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

Regulation of NF-kappaB activation in T cells via association of the adapter proteins ADAP and CARMA1.

Science (New York, N.Y.) - 4 May 2007

Medeiros Ricardo B, Burbach Brandon J, Mueller Kristen L, Srivastava Rupa, Moon James J, Highfill Sarah, Peterson Erik J, Shimizu Yoji

Abstract excerpt

The adapter protein ADAP regulates T lymphocyte adhesion and activation. We present evidence for a previously unrecognized function for ADAP in regulating T cell receptor (TCR)-mediated activation of the transcription factor NF-kappaB. Stimulation of ADAP-deficient mouse T cells with antibodies to CD3 and CD28 resulted in impaired nuclear translocation of NF-kappaB, a reduced DNA binding, and delayed degradation...

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to CARD Signaling Adaptor Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Caspases

Share to CD28 Antigens

Share to CD3 Complex

Share to I-kappa B Proteins

Share to Jurkat Cells

Share to Transcription Factor RelA

Source

Identifiers

PMID: 17478723
DOI: 10.1126/science.1137895

Genes

MALT1

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

Regulation of NF-kappaB activation in T cells via association of the adapter proteins ADAP and CARMA1.PMID 17478723Read ↗

The pleckstrin homology domain in the SKAP55 adapter protein defines the ability of the adapter protein ADAP to regulate integrin function and NF-kappaB activation.Semantic proximity Read ↗

HPK1 competes with ADAP for SLP‐76 binding and <i>via</i> Rap1 negatively affects T‐cell adhesionSemantic proximity Read ↗

SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesionSemantic proximity Read ↗

CD3/CD28 costimulation-induced NF-kappaB activation is mediated by recruitment of protein kinase C-theta, Bcl10, and IkappaB kinase beta to the immunological synapse through CARMA1.Semantic proximity Read ↗

A mutation within the SH2 domain of slp-76 regulates the tissue distribution and cytokine production of iNKT cells in mice.Semantic proximity Read ↗

Phosphorylation of CARMA1 by HPK1 is critical for NF-kappaB activation in T cells.Semantic proximity Read ↗

Functional defects of SKAP-55-deficient T cells identify a regulatory role for the adaptor in LFA-1 adhesion.Semantic proximity Read ↗

MAGUK-controlled ubiquitination of CARMA1 modulates lymphocyte NF-kappaB activity.Semantic proximity Read ↗

Clustering of CARMA1 through SH3-GUK domain interactions is required for its activation of NF-κB signalling.Semantic proximity Read ↗

SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility.Semantic proximity Read ↗

The adapter proteins LAT and SLP-76 are required for T-cell activation.Semantic proximity Read ↗

NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation.Semantic proximity Read ↗

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