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Distinct Spatial Relationship of the Interleukin‐9 Receptor with Interleukin‐2 Receptor and Major Histocompatibility Complex Glycoproteins in Human T Lymphoma Cells
Author(s) -
Nizsalóczki Enikő,
Csomós István,
Nagy Péter,
Fazekas Zsolt,
Goldman Carolyn K.,
Waldmann Thomas A.,
Damjanovich Sándor,
Vámosi György,
Mátyus László,
Bodnár Andrea
Publication year - 2014
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201402501
Subject(s) - major histocompatibility complex , glycoprotein , receptor , lymphoma , interleukin 4 receptor , immunology , interleukin 2 , interleukin , interleukin 12 receptor, beta 1 subunit , biology , chemistry , microbiology and biotechnology , cytokine , immune system , genetics
The interleukin‐9 receptor (IL‐9R) consists of an α subunit and a γ c chain that are shared with other cytokine receptors, including interleukin‐2 receptor (IL‐2R), an important regulator of T cells. We previously showed that IL‐2R is expressed in common clusters with major histocompatibility complex (MHC) glycoproteins in lipid rafts of human T lymphoma cells, which raised the question about what the relationship between clusters of IL‐2R/MHC and IL‐9R is. Confocal microscopy colocalization and fluorescence resonance energy transfer experiments capable of detecting membrane protein organization at different size scales revealed nonrandom association of IL‐9R with IL‐2R/MHC clusters at the surface of human T lymphoma cells. Accommodation of IL‐9Rα in membrane areas segregated from the IL‐2R/MHC domains was also detected. The bipartite nature of IL‐9R distribution was mirrored by signal transducer and activator of transcription (STAT) activation results. Our data indicate that co‐compartmentalization with MHC glycoproteins is a general property of γ c receptors. Distribution of receptor chains between different membrane domains may regulate their function.