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Hesse, Deike; Hommel, Angela; Jaschke, Alexander; Moser, Markus; Bernhardt, Ulrike; Zahn, Claudia; Kluge, Reinhart; Wittschen, Petra; Gruber, Achim D.; Al-Hasani, Hadi; Joost, Hans-Georg; Schürmann, Annette
Biochemical and biophysical research communications, 04/2010, Letnik: 394, Številka: 4Journal Article
The GTPase ADP-ribosylation factor related protein 1 (ARFRP1) controls the recruitment of proteins such as golgin-245 to the trans-Golgi. ARFRP1 is highly expressed in adipose tissues in which the insulin-sensitive glucose transporter GLUT4 is processed through the Golgi to a specialized endosomal compartment, the insulin-responsive storage compartment from which it is translocated to the plasma membrane in response to a stimulation of cells by insulin. In order to examine the role of ARFRP1 for GLUT4 targeting, subcellular distribution of GLUT4 was investigated in adipose tissue specific Arfrp1 knockout ( Arfrp1 ad −/−) mice. Immunohistochemical and ultrastructural studies of brown adipocytes demonstrated an abnormal trans-Golgi in Arfrp1 ad −/− adipocytes. In addition, in Arfrp1 ad −/− adipocytes GLUT4 protein accumulated at the plasma membrane rather than being sequestered in an intracellular compartment. A similar missorting of GLUT4 was produced by siRNA-mediated knockdown of Arfrp1 in 3T3-L1 adipocytes which was associated with significantly elevated uptake of deoxyglucose under basal conditions. Thus, Arfrp1 appears to be involved in sorting of GLUT4.
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