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lüll Rab27a, actin and beta-cell endocytosis Kimura T; Niki IEndocr J 2011[]; 58 (1): 1-6The 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.|*Endocytosis[MESH]|Actins/*metabolism[MESH]|Animals[MESH]|Exocytosis/drug effects[MESH]|Guanosine Diphosphate/metabolism[MESH]|Guanosine Triphosphate/metabolism[MESH]|Humans[MESH]|Insulin Secretion[MESH]|Insulin-Secreting Cells/metabolism/*physiology[MESH]|Insulin/*metabolism[MESH]|Microfilament Proteins[MESH]|rab GTP-Binding Proteins/*physiology[MESH]|rab27 GTP-Binding Proteins[MESH] |