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J. Biol. Chem., Vol. 275, Issue 43, 33197-33200, October 27, 2000
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From the This study provides evidence that the differences
in membrane composition found from one cell type to another can
represent a limiting factor to recovering the functionality of
transmembrane proteins when expressed in heterologous systems.
Restoring the properties of the human µ-opioid receptor in yeast
(Saccharomyces cerevisiae), similar to those observed in
native cells, was achieved by replacing ergosterol from yeast by
cholesterol, which is normally found in mammalian plasma membranes. The
results suggest that these two sterols have opposite effects with
respect to the ligand binding function of the receptor. Ergosterol was
found to constrain the µ-opioid receptor in an inactive state in
yeast plasma membranes and cannot replace cholesterol in activating it.
These data differ from previous works dealing with the function of
related G-protein-coupled receptors (GPCR) in ergosterol-enriched
membranes. This suggests that structural requirements of GPCR with
respect to their modulation by lipid components differ from one protein
to another. As a consequence, we assume that the presence of
appropriate lipids around transmembrane proteins determines their
function. This highlights the functional significance of lateral
heterogeneities of membrane components within biological membranes.
Institut de Pharmacologie et de Biologie
Structurale, CNRS INSA UMR 5089, 205 Route de Narbonne, 31077 Toulouse
cedex, France
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