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Received for publication April 23, 2004.
Revised July 26, 2004.
Accepted for publication August 3, 2004.
1b-adrenoceptor
Combinations of co-immunoprecipitation, single cell fluorescence resonance energy transfer and cell surface time-resolved fluorescence resonance energy transfer demonstrated protein-protein interactions and quaternary structure for the 
1b-adrenoceptor. Self-association of transmembrane domain 1 and its interaction with the full length receptor indicated a symmetrical interface provided by this domain. Lack of effect of mutation of the glycophorin-A dimerization-like region within this helix demonstrated that this did not provide the molecular mechanism. Multiple interactions were observed between the 1b-adrenoceptor and fragments derived from its sequence. Fragments comprising transmembrane domains 3 and 4 and transmembrane domains 5 and 6, but not transmembrane domain 7, were also able to interact with the full length receptor. Transmembrane domain 7 failed to interact significantly with any element of the receptor and was not transported to the cell surface following co-expression with the full length receptor. Symmetrical interactions were also noted between fragments incorporating transmembrane domain 4 but this segment of the receptor failed to interact with transmembrane domains 1 and 2 or transmembrane domains 5 and 6. Time-resolved fluorescence resonance energy transfer studies were also consistent with contributions of transmembrane domains 1 and/or 2 and transmembrane domains 3 and/or 4 to protein-protein interactions within the quaternary structure of the 1b-adrenoceptor, and with a contribution of transmembrane domains 5 and/or 6. These data are consistent with a complex oligomeric quaternary structure of the 1b-adrenoceptor in which major, symmetrical interactions may define intra-dimeric contacts with other contributions providing inter-dimer contacts to generate oligomeric complexes akin to those observed for murine rhodopsin. A model based on this was developed.
Key words:
Adrenergic, Gq/11 family, Receptor synthesis/trafficking, Fluorescence techniques
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