Evidence map›Paper›PMID 22010034›Full record

ArticleThe Plant cell2011

Single-molecule analysis of PIP2;1 dynamics and partitioning reveals multiple modes of Arabidopsis plasma membrane aquaporin regulation.

Xiaojuan Li, Xiaohua Wang, Yong Yang, Ruili Li, Qihua He, Xiaohong Fang, Doan-Trung Luu, Christophe Maurel, Jinxing Lin

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
10.1field-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

112 citing papers in PubMed, 267 citations in OpenAlex.

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  13. AtPIP1;4 and AtPIP2;4 Cooperatively Mediate HPlants (Basel, Switzerland) · 2024
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  17. Involvement of the Membrane Nanodomain Protein,International journal of molecular sciences · 2023
    Article
  18. Article
  19. Article
  20. Review

52 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

9 authors at 7 institutions in 2 countries.

Xiaojuan LiKey Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Xiaohua Wang
Yong Yang
Ruili Li
Qihua He
Xiaohong Fang
Doan-Trung Luu
Christophe Maurel
Jinxing Lin
Institute of Botany · CNUniversity of Chinese Academy of Sciences · CNBeijing National Laboratory for Molecular Sciences · CNChinese Academy of Sciences · CNInstitut Agro Montpellier · FRInstitut des Sciences des Plantes de Montpellier · FRPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PIP2;1 is an integral membrane protein that facilitates water transport across plasma membranes. To address the dynamics of Arabidopsis thaliana PIP2;1 at the single-molecule level as well as their role in PIP2;1 regulation, we tracked green fluorescent protein-PIP2;1 molecules by variable-angle evanescent wave microscopy and fluorescence correlation spectroscopy (FCS). Single-particle tracking analysis revealed that PIP2;1 presented four diffusion modes with large dispersion of diffusion coefficients, suggesting that partitioning and dynamics of PIP2;1 are heterogeneous and, more importantly, that PIP2;1 can move into or out of membrane microdomains. In response to salt stress, the diffusion coefficients and percentage of restricted diffusion increased, implying that PIP2;1 internalization was enhanced. This was further supported by the decrease in PIP2;1 density on plasma membranes by FCS. We additionally demonstrated that PIP2;1 internalization involves a combination of two pathways: a tyrphostin A23-sensitive clathrin-dependent pathway and a methyl-β-cyclodextrin-sensitive, membrane raft-associated pathway. The latter was efficiently stimulated under NaCl conditions. Taken together, our findings demonstrate that PIP2;1 molecules are heterogeneously distributed on the plasma membrane and that clathrin and membrane raft pathways cooperate to mediate the subcellular trafficking of PIP2;1, suggesting that the dynamic partitioning and recycling pathways might be involved in the multiple modes of regulating water permeability.

Indexed as

AquaporinsArabidopsisArabidopsis Proteinsbeta-CyclodextrinsCell MembraneClathrinGreen Fluorescent ProteinsModels, BiologicalPermeabilityPlant RootsPlants, Genetically ModifiedProtein TransportRecombinant Fusion ProteinsSodium ChlorideStress, PhysiologicalWaterAquaporinsArabidopsis Proteinsbeta-CyclodextrinsClathrinGreen Fluorescent Proteinsmethyl-beta-cyclodextrinplasma membrane intrinsic protein 2 ArabidopsisRecombinant Fusion ProteinsSodium ChlorideWater

Identifiers

PMID22010034
PMCPMC3229149
OpenAlexW2120770189

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.