Evidence map›Paper›PMID 35642916›Full record

ArticlePlant physiology2022

Friend or foe: Hybrid proline-rich proteins determine how plants respond to beneficial and pathogenic microbes.

Zeeshan Z Banday, Nicolás M Cecchini, DeQuantarius J Speed, Allison T Scott, Claire Parent, Ciara T Hu, Rachael C Filzen, Elinam Agbo, Jean T Greenberg

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 16 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

Zeeshan Z BandayDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0003-0598-3475
Nicolás M CecchiniDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0002-2894-7744
DeQuantarius J SpeedDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0003-3701-1603
Allison T ScottDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0001-8880-3796
Claire ParentDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0003-4190-0841
Ciara T HuDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0003-0160-1708
Rachael C FilzenDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0001-9380-2595
Elinam AgboDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.
Jean T GreenbergDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 60637, USA.ORCID 0000-0002-7213-7618
University of Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Howard Hughes Medical InstituteNIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Plant plastids generate signals, including some derived from lipids, that need to be mobilized to effect signaling. We used informatics to discover potential plastid membrane proteins involved in microbial responses in Arabidopsis (Arabidopsis thaliana). Among these are proteins co-regulated with the systemic immunity component AZELAIC ACID INDUCED 1, a hybrid proline-rich protein (HyPRP), and HyPRP superfamily members. HyPRPs have a transmembrane domain, a proline-rich region (PRR), and a lipid transfer protein domain. The precise subcellular location(s) and function(s) are unknown for most HyPRP family members. As predicted by informatics, a subset of HyPRPs has a pool of proteins that target plastid outer envelope membranes via a mechanism that requires the PRR. Additionally, two HyPRPs may be associated with thylakoid membranes. Most of the plastid- and nonplastid-localized family members also have pools that localize to the endoplasmic reticulum, plasma membrane, or plasmodesmata. HyPRPs with plastid pools regulate, positively or negatively, systemic immunity against the pathogen Pseudomonas syringae. HyPRPs also regulate the interaction with the plant growth-promoting rhizobacteria Pseudomonas simiae WCS417 in the roots to influence colonization, root system architecture, and/or biomass. Thus, HyPRPs have broad and distinct roles in immunity, development, and growth responses to microbes and reside at sites that may facilitate signal molecule transport.

Indexed as

ArabidopsisArabidopsis ProteinsPlantsPlastidsProlinePseudomonas syringaeArabidopsis ProteinsProline

Identifiers

PMID35642916
PMCPMC9434206
OpenAlexW4281686672

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.