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Article

Functional hierarchy of the N-terminal tyrosines of SLP-76.

Journal of immunology (Baltimore, Md. : 1950) - 15 Feb 2006

Jordan Martha S, Sadler Jeffrey, Austin Jessica E, Finkelstein Lisa D, Singer Andrew L, Schwartzberg Pamela L, Koretzky Gary A

Abstract excerpt

The adaptor protein Src homology 2 domain-containing leukocyte phosphoprotein of 76 kDa (SLP-76) plays a central role in T cell activation and T cell development. SLP-76 has three functional modules: an acidic domain with three key tyrosines, a central proline-rich domain, and a C-terminal Src homology 2 domain. Of these, mutation of the three N-terminal tyrosines (Y112, Y128, and Y145) results in the most...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 16456002
DOI: 10.4049/jimmunol.176.4.2430

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Functional hierarchy of the N-terminal tyrosines of SLP-76.PMID 16456002Read ↗

SRC homology 2 domain-containing leukocyte phosphoprotein of 76 kDa (SLP-76) N-terminal tyrosine residues regulate a dynamic signaling equilibrium involving feedback of proximal T-cell receptor (TCR) signaling.Semantic proximity Read ↗

Mutation of tyrosine 145 of lymphocyte cytosolic protein 2 protects mice from anaphylaxis and arthritis.Semantic proximity Read ↗

Complementation in trans of altered thymocyte development in mice expressing mutant forms of the adaptor molecule SLP76.Semantic proximity Read ↗

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Differential role of SLP-76 domains in T cell development and function.Semantic proximity Read ↗

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