1991 © 2014 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim wileyonlinelibrary.com
Localization and Dynamics of Glucocorticoid Receptor
at the Plasma Membrane of Activated Mast Cells
Emmanuel Oppong, Per Niklas Hedde, Sylwia Sekula-Neuner, Linxiao Yang,
Falko Brinkmann, René M. Dörlich, Michael Hirtz, Harald Fuchs,
Gerd Ulrich Nienhaus, and Andrew C. B. Cato*
these actions by binding to a glucocorticoid receptor (GR)
that is localized in the cytoplasm of target cells in complex
with molecular chaperones. Upon hormone binding, the
GR undergoes a conformation change, dissociates from the
In addition to their actions in the cell nucleus, glucocorticoids exhibit rapid non-
nuclear responses that are mechanistically not well understood. To explain these
effects, the localization of a glucocorticoid receptor (GR) expressed in mast cells as
a GFP fusion was analyzed after activation of the cells on allergenic lipid arrays.
These arrays were produced on glass slides by dip-pen nanolithography (DPN)
and total internal reflection (TIRF) microscopy was used to visualize the GR.
A rapid glucocorticoid-independent and -dependent recruitment of the GR-GFP
to the plasma cell membrane was observed following contact of the cells with the
allergenic array. In addition, the mobility of the GR at the membrane was monitored
by fluorescence recovery after photobleaching (FRAP) and shown to follow binding
kinetics demonstrating interactions of the receptor with membrane-bound factors.
Furthermore the recruitment of the GR to the cell membrane was shown to result
in a glucocorticoid-mediated increase in Erk phosphorylation. This is evidenced
by findings that destruction of the membrane composition of the mast cells by
cholesterol depletion impairs the membrane localization of the GR and subsequent
glucocorticoid-mediated enhancement of Erk phosphorylation. These results
demonstrate a membrane localization and function of the GR in mast cell signaling.
Nanolithography
1. Introduction
Glucocorticoids modulate a large variety of physiological
processes ranging from the control of intermediary metab-
olism to the mediation of stress response.
[1,2]
They exert
small 2014, 10, No. 10, 1991–1998
DOI: 10.1002/smll.201303677
Dr. E. Oppong,
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Prof. G. U. Nienhaus, Prof. A. C. B. Cato
Karlsruhe Institute of Technology
Institute of Toxicology and Genetics
76344, Eggenstein-Leopoldshafen, Germany
E-mail: Andrew.Cato@kit.edu
Dr. S. Sekula-Neuner, F. Brinkmann, Dr. M. Hirtz, Prof. H. Fuchs
Karlsruhe Institute of Technology
Institute of Nanotechnology (INT) & Karlsruhe Nano Micro Facility (KNMF)
Karlsruhe Institute of Technology (KIT)
76344, Eggenstein-Leopoldshafen, Germany
F. Brinkmann, Prof. H. Fuchs
Physical Institute and Center for Nanotechnology
(CeNTech) University of Münster
48149, Münster, Germany
Dr. P. N. Hedde,
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L. Yang, R. M. Dörlich,
Prof. G. U. Nienhaus
Karlsruhe Institute of Technology
Institute of Applied Physics and Centre
for Functional Nanostructures
76128, Karlsruhe, Germany
Prof. G. U. Nienhaus
Department of Physics
University of Illinois at Urbana-Champaign
Urbana, IL 61801, USA
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These authors contributed equally to this work.