Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The ubiquitin ligase PUB22 targets a subunit of the exocyst complex required for PAMP-triggered responses in Arabidopsis.

The Plant cell - 1 Nov 2012

Stegmann Martin, Anderson Ryan G, Ichimura Kazuya, Pecenkova Tamara, Reuter Patrick, Žársky Viktor, McDowell John M, Shirasu Ken, Trujillo Marco

Abstract excerpt

Plant pathogens are perceived by pattern recognition receptors, which are activated upon binding to pathogen-associated molecular patterns (PAMPs). Ubiquitination and vesicle trafficking have been linked to the regulation of immune signaling. However, little information exists about components of vesicle trafficking involved in immune signaling and the mechanisms that regulate them. In this study, we identified...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Oomycetes
Share to Proteasome Endopeptidase Complex

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proteolysis

Share to Pseudomonas syringae

Share to Receptors, Pattern Recognition

Share to Ubiquitin

Share to Ubiquitination

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23170036
DOI: 10.1105/tpc.112.104463
PMCID: PMC3531861

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The ubiquitin ligase PUB22 targets a subunit of the exocyst complex required for PAMP-triggered responses in Arabidopsis.PMID 23170036Read ↗

The exocyst subunit Exo70B1 is involved in the immune response of Arabidopsis thaliana to different pathogens and cell death.Semantic proximity Read ↗

Ubiquitylome analysis reveals a central role for the ubiquitin-proteasome system in plant innate immunitySemantic proximity Read ↗

Ubiquitylome Analysis Reveals a Central Role for the Ubiquitin-Proteasome System in Plant Innate ImmunitySemantic proximity Read ↗

The dominant negative ARM domain uncovers multiple functions of PUB13 in Arabidopsis immunity, flowering, and senescence.Semantic proximity Read ↗

Deubiquitinating enzymes AtUBP12 and AtUBP13 and their tobacco homologue NtUBP12 are negative regulators of plant immunity.Semantic proximity Read ↗

A truncated NLR protein, TIR-NBS2, is required for activated defense responses in the exo70B1 mutant.Semantic proximity Read ↗

TOLs Function as Ubiquitin Receptors in the Early Steps of the ESCRT Pathway in Higher Plants.Semantic proximity Read ↗

Ubiquitination in the rice blast fungus Magnaporthe oryzae: from development and pathogenicity to stress responsesSemantic proximity Read ↗

Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis.Semantic proximity Read ↗

The Proteasome Acts as a Hub for Plant Immunity and Is Targeted by Pseudomonas Type III Effectors.Semantic proximity Read ↗

The RING-Type E3 Ligase XBAT35.2 Is Involved in Cell Death Induction and Pathogen ResponseSemantic proximity Read ↗

Multi-tiered pairing selectivity between E2 ubiquitin–conjugating enzymes and E3 ligasesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.