Evidence map›Paper›PMID 28158631›Full record

ArticlePlant & cell physiology2017

Visualization of Phosphatidylinositol 3,5-Bisphosphate Dynamics by a Tandem ML1N-Based Fluorescent Protein Probe in Arabidopsis.

Tomoko Hirano, Kelly Stecker, Teun Munnik, Haoxing Xu, Masa H Sato

Open access · bronzeAbstract read
In one paragraph

Article in Plant & cell physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Imaging Plant Lipids with Fluorescent Reporters.Plants (Basel, Switzerland) · 2024
    Review
  5. Exploring lipid-protein interactions in plant membranes.Journal of experimental botany · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Phospholipids in Salt Stress Response.Plants (Basel, Switzerland) · 2021
    Review
  10. Article
  11. DownregulatingFrontiers in plant science · 2020
    Article
  12. Review
  13. Review
  14. Phosphoinositides control the localization of HOPS subunit VPS41, which together with VPS33 mediates vacuole fusion in plants.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. ArabidopsisPlant physiology · 2018
    Article
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

5 authors at 4 institutions in 3 countries.

Tomoko HiranoLaboratory of Cellular Dynamics, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Shimogamo-nakaragi-cho, Sakyo-ku, Kyoto, 606-8522 Japan.
Kelly SteckerBiotechnology Center, University of Wisconsin, Madison, WI 53706, USA.
Teun MunnikSection of Plant Physiology, Swammerdam Institute for Life Sciences, University of Amsterdam, Science park 904, 1098 XH Amsterdam 94216, The Netherlands.
Haoxing XuDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Masa H SatoLaboratory of Cellular Dynamics, Graduate School of Life and Environmental Sciences, Kyoto Prefectural University, Shimogamo-nakaragi-cho, Sakyo-ku, Kyoto, 606-8522 Japan.
Kyoto Prefectural University · JPUniversity of Amsterdam · NLUniversity of Michigan–Ann Arbor · USUniversity of Wisconsin–Madison · US

Funding

The Mucolipin TRP Ion ChannelsR01NS062792 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI XU, HAOXING · 2009 to 2018
$3.3M
NINDS NIH HHS R01 NS062792
6 · The paper itself

Abstract

Phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2] is a low-abundance phospholipid known to be associated with a wide variety of physiological functions in plants. However, the localization and dynamics of PI(3,5)P2 in plant cells remain largely unknown, partially due to the lack of an effective fluorescent probe. Using Arabidopsis transgenic plant expressing the PI(3,5)P2-labeling fluorescent probe (tagRFP-ML1N*2) developed based on a tandem repeat of the cytosolic phosphoinositide-interacting domain (ML1N) of the mammalian lysosomal transient receptor potential cation channel, Mucolipin 1 (TRPML1), here we show that PI(3,5)P2 is predominantly localized on the limited membranes of the FAB1- and SNX1-positive late endosomes, but rarely localized on the membranes of plant vacuoles or trans-Golgi network/early endosomes of cortical cells of the root differentiation zone. The late endosomal localization of tagRFP-ML1N*2 is reduced or abolished by pharmacological inhibition or genetic knockdown of expression of genes encoding PI(3,5)P2-synthesizing enzymes, FAB1A/B, but markedly increased with FAB1A overexpression. Notably, reactive oxygen species (ROS) significantly increase late endosomal levels of PI(3,5)P2. Thus, tandem ML1N-based PI(3,5)P2 probes can reliably monitor intracellular dynamics of PI(3,5)P2 in Arabidopsis cells with less binding activity to other endomembrane organelles.

Indexed as

ArabidopsisEndosomesFluorescent DyesLuminescent ProteinsLysosomesMicroscopy, ConfocalPhosphatidylinositol PhosphatesPhosphatidylinositolsPlant RootsPlants, Genetically ModifiedReactive Oxygen SpeciesRecombinant Fusion ProteinsRed Fluorescent Proteintrans-Golgi NetworkTransport VesiclesVacuolesFluorescent DyesLuminescent Proteinsphosphatidylinositol 3,5-diphosphatePhosphatidylinositol PhosphatesPhosphatidylinositolsReactive Oxygen SpeciesRecombinant Fusion ProteinsRed Fluorescent ProteinArabidopsisFluorescent protein probeLate endosomesML1N*2PI(3,5)P2YM201636

Identifiers

PMID28158631
PMCPMC5921506
OpenAlexW2585076094

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.