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Article

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

The Journal of cell biology - 1 Apr 1992

Pelchen-Matthews A, Boulet I, Littman D R, Fagard R, Marsh M

Abstract excerpt

The lymphocyte glycoprotein CD4 is constitutively internalized and recycled in nonlymphoid cells, but is excluded from the endocytic pathway in lymphocytic cells (Pelchen-Matthews, A., J. E. Armes, G. Griffiths, and M. Marsh. 1991. J. Exp. Med. 173: 575-587). Inhibition of CD4 endocytosis is dependent on CD4 expressing an intact cytoplasmic domain and is only observed in cells where CD4 can interact with the...

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Identifiers

PMID: 1373141
DOI: 10.1083/jcb.117.2.279
PMCID: PMC2289416

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The protein tyrosine kinase p56lck inhibits CD4 endocytosis by preventing entry of CD4 into coated pits.PMID 1373141Read ↗

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

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

Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization.Semantic proximity Read ↗

The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase.Semantic proximity Read ↗

Platelet-derived growth factor receptor-beta (PDGFR-beta) activation promotes its association with the low density lipoprotein receptor-related protein (LRP). Evidence for co-receptor function.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 ↗

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

Phosphorylation-dependent down-modulation of CD4 requires a specific structure within the cytoplasmic domain of CD4.Semantic proximity Read ↗

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

Role of clathrin-coated vesicles in glycoprotein transport from the cell surface to the Golgi complex.Semantic proximity Read ↗

Interaction of CTLA-4 with the clathrin-associated protein AP50 results in ligand-independent endocytosis that limits cell surface expression.Semantic proximity Read ↗

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