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Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex

The high-affinity IL-2-R complex is composed of at least two distinct IL-2-binding subunits, including p55 (Tac, IL-2-R alpha) and p70 (IL-2- R beta). Using a radiolabeled mAb specific for the p55 receptor subunit and cells expressing a homogeneous population of high-affinity binding sites, we demon...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1988
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189118/
https://www.ncbi.nlm.nih.gov/pubmed/3263468
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description The high-affinity IL-2-R complex is composed of at least two distinct IL-2-binding subunits, including p55 (Tac, IL-2-R alpha) and p70 (IL-2- R beta). Using a radiolabeled mAb specific for the p55 receptor subunit and cells expressing a homogeneous population of high-affinity binding sites, we demonstrate that p55 is co-internalized with p70 after IL-2 binding to the receptor complex. Endocytosis of p55 depends upon the presence of IL-2 in a form capable of effectively interacting with the p70 subunit. Whether IL-2 is required for high-affinity receptor assembly or triggering of the internalization of preassembled receptors remains unresolved. Together, these findings support the existence of a stable, high-affinity human IL-2-R membrane complex composed of at least the p55 and p70 receptor subunits and IL-2.
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spelling pubmed-21891182008-04-17 Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex J Exp Med Articles The high-affinity IL-2-R complex is composed of at least two distinct IL-2-binding subunits, including p55 (Tac, IL-2-R alpha) and p70 (IL-2- R beta). Using a radiolabeled mAb specific for the p55 receptor subunit and cells expressing a homogeneous population of high-affinity binding sites, we demonstrate that p55 is co-internalized with p70 after IL-2 binding to the receptor complex. Endocytosis of p55 depends upon the presence of IL-2 in a form capable of effectively interacting with the p70 subunit. Whether IL-2 is required for high-affinity receptor assembly or triggering of the internalization of preassembled receptors remains unresolved. Together, these findings support the existence of a stable, high-affinity human IL-2-R membrane complex composed of at least the p55 and p70 receptor subunits and IL-2. The Rockefeller University Press 1988-11-01 /pmc/articles/PMC2189118/ /pubmed/3263468 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex
title Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex
title_full Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex
title_fullStr Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex
title_full_unstemmed Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex
title_short Co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. Evidence for a stable ternary receptor complex
title_sort co-internalization of the p55 and p70 subunits of the high-affinity human interleukin 2 receptor. evidence for a stable ternary receptor complex
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189118/
https://www.ncbi.nlm.nih.gov/pubmed/3263468