Evidence map›Paper›PMID 36562946›Full record

ArticlePlant molecular biology2023

Barley RIC157, a potential RACB scaffold protein, is involved in susceptibility to powdery mildew.

Stefan Engelhardt, Adriana Trutzenberg, Michaela Kopischke, Katja Probst, Christopher McCollum, Johanna Hofer, Ralph Hückelhoven

Open access · hybridAbstract read
In one paragraph

Article in Plant molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

7 citing papers in PubMed, 9 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

7 authors at 1 institution in 1 country.

Stefan EngelhardtPhytopathology, TUM School of Life Sciences, Technical University of Munich, Emil- Ramann-Str.2, 85354, Freising-Weihenstephan, Germany.ORCID http://orcid.org/0000-0003-1933-1160
Adriana TrutzenbergPhytopathology, TUM School of Life Sciences, Technical University of Munich, Emil- Ramann-Str.2, 85354, Freising-Weihenstephan, Germany.
Michaela KopischkePhytopathology, TUM School of Life Sciences, Technical University of Munich, Emil- Ramann-Str.2, 85354, Freising-Weihenstephan, Germany.
Katja ProbstPhytopathology, TUM School of Life Sciences, Technical University of Munich, Emil- Ramann-Str.2, 85354, Freising-Weihenstephan, Germany.
Christopher McCollumPhytopathology, TUM School of Life Sciences, Technical University of Munich, Emil- Ramann-Str.2, 85354, Freising-Weihenstephan, Germany.
Johanna HoferPhytopathology, TUM School of Life Sciences, Technical University of Munich, Emil- Ramann-Str.2, 85354, Freising-Weihenstephan, Germany.
Ralph HückelhovenPhytopathology, TUM School of Life Sciences, Technical University of Munich, Emil- Ramann-Str.2, 85354, Freising-Weihenstephan, Germany. hueckelhoven@tum.de.ORCID http://orcid.org/0000-0001-5632-5451
Technical University of Munich · DE

Funding

Deutsche Forschungsgemeinschaft SFB924, HE6432/8, HU886/8
6 · The paper itself

Abstract

key messageCRIB motif-containing barley RIC157 is a novel ROP scaffold protein that interacts directly with barley RACB, promotes susceptibility to fungal penetration, and colocalizes with RACB at the haustorial neck. Successful obligate pathogens benefit from host cellular processes. For the biotrophic ascomycete fungus Blumeria hordei (Bh) it has been shown that barley RACB, a small monomeric G-protein (ROP, Rho of plants), is required for full susceptibility to fungal penetration. The susceptibility function of RACB probably lies in its role in cell polarity, which may be co-opted by the pathogen for invasive ingrowth of its haustorium. However, how RACB supports fungal penetration success and which other host proteins coordinate this process is incompletely understood. RIC (ROP-Interactive and CRIB-(Cdc42/Rac Interactive Binding) motif-containing) proteins are considered scaffold proteins which can interact directly with ROPs via a conserved CRIB motif. Here we describe a previously uncharacterized barley RIC protein, RIC157, which can interact directly with RACB in planta. We show that, in the presence of constitutively activated RACB, RIC157 shows a localization at the cell periphery/plasma membrane, whereas it otherwise localizes to the cytoplasm. RIC157 appears to mutually stabilize the plasma membrane localization of the activated ROP. During fungal infection, RIC157 and RACB colocalize at the penetration site, particularly at the haustorial neck. Additionally, transiently overexpressed RIC157 renders barley epidermal cells more susceptible to fungal penetration. We discuss that RIC157 may promote fungal penetration into barley epidermal cells by operating probably downstream of activated RACB.

Indexed as

AscomycotaHordeumPlant ProteinsPlant ProteinsBarleyCRIB-domainGTPasePowdery mildewScaffoldSusceptibility

Identifiers

PMID36562946
PMCPMC10090020
OpenAlexW4312114209

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.