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J. Biol. Chem., Vol. 266, Issue 17, 10807-10812, 06, 1991
WR Moyle, MP Bernard, RV Myers, OM Marko and CD Strader
In some G-protein-coupled receptors (e.g. beta-adrenergic receptor (beta 2
AR)), the ligand-binding pocket is contained within the hydrophobic
transmembrane domain. In others (e.g. luteinizing hormone receptor (LHR)),
the relative roles of the extracellular N-terminal domain and the
transmembrane region in hormone binding are unknown. To study the roles of
these domains, we prepared vectors encoding the rat LHR N-terminal domain
alone (L- -), the LHR N-terminal domain fused to the transmembrane and
C-terminal domains of the vesicular stomatitis virus-G protein (LVV), the
LHR N-terminal domain fused to the transmembrane and C-terminal domains of
the hamster beta 2 AR (LAA), and the beta 2 AR N-terminal domain fused to
the transmembrane and C- terminal domains of the rat LHR (ALL). Membrane
preparations obtained from COS-7 cells expressing the beta 2 AR or LAA
bound the beta- adrenergic antagonist 125I-cyanopindolol with equal
affinity, confirming the observation that the beta 2 AR transmembrane
domain forms the hormone-binding site. Membranes from COS-7 cells
transfected with LHR bound 125I-human choriomic gonadotropin (hCG).
However, membranes from LAA-, L(- -)-, and LVV-transfected cells had low
capacity to bind 125I-hCG unless they were solubilized with Triton X- 100.
The affinity of the detergent-solubilized receptors for 125I-hCG was
similar to that of the LHR. We were unable to detect binding of 125I-hCG to
ALL in the presence or absence of detergent. These observations suggest
that, whereas the transmembrane region of the beta 2 AR is sufficient to
bind adrenergic ligands, the N-terminal region of the LHR is required for
binding of hCG. Although the N terminus of the LHR is sufficient to bind
hCG, both the N terminus and the transmembrane domains of the LHR are
required for receptor expression on the cell surface.
Leutropin/beta-adrenergic receptor chimeras bind choriogonadotropin and adrenergic ligands but are not expressed at the cell surface
Department of Obstetrics and Gynecology, Robert Wood Johnson (Rutgers) Medical School, Piscataway, New Jersey 08854.
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