Volume 15, Issue 18 p. 3969-3978
Article

Distinct Spatial Relationship of the Interleukin-9 Receptor with Interleukin-2 Receptor and Major Histocompatibility Complex Glycoproteins in Human T Lymphoma Cells

Enikő Nizsalóczki

Enikő Nizsalóczki

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

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István Csomós

István Csomós

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

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Dr. Péter Nagy

Dr. Péter Nagy

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

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Dr. Zsolt Fazekas

Dr. Zsolt Fazekas

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

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Dr. Carolyn K. Goldman

Dr. Carolyn K. Goldman

Metabolism Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 (USA)

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Dr. Thomas A. Waldmann

Dr. Thomas A. Waldmann

Metabolism Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892 (USA)

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Dr. Sándor Damjanovich

Dr. Sándor Damjanovich

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

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Dr. György Vámosi

Dr. György Vámosi

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

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Dr. László Mátyus

Corresponding Author

Dr. László Mátyus

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)Search for more papers by this author
Dr. Andrea Bodnár

Dr. Andrea Bodnár

Department of Biophysics and Cell Biology, Research Center for Molecular Medicine, University of Debrecen, P.O.B. 39., 4012, Debrecen (Hungary)

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First published: 08 October 2014
Citations: 10

Graphical Abstract

To be or not to be together: Confocal microscopy coexpression and fluorescence resonance energy transfer data show nonrandom colocalization of the interleukin-9 receptor (IL-9R) with IL-2R and major histocompatibility complex (MHC) molecules in human T cells. IL-9Rα can also be detected in membrane areas spatially segregated from the aforesaid molecules. The bipartite nature of IL-9R localization is mirrored in its signaling capacity.

Abstract

The interleukin-9 receptor (IL-9R) consists of an α subunit and a γc 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 γc receptors. Distribution of receptor chains between different membrane domains may regulate their function.