Format

Send to

Choose Destination
Biochim Biophys Acta. 2015 Apr;1853(4):802-9. doi: 10.1016/j.bbamcr.2014.12.017. Epub 2014 Dec 20.

Nanoclusters of the resting T cell antigen receptor (TCR) localize to non-raft domains.

Author information

1
Department of Molecular Immunology, Faculty of Biology, BIOSS Center for Biological Signalling Studies, Freiburg, Germany; Spemann Graduate School of Biology and Medicine (SGBM), Freiburg, Germany; Centre for Chronic Immunodeficiency CCI, Albert-Ludwigs-University Freiburg, Germany; Max Planck-Institute of Immunobiology and Epigenetics, Freiburg, Germany.
2
Department of Molecular Immunology, Faculty of Biology, BIOSS Center for Biological Signalling Studies, Freiburg, Germany; Centre for Chronic Immunodeficiency CCI, Albert-Ludwigs-University Freiburg, Germany; Max Planck-Institute of Immunobiology and Epigenetics, Freiburg, Germany; International Max Planck Research School for Molecular and Cellular Biology (IMPRS-MCB), Freiburg, Germany.
3
Department of Molecular Immunology, Faculty of Biology, BIOSS Center for Biological Signalling Studies, Freiburg, Germany; Max Planck-Institute of Immunobiology and Epigenetics, Freiburg, Germany.
4
Department of Molecular Immunology, Faculty of Biology, BIOSS Center for Biological Signalling Studies, Freiburg, Germany; Centre for Chronic Immunodeficiency CCI, Albert-Ludwigs-University Freiburg, Germany.
5
Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
6
Department of Integrative Biology and Pharmacology, University of Texas Health Science Center at Houston, USA.
7
Centro de Biología Molecular Severo Ochoa, CSIC-Universidad Autónoma de Madrid, Madrid, Spain.
8
Department of Molecular Immunology, Faculty of Biology, BIOSS Center for Biological Signalling Studies, Freiburg, Germany; Spemann Graduate School of Biology and Medicine (SGBM), Freiburg, Germany; Centre for Chronic Immunodeficiency CCI, Albert-Ludwigs-University Freiburg, Germany; Max Planck-Institute of Immunobiology and Epigenetics, Freiburg, Germany. Electronic address: wolfgang.schamel@biologie.uni-freiburg.de.

Abstract

In the last decade an increasing number of plasma membrane (PM) proteins have been shown to be non-randomly distributed but instead forming submicron-sized oligomers called nanoclusters. Nanoclusters exist independently of the ligand-bound state of the receptors and their existence implies a high degree of lateral organisation of the PM and its proteins. The mechanisms that drive receptor nanoclustering are largely unknown. One well-defined example of a transmembrane receptor that forms nanoclusters is the T cell antigen receptor (TCR), a multisubunit protein complex whose nanoclustering influences its activity. Membrane lipids, namely cholesterol and sphingomyelin, have been shown to contribute to TCR nanoclustering. However, the identity of the membrane microdomain in which the TCR resides remains controversial. Using a GFP-labeled TCR we show here that the resting TCR localized in the disordered domain of giant PM vesicles (GPMVs) and PM spheres (PMSs) and that single and nanoclustered TCRs are found in the high-density fractions in sucrose gradients. Both findings are indicative of non-raft localization. We discuss possible mechanisms of TCR nanoclustering in T cells. This article is part of a Special Issue entitled: Nanoscale membrane organisation and signalling.

KEYWORDS:

Cholesterol; Lipid; Membrane; Nanoclustering; TCR

PMID:
25535948
DOI:
10.1016/j.bbamcr.2014.12.017
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center