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NotificationsNotify me of updates to RAB5 MEDIATED CAVEOLAE ENDOCYTOSIS pp. 211-221
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Authors:  Yuji Yamamoto, Tadahiro Taokoro, Makoto Hagiwara, Department of Agricultural Chemistry, Graduate School of Agriculture, Tokyo University of Agriculture, Sakuragaoka, Setagaya-ku, Tokyo, Japan
Caveolae are morphologically flask-shaped invaginations of the plasma membrane identified in various types of cells such as adipocytes, endothelial cells and myocytes. Unlike clathrin-coated pits, caveolae are detergent insoluble, cholesterol- and sphingolipid-rich, and show high caveolin expression (of caveolin-1, -2 and -3). A large number of molecules have been identified to localize to the caveolae including G-protein coupled receptors, membrane receptors and small GTPases. Recent research has made it clear that caveolae can participate in endocytosis and that they are morphologically distinct from clathrin-coated pits. Caveolin-1, the constitutive protein of the caveolae, is implicated in processes of vesicular transport during caveolae-mediated endocytosis. However, the precise molecular mechanisms of caveolae-mediated endocytosis remain unclear. Rab5 is a small GTPase involved in clathrin-coated vesicle formation, vesicle-early endosome fusion, and early endosome homotypic fusion as well as endosome maturation. Rab5 cycles between the GDP- (inactive) and GTP-bound (active) forms, a process that is tightly controlled by several Rab5 associating proteins. Here we discuss how and when Rab5 activity is controlled during the caveolae-mediated endocytosis and especially focus on the crucial role of the scaffolding domain (SD domain) of cavelolin-1. We also suggest the importance of Rab5 and caveolin-1 interaction during the intracellular trafficking of caveolae on the plasma membrane to the early endosome and to one of their final destination, the Golgi apparatus. 

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