Fachbereich Veterinärmedizin



    Altered GLUT4 Trafficking in Adipocytes in the Absence of the GTPase Arfrp1 (2010)

    Zeitschriftenartikel / wissenschaftlicher Beitrag
    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; 394(4) — S. 896–903
    ISSN: 0006-291x
    DOI: 10.1016/j.bbrc.2010.03.059
    Pubmed: 20230794
    Institut für Tierpathologie

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    Abstract / Zusammenfassung

    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.