Many of the receptors and downstream signalling elements involved in taste transduction are also expressed in enteroendocrine cells where they underlie the chemosensory functions of the gut. We showed, for the first time, that taste receptor 1, T1R, family members, T1R1, T1R2 and T1R3 are expressed in the intestinal epithelium, and proposed that the sweet taste receptor, T1R2+T1R3, functions as the luminal sugar sensor. Recent work in our laboratory has determined that T1R2+ T1R3, and the partner G-protein, gustducin, are co-expressed in glucagon like peptide 1 (GLP-1), glucose-dependent insulinotropic peptide (GIP) and serotonin containing endocrine cells. We have been interested in the role played by the intestinal sweet taste receptor in regulation of the intestinal glucose transporter, Na+/glucose cotransporter 1, SGLT1. SGLT1 is the major route for the transport of dietary sugars from the lumen of the intestine into enterocytes. Regulation of this protein is essential for the provision of glucose to the body and, thus, is important for maintenance of glucose homeostasis. We demonstrated that dietary sugars and artificial sweeteners increase SGLT1 mRNA and protein expression and glucose-absorptive capacity in wild type mice, but not in T1R3, or gustducin, knockout mice, indicating that T1R3 and gustducin are required for enhanced expression of SGLT1 in response to lumenal sugars and sweeteners. The findings that gustducin and T1Rs reside in enteroendocrine cells, whereas SGLT1 is expressed in neighbouring absorptive enterocytes implies a signalling event taking place between the chemosensory enteroendocrine cells and absorptive enterocytes. I shall discuss progress made in understanding the mechanisms underlying this cell to cell communication.