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

Serine residues in the LAT adaptor are essential for TCR-dependent signal transduction.

Journal of leukocyte biology - 1 Jan 2011

Martínez-Florensa Mario, García-Blesa Antonio, Yélamos José, Muñoz-Suano Alba, Domínguez-Villar Margarita, Valdor Rut, Alonso Antonio, García-Cózar Francisco, Aparicio Pedro, Malissen Bernard, Aguado Enrique

Abstract excerpt

The adaptor protein LAT has a prominent role in the transduction of intracellular signals elicited by the TCR/CD3 complex. Upon TCR engagement, LAT becomes tyrosine-phosphorylated and thereby, recruits to the membrane several proteins implicated in the activation of downstream signaling pathways....

Read the complete abstract on PubMed

Topics

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

Share to Interleukin-2
Share to Jurkat Cells
Share to Mitogen-Activated Protein Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Phospholipase C gamma

Share to Phosphotyrosine

Share to Receptors, Antigen, T-Cell

Share to ZAP-70 Protein-Tyrosine Kinase

Source

Identifiers

PMID: 20940326
DOI: 10.1189/jlb.0509342

Genes

LAT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20940326-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Serine residues in the LAT adaptor are essential for TCR-dependent signal transduction.PMID 20940326Read ↗

Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line.Semantic proximity Read ↗

Mutation of the glycine residue preceding the sixth tyrosine of the LAT adaptor severely alters T cell development and activation.Semantic proximity Read ↗

Activation of T lymphocytes and the role of the adapter LAT.Semantic proximity Read ↗

Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell angigen receptor-mediated signaling.Semantic proximity Read ↗

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

Loss of the LAT adaptor converts antigen-responsive T cells into pathogenic effectors that function independently of the T cell receptor.Semantic proximity Read ↗

Early onset combined immunodeficiency and autoimmunity in patients with loss-of-function mutation in LAT.Semantic proximity Read ↗

The role of LAT-PLCγ1 interaction in γδ T cell development and homeostasis.Semantic proximity Read ↗

Mutation of the phospholipase C-gamma1-binding site of LAT affects both positive and negative thymocyte selection.Semantic proximity Read ↗

Th2 lymphoproliferative disorders resulting from defective LAT signalosomes.Semantic proximity Read ↗

LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway.Semantic proximity Read ↗

LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation.Semantic proximity Read ↗

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