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Article

The cytoplasmic domain of CD4 is required for stable association with the lymphocyte-specific tyrosine protein kinase p56lck.

European journal of immunology - 1 Jun 1990

Veillette A, Sleckman B P, Ratnofsky S, Bolen J B, Burakoff S J

Abstract excerpt

The CD4 T cell surface molecule binds MHC class II determinants expressed on antigen-presenting cells. CD4 is thought to enhance T cell activation by serving as an adhesion molecule as well as possibly by transducing an independent intracellular signal during the process of antigen stimulation. The recent observation that CD4 is physically associated with the Src-related tyrosine protein kinase p56lck suggests...

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Source

Identifiers

PMID: 2369920
DOI: 10.1002/eji.1830200628

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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.

Related research

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The cytoplasmic domain of CD4 is required for stable association with the lymphocyte-specific tyrosine protein kinase p56lck.PMID 2369920Read ↗

Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs.Semantic proximity Read ↗

The protein tyrosine kinase p56lck inhibits CD4 endocytosis by preventing entry of CD4 into coated pits.Semantic proximity Read ↗

Cloning of ACP33 as a novel intracellular ligand of CD4.Semantic proximity Read ↗

Genetic and immunochemical evidence for CD4-dependent association of p56lck with the alpha beta T-cell receptor (TCR): regulation of TCR-induced activation.Semantic proximity Read ↗

Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck.Semantic proximity Read ↗

The unique amino-terminal domain of p56lck regulates interactions with tyrosine protein phosphatases in T lymphocytes.Semantic proximity Read ↗

Cytotoxic T lymphocyte antigen 4 (CTLA-4) engagement delivers an inhibitory signal through the membrane-proximal region in the absence of the tyrosine motif in the cytoplasmic tail.Semantic proximity Read ↗

Interaction of the cytoplasmic tail of CTLA-4 (CD152) with a clathrin-associated protein is negatively regulated by tyrosine phosphorylation.Semantic proximity Read ↗

CTLA-4 interacts with STAT5 and inhibits STAT5-mediated transcription.Semantic proximity Read ↗

Residues Y429 and Y463 of the human CD5 are targeted by protein tyrosine kinases.Semantic proximity Read ↗

Interaction of CTLA-4 with AP50, a clathrin-coated pit adaptor proteinSemantic proximity Read ↗

HLA-DR polymorphism affects the interaction with CD4.Semantic proximity Read ↗

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