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 RING-finger scaffold protein Plenty of SH3s targets TAK1 to control immunity signalling in Drosophila.

EMBO reports - 1 Nov 2005

Tsuda Manabu, Langmann Caillin, Harden Nicholas, Aigaki Toshiro

Abstract excerpt

Imd-mediated innate immunity is activated in response to infection by Gram-negative bacteria and leads to the activation of Jun amino-terminal kinase (JNK) and Relish, a nuclear factor-kappaB transcription factor responsible for the expression of antimicrobial peptides. Plenty of SH3s (POSH) has been shown to function as a scaffold protein for JNK activation, leading to apoptosis in mammals. Here, we report that...

Read the complete abstract on PubMed

Topics

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

Share to Cytoskeletal Proteins
Share to Feedback, Physiological

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Silencing

Share to JNK Mitogen-Activated Protein Kinases

Share to Lipopolysaccharides

Share to MAP Kinase Kinase Kinases

Share to Phosphoprotein Phosphatases

Share to Ubiquitin-Protein Ligases

Source

Open in PubMed Open full text

Identifiers

PMID: 16179944
DOI: 10.1038/sj.embor.7400537
PMCID: PMC1371032

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The RING-finger scaffold protein Plenty of SH3s targets TAK1 to control immunity signalling in Drosophila.PMID 16179944Read ↗

Cooperative control of Drosophila immune responses by the JNK and NF-kappaB signaling pathways.Semantic proximity Read ↗

Hyd ubiquitinates the NF-κB co-factor Akirin to activate an effective immune response in <i>Drosophila</i>Semantic proximity Read ↗

The Kinase IKKβ Regulates a STING- and NF-κB-Dependent Antiviral Response Pathway in DrosophilaSemantic proximity Read ↗

Akirin specifies NF-κB selectivity of Drosophila innate immune response via chromatin remodeling.Semantic proximity Read ↗

The protein Dredd is an essential component of the c-Jun N-terminal kinase pathway in the Drosophila immune response.Semantic proximity Read ↗

A non-redundant role for Drosophila Mkk4 and hemipterous/Mkk7 in TAK1-mediated activation of JNK.Semantic proximity Read ↗

Systems analysis identifies an essential role for SHANK-associated RH domain-interacting protein (SHARPIN) in macrophage Toll-like receptor 2 (TLR2) responses.Semantic proximity Read ↗

E3 ligase SAUL1 serves as a positive regulator of PAMP-triggered immunity and its homeostasis is monitored by immune receptor SOC3.Semantic proximity Read ↗

Caspar, a suppressor of antibacterial immunity in Drosophila.Semantic proximity Read ↗

Activation of the JNK pathway during dorsal closure in Drosophila requires the mixed lineage kinase, slipper.Semantic proximity Read ↗

CATERPILLER: a novel gene family important in immunity, cell death, and diseases.Semantic proximity Read ↗

Modular Architecture of the STING C-Terminal Tail Allows Interferon and NF-κB Signaling AdaptationSemantic proximity Read ↗

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