Publikationsdatenbank

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

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

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

Quelle

Biochemical and biophysical research communications

Bandzählung: 394

Heftzählung: 4

Seiten: 896 – 903

ISSN: 0006-291x

Sprache

Englisch

Verweise

DOI: 10.1016/j.bbrc.2010.03.059

Pubmed: 20230794

Kontakt

Institut für Tierpathologie

Robert-von-Ostertag-Str. 15
14163 Berlin
+49 30 838 62450
pathologie@vetmed.fu-berlin.de

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.