Evidence map›Paper›PMID 24586161›Full record

ArticlePLoS pathogens2014

AvrBsT acetylates Arabidopsis ACIP1, a protein that associates with microtubules and is required for immunity.

Mi Sun Cheong, Angela Kirik, Jung-Gun Kim, Kenneth Frame, Viktor Kirik, Mary Beth Mudgett

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
16.8field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Structure-Function Characterisation of Eop1 Effectors from theInternational journal of molecular sciences · 2023
    Article
  12. The SbbHLH041-International journal of molecular sciences · 2023
    Article
  13. Article
  14. The Cytoskeleton in Plant Immunity: Dynamics, Regulation, and Function.International journal of molecular sciences · 2022
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. TALEN-BasedFrontiers in plant science · 2021
    Article
  20. Natural Variation in Virulence ofThe plant pathology journal · 2020
    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 1 country.

Mi Sun CheongDepartment of Biology, Stanford University, Stanford, California, United States of America.
Angela KirikSchool of Biological Sciences, Illinois State University, Normal, Illinois, United States of America.
Jung-Gun KimDepartment of Biology, Stanford University, Stanford, California, United States of America.
Kenneth FrameDepartment of Biology, Stanford University, Stanford, California, United States of America.
Viktor KirikSchool of Biological Sciences, Illinois State University, Normal, Illinois, United States of America.
Mary Beth MudgettDepartment of Biology, Stanford University, Stanford, California, United States of America.
Stanford University · USIllinois State University · US

Funding

Dissection of AvrBsT-BST defense pathway in ArabidopsisR01GM068886 · NIGMS · STANFORD UNIVERSITY · PI MUDGETT, MARY BETH · 2004 to 2013
$2.6M
Elucidating conserved mechanisms of noncentrosomal microtubule array formationR15GM102839 · NIGMS · ILLINOIS STATE UNIVERSITY · PI KIRIK, VIKTOR · 2013 to 2013
$288k
NIGMS NIH HHS 1R15GM102839-01A1NIGMS NIH HHS 2R01GM068886-06A1NIGMS NIH HHS R01 GM068886NIGMS NIH HHS R15 GM102839
6 · The paper itself

Abstract

Bacterial pathogens of plant and animals share a homologous group of virulence factors, referred to as the YopJ effector family, which are translocated by the type III secretion (T3S) system into host cells during infection. Recent work indicates that some of these effectors encode acetyltransferases that suppress host immunity. The YopJ-like protein AvrBsT is known to activate effector-triggered immunity (ETI) in Arabidopsis thaliana Pi-0 plants; however, the nature of its enzymatic activity and host target(s) has remained elusive. Here we report that AvrBsT possesses acetyltransferase activity and acetylates ACIP1 (for ACETYLATED INTERACTING PROTEIN1), an unknown protein from Arabidopsis. Genetic studies revealed that Arabidopsis ACIP family members are required for both pathogen-associated molecular pattern (PAMP)-triggered immunity and AvrBsT-triggered ETI during Pseudomonas syringae pathovar tomato DC3000 (Pst DC3000) infection. Microscopy studies revealed that ACIP1 is associated with punctae on the cell cortex and some of these punctae co-localize with microtubules. These structures were dramatically altered during infection. Pst DC3000 or Pst DC3000 AvrRpt2 infection triggered the formation of numerous, small ACIP1 punctae and rods. By contrast, Pst DC3000 AvrBsT infection primarily triggered the formation of large GFP-ACIP1 aggregates, in an acetyltransferase-dependent manner. Our data reveal that members of the ACIP family are new components of the defense machinery required for anti-bacterial immunity. They also suggest that AvrBsT-dependent acetylation in planta alters ACIP1's defense function, which is linked to the activation of ETI.

Indexed as

AcetylationArabidopsisArabidopsis ProteinsMicrotubulesPlant DiseasesPlants, Genetically ModifiedPolymerase Chain ReactionPseudomonas InfectionsPseudomonas syringaeTwo-Hybrid System TechniquesVirulence FactorsArabidopsis ProteinsVirulence Factors

Identifiers

PMID24586161
PMCPMC3930583
OpenAlexW2085283297

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.