Evidence map›Paper›PMID 21423366›Full record

ArticleFrontiers in physiology2010

A membrane protein/signaling protein interaction network for Arabidopsis version AMPv2.

Sylvie Lalonde, Antoinette Sero, Réjane Pratelli, Guillaume Pilot, Jin Chen, Maria I Sardi, Saman A Parsa, Do-Young Kim, Biswa R Acharya, Erica V Stein and 14 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
7.5field-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

62 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
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  6. TheInternational journal of molecular sciences · 2023
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  13. The Regulatory Network ofInternational journal of molecular sciences · 2020
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2 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

24 authors at 1 institution in 1 country.

Sylvie LalondeDepartment of Plant Biology, Carnegie Institution for Science Stanford, CA, USA. slalonde@stanford.edu
Antoinette Sero
Réjane Pratelli
Guillaume Pilot
Jin Chen
Maria I Sardi
Saman A Parsa
Do-Young Kim
Biswa R Acharya
Erica V Stein
Heng-Chen Hu
Florent Villiers
Kouji Takeda
Yingzhen Yang
Yong S Han
Rainer Schwacke
William Chiang
Naohiro Kato
Dominique Loqué
Sarah M Assmann
June M Kwak
Julian I Schroeder
Seung Y Rhee
Wolf B Frommer
Department of Plant Biology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interactions between membrane proteins and the soluble fraction are essential for signal transduction and for regulating nutrient transport. To gain insights into the membrane-based interactome, 3,852 open reading frames (ORFs) out of a target list of 8,383 representing membrane and signaling proteins from Arabidopsis thaliana were cloned into a Gateway-compatible vector. The mating-based split ubiquitin system was used to screen for potential protein-protein interactions (pPPIs) among 490 Arabidopsis ORFs. A binary robotic screen between 142 receptor-like kinases (RLKs), 72 transporters, 57 soluble protein kinases and phosphatases, 40 glycosyltransferases, 95 proteins of various functions, and 89 proteins with unknown function detected 387 out of 90,370 possible PPIs. A secondary screen confirmed 343 (of 386) pPPIs between 179 proteins, yielding a scale-free network (r(2) = 0.863). Eighty of 142 transmembrane RLKs tested positive, identifying 3 homomers, 63 heteromers, and 80 pPPIs with other proteins. Thirty-one out of 142 RLK interactors (including RLKs) had previously been found to be phosphorylated; thus interactors may be substrates for respective RLKs. None of the pPPIs described here had been reported in the major interactome databases, including potential interactors of G-protein-coupled receptors, phospholipase C, and AMT ammonium transporters. Two RLKs found as putative interactors of AMT1;1 were independently confirmed using a split luciferase assay in Arabidopsis protoplasts. These RLKs may be involved in ammonium-dependent phosphorylation of the C-terminus and regulation of ammonium uptake activity. The robotic screening method established here will enable a systematic analysis of membrane protein interactions in fungi, plants and metazoa.

Indexed as

kinasephosphorylationprotein interactionreceptorsplit ubiquitin systemtransportyeast two hybrid

Identifiers

PMID21423366
PMCPMC3059934
OpenAlexW2114908564

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.