Evidence map›Paper›PMID 15728190›Full record

ArticleThe Journal of cell biology2005

A Sec14p-nodulin domain phosphatidylinositol transfer protein polarizes membrane growth of Arabidopsis thaliana root hairs.

Patrick Vincent, Michael Chua, Fabien Nogue, Ashley Fairbrother, Hal Mekeel, Yue Xu, Nina Allen, Tatiana N Bibikova, Simon Gilroy, Vytas A Bankaitis

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

87 citing papers in PubMed, 212 citations in OpenAlex.

  1. Article
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  6. Imaging Plant Lipids with Fluorescent Reporters.Plants (Basel, Switzerland) · 2024
    Review
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27 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

10 authors at 4 institutions in 2 countries.

Patrick VincentDepartment of Cell and Developmental Biology, Michael Hooker Microscopy Facility, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA. patrick_vincent@med.unc.edu
Michael Chua
Fabien Nogue
Ashley Fairbrother
Hal Mekeel
Yue Xu
Nina Allen
Tatiana N Bibikova
Simon Gilroy
Vytas A Bankaitis
University of North Carolina at Chapel Hill · USNorth Carolina State University · USPennsylvania State University · USDépartement Santé des Plantes et Environnement · FR

Funding

Role of the Phospholipids in Golgi Secretory FunctionR01GM044530 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BANKAITIS, VYTAS A · 1991 to 2019
$5.6M
NIGMS NIH HHS GM44530NIGMS NIH HHS R01 GM044530
6 · The paper itself

Abstract

Phosphatidylinositol (PtdIns) transfer proteins (PITPs) regulate signaling interfaces between lipid metabolism and membrane trafficking. Herein, we demonstrate that AtSfh1p, a member of a large and uncharacterized Arabidopsis thaliana Sec14p-nodulin domain family, is a PITP that regulates a specific stage in root hair development. AtSfh1p localizes along the root hair plasma membrane and is enriched in discrete plasma membrane domains and in the root hair tip cytoplasm. This localization pattern recapitulates that visualized for PtdIns(4,5)P2 in developing root hairs. Gene ablation experiments show AtSfh1p nullizygosity compromises polarized root hair expansion in a manner that coincides with loss of tip-directed PtdIns(4,5)P2, dispersal of secretory vesicles from the tip cytoplasm, loss of the tip f-actin network, and manifest disorganization of the root hair microtubule cytoskeleton. Derangement of tip-directed Ca2+ gradients is also apparent and results from isotropic influx of Ca2+ from the extracellular milieu. We propose AtSfh1p regulates intracellular and plasma membrane phosphoinositide polarity landmarks that focus membrane trafficking, Ca2+ signaling, and cytoskeleton functions to the growing root hair apex. We further suggest that Sec14p-nodulin domain proteins represent a family of regulators of polarized membrane growth in plants.

Indexed as

ActinsAmino Acid SequenceArabidopsisCalciumCell MembraneCytoplasmCytoskeletonGenes, ReporterMicroscopy, ElectronMolecular Sequence DataPhospholipid Transfer ProteinsPlant RootsProtein Structure, TertiaryActinsCalciumPhospholipid Transfer Proteins

Identifiers

PMID15728190
PMCPMC2171805
OpenAlexW2036047219

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.