Evidence map›Paper›PMID 25538184›Full record

ArticleThe Plant cell2014

The Arabidopsis abiotic stress-induced TSPO-related protein reduces cell-surface expression of the aquaporin PIP2;7 through protein-protein interactions and autophagic degradation.

Charles Hachez, Vasko Veljanovski, Hagen Reinhardt, Damien Guillaumot, Celine Vanhee, François Chaumont, Henri Batoko

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
15.9field-weighted citation impact, top 1% 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

76 citing papers in PubMed, 152 citations in OpenAlex.

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16 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Charles HachezInstitut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium.
Vasko VeljanovskiInstitut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium.
Hagen ReinhardtInstitut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium.
Damien GuillaumotInstitut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium.
Celine VanheeInstitut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium.
François ChaumontInstitut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium.
Henri BatokoInstitut des Sciences de la Vie, Université Catholique de Louvain, 1348 Louvain-la-Neuve, Belgium henri.batoko@uclouvain.be.ORCID http://orcid.org/0000-0002-8256-519X
UCLouvain · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Arabidopsis thaliana multi-stress regulator TSPO is transiently induced by abiotic stresses. The final destination of this polytopic membrane protein is the Golgi apparatus, where its accumulation is strictly regulated, and TSPO is downregulated through a selective autophagic pathway. TSPO-related proteins regulate the physiology of the cell by generating functional protein complexes. A split-ubiquitin screen for potential TSPO interacting partners uncovered a plasma membrane aquaporin, PIP2;7. Pull-down assays and fluorescence imaging approaches revealed that TSPO physically interacts with PIP2;7 at the endoplasmic reticulum and Golgi membranes in planta. Intriguingly, constitutive expression of fluorescently tagged PIP2;7 in TSPO-overexpressing transgenic lines resulted in patchy distribution of the fluorescence, reminiscent of the pattern of constitutively expressed yellow fluorescent protein-TSPO in Arabidopsis. Mutational stabilization of TSPO or pharmacological inhibition of the autophagic pathway affected concomitantly the detected levels of PIP2;7, suggesting that the complex containing both proteins is degraded through the autophagic pathway. Coexpression of TSPO and PIP2;7 resulted in decreased levels of PIP2;7 in the plasma membrane and abolished the membrane water permeability mediated by transgenic PIP2;7. Taken together, these data support a physiological role for TSPO in regulating the cell-surface expression of PIP2;7 during abiotic stress conditions through protein-protein interaction and demonstrate an aquaporin regulatory mechanism involving TSPO.

Indexed as

AutophagyAquaporinsArabidopsisArabidopsis ProteinsEndoplasmic ReticulumGene Expression Regulation, PlantGolgi ApparatusMembrane ProteinsPlants, Genetically ModifiedAquaporinsArabidopsis ProteinsMembrane ProteinsTSPO-related protein, Arabidopsis

Identifiers

PMID25538184
PMCPMC4311218
OpenAlexW2118010772

What OpenQuestion holds

Textmetadata
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.