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J. Biol. Chem., Vol. 278, Issue 44, 42744-42749, October 31, 2003

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Membrane Organization of Luteinizing Hormone Receptors Differs between Actively Signaling and Desensitized Receptors^*

Mary Hunzicker-Dunn, George Barisas¶, Jinming Song||, and Deborah A. Roess||

From the Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611 and the Departments of ^||Physiology and ^¶Chemistry, Colorado State University, Fort Collins, Colorado 80523

Signaling by the luteinizing hormone/choriogonadotropin receptor (LHR) is of considerable interest because of its requirement for successful reproduction. Time-resolved phosphorescence anisotropy and fluorescence resonance energy transfer were used to investigate the organization of endogenous LHRs in porcine follicular membranes in two distinct signaling states, active and desensitized. Desensitized LHRs exhibited 3-fold slower rotational correlation times compared with active LHRs (59 ± 4 and 21 ± 9 µs, respectively), suggesting that with agonist-dependent desensitization the receptors are organized into larger protein complexes. Incubation of membranes with inhibitors of LHR desensitization, such as neutralizing anti-arrestin antibodies, a synthetic peptide corresponding to the third intracellular loop of the LHR but not the corresponding scrambled peptide, or catalytically inactive ARNO, resulted in faster rotational diffusion times equivalent to those of actively signaling LHRs. Furthermore, desensitized LHRs exhibited a 2.4-fold increase in fluorescence resonance energy transfer between LHRs suggesting that the larger protein aggregates formed during desensitization contain more self-associated LHRs. These results indicate that agonist-dependent LHR desensitization precedes organization of LHRs at the cells surface into larger protein aggregates.

Received for publication, June 11, 2003 , and in revised form, July 29, 2003.

^* This work was supported by the National Institutes of Health Grants R01 HD38060 (to M. H. D.) and HD23226 (to D. A. R.) and National Science Foundation Grant MCB-9807822 (to G. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 312-503-8940; Fax: 312-503-0566; E-mail: mhd{at}northwestern.edu.

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