“…11) were identified more than 30 years ago using electron microscopy (383), and their function first indirectly suggested by two electrode recordings that documented synchronous waves of electrical activity induced by glucose in different cells of the same islet (25,125,247,333,336,350). Further studies showed that in vivo these gap junctions typically comprise small numbers of connexons (341,345) made only of Cx36 in vivo (65,421,478,479,538) within the islets of adult, control animals of all species investigated so far, whereas under certain in vitro conditions they may also contain Cx43 (91,296,309). Cx36 is a 321-amino acid protein with a long (99 amino acid) cytoplasmic loop containing an unusual stretch of 10 glycine residues (94) and a short cytoplasmic COOH-terminal region containing potential recognition sites for casein kinases I and II, cAMP-dependent protein kinase, and calmodulin-dependent protein kinase II (60), consistent with the finding that, at least under certain conditions, the function of Cx36 may be regulated by phosphorylation (3,274,550).…”