Evidence map›Paper›PMID 30712282›Full record

ArticleThe Plant journal : for cell and molecular biology2019

Medicago falcata MfSTMIR, an E3 ligase of endoplasmic reticulum-associated degradation, is involved in salt stress response.

Rongxue Zhang, Hong Chen, Mei Duan, Fugui Zhu, Jiangqi Wen, Jiangli Dong, Tao Wang

Open access · hybridAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

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  11. Roles of E3 Ubiquitin Ligases in Plant Responses to Abiotic Stresses.International journal of molecular sciences · 2022
    Review
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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

7 authors at 3 institutions in 2 countries.

Rongxue ZhangState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Hong ChenState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Mei DuanState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Fugui ZhuState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Jiangqi WenPlant Biology Division, Samuel Roberts Noble Research Institute, Ardmore, Oklahoma, 73401, USA.
Jiangli DongState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Tao WangState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
China Agricultural University · CNNoble Research Institute · USTianjin Academy of Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent studies on E3 of endoplasmic reticulum (ER)-associated degradation (ERAD) in plants have revealed homologs in yeast and animals. However, it remains unknown whether the plant ERAD system contains a plant-specific E3 ligase. Here, we report that MfSTMIR, which encodes an ER-membrane-localized RING E3 ligase that is highly conserved in leguminous plants, plays essential roles in the response of ER and salt stress in Medicago. MfSTMIR expression was induced by salt and tunicamycin (Tm). mtstmir loss-of-function mutants displayed impaired induction of the ER stress-responsive genes BiP1/2 and BiP3 under Tm treatment and sensitivity to salt stress. MfSTMIR promoted the degradation of a known ERAD substrate, CPY*. MfSTMIR interacted with the ERAD-associated ubiquitin-conjugating enzyme MtUBC32 and Sec61-translocon subunit MtSec61γ. MfSTMIR did not affect MtSec61γ protein stability. Our results suggest that the plant-specific E3 ligase MfSTMIR participates in the ERAD pathway by interacting with MtUBC32 and MtSec61γ to relieve ER stress during salt stress.

Indexed as

Arabidopsis ProteinsEndoplasmic Reticulum-Associated DegradationEndoplasmic Reticulum StressGene Expression Regulation, PlantMedicagoMolecular ChaperonesPlant ProteinsProtein StabilitySalt StressSEC Translocation ChannelsTunicamycinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesArabidopsis ProteinsBiP1 protein, ArabidopsisBiP2 protein, ArabidopsisBiP3 protein, ArabidopsisMolecular ChaperonesPlant ProteinsSEC Translocation ChannelsTunicamycinUBC32 protein, ArabidopsisUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasesendoplasmic reticulum-associated degradationendoplasmic reticulum stressMedicagosalt stressunfolded protein response

Identifiers

PMID30712282
PMCPMC6849540
OpenAlexW2913820830

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.