Biology, College of Life Science, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Nanjing Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoplasmic reticulum (ER) stress activates unfolded protein response (UPR) and autophagy. However, prolonged, severe stresses activate programmed cell death (PCD) in both animal and plant cells. Compared to the well-studied UPR pathway, the molecular mechanisms of ER-stress-induced PCD are less understood. Here, we report the identification of Gas2, the glucosidase II β subunit in the ER, as a potential switch between PCD and autophagy in rice. MS analysis identified Gas2, GRP94, and HSP40 protein in a purified caspase-3-like activity from heat stressed rice cell suspensions. The three corresponding genes were down-regulated under DTT-induced ER stress. Gas2 and GRP94 were localized to the ER, while HSP40 localized to the cytoplasm. Compared to wild-type, a Gas2 RNAi cell line was much sensitive to DTT treatment and had high levels of autophagy. Both caspase-3 and heat-stressed cell suspension lysate could cleave Gas2, producing a 14 kDa N-terminal fragment. Conditional expression of corresponding C-terminal fragment resulted in enhanced caspase-3-like activity in the protoplasts under heat stress. We proposed that mild ER stress causes down-regulation of Gas2 and induces autophagy, while severe stress results in Gas2 cleavage by caspase-3-like activity and the cleavage product amplifies this activity, possibly participating in the initiation of PCD.

Indexed as

AutophagyEndoplasmic Reticulum StressEryptosisalpha-GlucosidasesCaspase 3OryzaPlant ProteinsSeedlings4-nitrophenyl-alpha-glucosidasealpha-GlucosidasesCaspase 3Plant Proteins

Identifiers

PMID27538481
PMCPMC4990886
OpenAlexW2509670537

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.