The output and time-course of insulin release from pancreatic beta-cells are elegantly controlled. The secretory process comprises pre-exocytotic stages, exocytosis and post-exocytotic stages. The small GTPase Rab27a is known to regulate pre-exocytotic stages that determine the size of the readily-releasable pool of insulin granules. GTP-Rab27a and its specific effectors are responsible for this process like other GTPases. Recently, we searched for Rab27a-interacting proteins and identified coronin 3. Unexpectedly, coronin 3 only bound GDP-Rab27a and this interaction regulated post-exocytotic stages via reorganization of the actin cytoskeleton. Since glucose converts Rab27a from the GTP- to GDP-bound form, we suggested that Rab27a plays a crucial role in stimulus-endocytosis coupling in pancreatic beta-cells, and that this is the key molecule for membrane recycling of insulin granules. In this review, we provide an overview of the roles of Rab27a and its GTP- and GDP-dependent effectors in the insulin secretory pathway of pancreatic beta-cells.