| First Author | Hesse D | Year | 2010 |
| Journal | Biochem Biophys Res Commun | Volume | 394 |
| Issue | 4 | Pages | 896-903 |
| PubMed ID | 20230794 | Mgi Jnum | J:159231 |
| Mgi Id | MGI:4442109 | Doi | 10.1016/j.bbrc.2010.03.059 |
| Citation | Hesse D, et al. (2010) Altered GLUT4 trafficking in adipocytes in the absence of the GTPase Arfrp1. Biochem Biophys Res Commun 394(4):896-903 |
| abstractText | 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. |
