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J. Biol. Chem., Vol. 277, Issue 18, 15795-15800, May 3, 2002
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From the Luteinizing hormone receptor is a G
protein-coupled receptor and consists of two halves: the N-terminal
extracellular half (exodomain) and C-terminal membrane-associated half
(endodomain). Hormone binds to the exodomain, and the
resulting hormone-exodomain complex modulates the endodomain to
generate signals. There are mutations that impair either hormone
binding or signal generation. We report that the coexpression of a
binding defective mutant and a signal-defective mutant rescues signal
generation to produce cAMP. This rescue requires both types of mutant
receptors and is dependent on the human chorionic gonadotropin
dose, the surface concentration of mutant receptors, and the amino acid
position of mutations. Furthermore, random collisions among mutant
receptors are not involved in the rescue. Our observations provide new
insights into the mechanisms of the functional and structural
relationship of the exo- and endodomain, signal transduction, and
receptor genetics, in particular for defective heterozygotes.
Two Defective Heterozygous Luteinizing Hormone Receptors Can
Rescue Hormone Action*
,,,,¶
Department of Chemistry, University of
Kentucky, Lexington, Kentucky 40506-0055 and the § Oregon
Regional Primate Research Center and Department of Physiology and
Pharmacology, Oregon Health Sciences University, Portland, Oregon
97201
*
This work was supported by Grants HD-18702 and DK-51469 from
the National Institutes of Health.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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