Evidence map›Paper›PMID 26358044›Full record

ArticlePlant molecular biology2015

Molecular dissection of a rice microtubule-associated RING finger protein and its potential role in salt tolerance in Arabidopsis.

Sung Don Lim, Chang Gyo Jung, Yong Chan Park, Sung Chul Lee, Chanhui Lee, Chae Woo Lim, Dong Sub Kim, Cheol Seong Jang

Abstract read
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Article in Plant molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

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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 4 institutions in 1 country.

Sung Don LimDepartment of Applied Plant Sciences Technology, Kangwon National University, Chuncheon, 200-713, Korea.
Chang Gyo JungDepartment of Applied Plant Sciences Technology, Kangwon National University, Chuncheon, 200-713, Korea.
Yong Chan ParkDepartment of Applied Plant Sciences Technology, Kangwon National University, Chuncheon, 200-713, Korea.
Sung Chul LeeSchool of Biological Sciences, Chung-Ang University, Seoul, 156-756, Korea.
Chanhui LeeDepartment of Plant Environmental New Resources, KyungHee University, Yongin, 446-701, Korea.
Chae Woo LimSchool of Biological Sciences, Chung-Ang University, Seoul, 156-756, Korea.
Dong Sub KimAdanced Radiation Technology Institute, Korea Atomic Energy Research Institute, Jeongeup, 580-185, Korea.
Cheol Seong JangDepartment of Applied Plant Sciences Technology, Kangwon National University, Chuncheon, 200-713, Korea. csjang@kangwon.ac.kr.
Kangwon National University · KRChung-Ang University · KRKorea Atomic Energy Research Institute · KRKyung Hee University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although a number of RING E3 ligases in plants have been demonstrated to play key roles in a wide range of abiotic stresses, relatively few studies have detailed how RING E3 ligases exert their cellular actions. We describe Oryza sativa RING finger protein with microtubule-targeting domain 1 (OsRMT1), a functional RING E3 ligase that is likely involved in a salt tolerance mechanism. Functional characterization revealed that OsRMT1 undergoes homodimer formation and subsequently autoubiquitination-mediated protein degradation under normal conditions. By contrast, OsRMT1 is predominantly found in the nucleus and microtubules and its degradation is inhibited under salt stress. Domain dissection of OsRMT1 indicates that the N-terminal domain is required for microtubule targeting. Bimolecular fluorescence complementation analysis and degradation assay revealed that OsRMT1-interacted proteins localized in various organelles were degraded via the ubiquitin (Ub)/26S proteasome-dependent pathway. Interestingly, when OsRMT1 and its target proteins were co-expressed in N. benthamiana leaves, the protein-protein interactions appeared to take place mainly in the microtubules. Overexpression of OsRMT1 in Arabidopsis resulted in increased tolerance to salt stress. Our findings suggest that the abundance of microtubule-associated OsRMT1 is strictly regulated, and OsRMT1 may play a relevant role in salt stress response by modulating levels of its target proteins.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionArabidopsisGenes, PlantMicrotubulesMolecular Sequence DataMutagenesis, Site-DirectedOryzaPlant ProteinsPlants, Genetically ModifiedProteasome Endopeptidase ComplexProtein MultimerizationRecombinant ProteinsRING Finger DomainsSalt ToleranceSequence Homology, Amino AcidATP dependent 26S proteasePlant ProteinsProteasome Endopeptidase ComplexRecombinant ProteinsUbiquitin-Protein LigasesMicrotubulesRiceRING E3 ligaseSalt stressUbiquitination

Identifiers

PMID26358044
OpenAlexW1949351819

What OpenQuestion holds

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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.