Evidence map›Paper›PMID 27609422›Full record

ArticleMolecular & cellular proteomics : MCP2016

Novel Aquaporin Regulatory Mechanisms Revealed by Interactomics.

Jorge Bellati, Chloé Champeyroux, Sonia Hem, Valérie Rofidal, Gabriel Krouk, Christophe Maurel, Véronique Santoni

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
23.3field-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

37 citing papers in PubMed, 91 citations in OpenAlex.

  1. Overexpression ofPlants (Basel, Switzerland) · 2026
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  14. Salt stress proteins in plants: An overview.Frontiers in plant science · 2022
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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 1 country.

Jorge BellatiFrom the ‡Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier, F-34060 Montpellier, Cedex 2, France.
Chloé ChampeyrouxFrom the ‡Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier, F-34060 Montpellier, Cedex 2, France.
Sonia HemFrom the ‡Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier, F-34060 Montpellier, Cedex 2, France.
Valérie RofidalFrom the ‡Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier, F-34060 Montpellier, Cedex 2, France.
Gabriel KroukFrom the ‡Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier, F-34060 Montpellier, Cedex 2, France.
Christophe MaurelFrom the ‡Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier, F-34060 Montpellier, Cedex 2, France.
Véronique SantoniFrom the ‡Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, UMR 5004 CNRS/UMR 0386 INRA/Montpellier SupAgro/Université Montpellier, F-34060 Montpellier, Cedex 2, France santoniv@supagro.inra.fr.
Centre National de la Recherche Scientifique · FRInstitut des Sciences des Plantes de Montpellier · FRUniversité de Montpellier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PIP1;2 and PIP2;1 are aquaporins that are highly expressed in roots and bring a major contribution to root water transport and its regulation by hormonal and abiotic factors. Interactions between cellular proteins or with other macromolecules contribute to forming molecular machines. Proteins that molecularly interact with PIP1;2 and PIP2;1 were searched to get new insights into regulatory mechanisms of root water transport. For that, a immuno-purification strategy coupled to protein identification and quantification by mass spectrometry (IP-MS) of PIPs was combined with data from the literature, to build thorough PIP1;2 and PIP2;1 interactomes, sharing about 400 interacting proteins. Such interactome revealed PIPs to behave as a platform for recruitment of a wide range of transport activities and provided novel insights into regulation of PIP cellular trafficking by osmotic and oxidative treatments. This work also pointed a role of lipid signaling in PIP function and enhanced our knowledge of protein kinases involved in PIP regulation. In particular we show that 2 members of the receptor-like kinase (RLK) family (RKL1 (At1g48480) and Feronia (At3g51550)) differentially modulate PIP activity through distinct molecular mechanisms. The overall work opens novel perspectives in understanding PIP regulatory mechanisms and their role in adjustment of plant water status.

Indexed as

AquaporinsArabidopsisArabidopsis ProteinsDatabases, ProteinGene Expression Regulation, PlantMass SpectrometryMembrane ProteinsPhosphotransferasesPlant RootsProtein Interaction MapsProtein KinasesProtein Serine-Threonine KinasesAquaporinsArabidopsis ProteinsAt2g45960 protein, ArabidopsisAt3g51550 protein, ArabidopsisMembrane ProteinsPhosphotransferasesplasma membrane intrinsic protein 2 ArabidopsisProtein KinasesProtein Serine-Threonine KinasesRKL1 protein, Arabidopsis

Identifiers

PMID27609422
PMCPMC5098044
OpenAlexW2516044865

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.