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Background  In the present study, we describe heterodimerization between human-Somatostatin Receptor 5 (hSSTR5) and β 2 -Adrenergic Receptor (β 2 AR) and its impact on the receptor trafficking, coupling to adenylyl cyclase and signaling including mitogen activated protein kinases and calcineurin-NFAT pathways.    Methods  We used co-immunoprecipitation, photobleaching- fluorescence resonance energy transfer and Fluorescence assisted cell sorting analysis to characterize heterodimerization between SSTR5 and β 2 AR.    Results  Our results indicate that hSSTR5/β 2 AR exist as preformed heterodimers in the basal condition which is enhanced upon co-activation of both receptors. In contrast, the activation of individual receptors leads to the dissociation of heterodimers. Receptor coupling to adenylyl cyclase displayed predominant effect of β 2 AR, however, somatostatin mediated inhibition of cAMP was enhanced upon blocking β 2 AR. Our results indicate hSSTR5 mediated significant activation of ERK1/2 and inhibition of phospho-p38. The phospho-NFAT level was enhanced in cotransfected cells indicating the blockade of calcineurin mediated dephosphorylation of NFAT upon receptor heterodimerization.    Conclusion  These data for the first time unveil a novel insight for the role of hSSTR5/β 2 AR in the modulation of signaling pathways which has not been addressed earlier.

Heterodimerization of β<sub>2</sub> adrenergic receptor and somatostatin receptor 5: Implications in modulation of signaling pathway