Somatostatin (SRIF) exerts its multiple actions, including inhibition of growth hormone (GH) secretion and of tumoral growth, through a family of five receptor subtypes (sst1-sst5). We recently reported that an sst2-selective agonist markedly decreases GH release from pig somatotropes, suggesting important roles for this scarcely explored receptor, psst2. Here, functional expression of psst2 in CHO-K1 and HEK-293-AD cell lines was employed to determine its pharmacological features and functional ability to reduce cAMP, and to examine its homodimerization and internalization dynamics in real time in single living cells. Results show that psst2 is a high affinity receptor (Kd = 0.27 nM) displaying a typical sst2 profile (nM affinity for SRIF-14SRIF-28>cortistatin>MK678>octreotide) and high selectivity (EC₅₀=1.1 nM) for the sst2 agonist L-779,976, but mM or undetectable affinity to other sst-specific agonists (sst3>sst1>sst5>>>sst4). Accordingly, SRIF dose-dependently inhibited forskolin-stimulated cAMP with high potency (EC₅₀=6.55 pM) and modest efficacy (maximum 29.1%) via psst2. Cotransfection of HEK-293 and CHO-K1 cells with two receptor constructs modified with distinct fluorescent tags (psst2-YFP/psst2-CFP) enabled FRET measurement of physical interaction between psst2 receptors and also receptor internalization in single living cells. This revealed that under basal conditions, psst2 forms constitutive homodimers/homomultimers, which dissociate immediately (11 sec) upon SRIF binding. Interestingly, contrary to human sst2, psst2 rapidly reassociates (110.5 sec) during a subsequent process that temporally overlaps with receptor internalization (half-maximal=95.1 sec). Therefore, psst2 is a potent inhibitory receptor displaying a unique set of interrelated dynamic features of agonist-dependent dimerization, dissociation, internalization and reassociation, a cascade of events that might be critical for receptor function.