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PNAS | March 5, 2002 | vol. 99 | no. 5 | 3294-3299
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Pharmacology
 Ligand binding to somatostatin receptors induces receptor-specific oligomer formation in live cells

Ramesh C. Patel*,dagger ,Dagger , Ujendra Kumar*,Dagger , Don C. Lamb§, John S. Eid§, Magalie Rocheville*, Michael Grant*, Aruna Rani*, Theodore Hazlett§, Shutish C. Patel, Enrico Gratton§, and Yogesh C. Patel*,||

* Fraser Laboratories, Departments of Medicine, Pharmacology, and Therapeutics and Neurology and Neurosurgery, McGill University, and Royal Victoria Hospital, Montreal, QC, Canada H3A 1A1; dagger  Department of Chemistry and Physics, Clarkson University, Potsdam, NY 13699, and Neural Connections, Potsdam, NY 13676; § Fluorescence Dynamics Laboratory, University of Illinois, Champaign-Urbana, IL 61801-3080; and  New England Biomedical Research Center, Newington, CT 06111

Communicated by Susan E. Leeman, Boston University School of Medicine, Boston, MA, December 27, 2001 (received for review October 2, 2001)

Heptahelical receptors (HHRs) are generally thought to function as monomeric entities. Several HHRs such as somatostatin receptors (SSTRs), however, form homo- and heterooligomers when activated by ligand binding. By using dual fluorescent ligands simultaneously applied to live cells monotransfected with SSTR5 (R5) or SSTR1 (R1), or cotransfected with R5 and R1, we have analyzed the ligand receptor stoichiometry and aggregation states for the three receptor systems by fluorescence resonance energy transfer and fluorescence correlation spectroscopy. Both homo- and heterooligomeric receptors are occupied by two ligand molecules. We find that monomeric, homooligomeric, and heterooligomeric receptor species occur in the same cell cotransfected with two SSTRs, and that oligomerization of SSTRs is regulated by ligand binding by a selective process that is restricted to some (R5) but not other (R1) SSTR subtypes. We propose that induction by ligand of different oligomeric states of SSTRs represents a unique mechanism for generating signaling specificity not only within the SSTR family but more generally in the HHR family.

Dagger R.C.P. and U.K. contributed equally to this work.

|| To whom reprint requests should be addressed. E-mail: yogesh.patel{at}mcgill.ca.

www.pnas.org/cgi/doi/10.1073/pnas.042705099
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