Evidence map›Paper›PMID 18599656›Full record

ArticlePlant physiology2008

A novel role for protein farnesylation in plant innate immunity.

Sandra Goritschnig, Tabea Weihmann, Yuelin Zhang, Pierre Fobert, Peter McCourt, Xin Li

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
7.8field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
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  15. Alternative splicing in plant immunity.International journal of molecular sciences · 2014
    Review
  16. Article
  17. Article
  18. Article
  19. The roles of ABA in plant-pathogen interactions.Journal of plant research · 2011
    Review
  20. 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

6 authors at 2 institutions in 2 countries.

Sandra GoritschnigMichael Smith Laboratories , University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4.
Tabea Weihmann
Yuelin Zhang
Pierre Fobert
Peter McCourt
Xin Li
National Institute of Biological Sciences, Beijing · CNUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants utilize tightly regulated mechanisms to defend themselves against pathogens. Initial recognition results in activation of specific Resistance (R) proteins that trigger downstream immune responses, in which the signaling networks remain largely unknown. A point mutation in SUPPRESSOR OF NPR1 CONSTITUTIVE1 (SNC1), a RESISTANCE TO PERONOSPORA PARASITICA4 R gene homolog, renders plants constitutively resistant to virulent pathogens. Genetic suppressors of snc1 may carry mutations in genes encoding novel signaling components downstream of activated R proteins. One such suppressor was identified as a novel loss-of-function allele of ENHANCED RESPONSE TO ABSCISIC ACID1 (ERA1), which encodes the beta-subunit of protein farnesyltransferase. Protein farnesylation involves attachment of C15-prenyl residues to the carboxyl termini of specific target proteins. Mutant era1 plants display enhanced susceptibility to virulent bacterial and oomycete pathogens, implying a role for farnesylation in basal defense. In addition to its role in snc1-mediated resistance, era1 affects several other R-protein-mediated resistance responses against bacteria and oomycetes. ERA1 acts partly independent of abscisic acid and additively with the resistance regulator NON-EXPRESSOR OF PR GENES1 in the signaling network. Defects in geranylgeranyl transferase I, a protein modification similar to farnesylation, do not affect resistance responses, indicating that farnesylation is most likely specifically required in plant defense signaling. Taken together, we present a novel role for farnesyltransferase in plant-pathogen interactions, suggesting the importance of protein farnesylation, which contributes to the specificity and efficacy of signal transduction events.

Indexed as

Immunity, InnateProtein PrenylationAbscisic AcidAlkyl and Aryl TransferasesAmino Acid SequenceArabidopsisArabidopsis ProteinsBase SequenceCodon, InitiatorFarnesyltranstransferaseMolecular Sequence DataMutationPlant DiseasesSignal TransductionAbscisic AcidAlkyl and Aryl TransferasesArabidopsis ProteinsCodon, InitiatorERA1 protein, ArabidopsisFarnesyltranstransferasegeranylgeranyltransferase type-INPR1 protein, ArabidopsisSNC1 protein, Arabidopsis

Identifiers

PMID18599656
PMCPMC2528093
OpenAlexW2094030937

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.