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A dual role of the N-terminal FQQI motif in GLUT4 trafficking by Ulrike Bernhardt; Françoise Carlotti; Rob C. Hoeben; Hans-Georg Joost; Hadi Al-Hasani is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is A dual role of the N-terminal FQQI motif in GLUT4 trafficking about?

## Abstract In adipocytes, the glucose transporter GLUT4 recycles between intracellular storage vesicles and the plasma membrane. GLUT4 is internalized by a clathrin- and dynamin-dependent mechanism, and sorted into an insulin-sensitive storage compartment. Insulin stimulation leads to GLUT4 accumulation on the cell surface. The N-terminal F5QQI motif in GLUT4 has been shown previously to be required for sorting of the protein in the basal state. Here, we show that the FQQI motif is a binding site for the medium chain adaptin μ1, a subunit of the AP-1 adaptor complex that plays a role in post-Golgi/endosomal trafficking events. In order to investigate the role of AP-1 and AP-2 in GLUT4 trafficking, we generated 3T3-L1 adipocytes expressing HA-GLUT4-GFP and knocked down the AP-1 and AP-2 complex by RNAi, respectively. In AP-1 and AP-2 knockdown adipocytes, GLUT4 accumulates at the cell surface in the basal state, consistent with a role of AP-1 in post-endosomal sorting of GLUT4 to the insulin-sensitive storage compartment, and of AP-2 in clathrin-mediated endocytosis. Our data demonstrate a dual role of the F5QQI motif and support the conclusion that the AP complexes direct GLUT4 tr

Who reads A dual role of the N-terminal FQQI motif in GLUT4 trafficking?

It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Ulrike Bernhardt; Françoise Carlotti; Rob C. Hoeben; Hans-Georg Joost; Hadi Al-Hasani
Publisher
Walter de Gruyter GmbH
Published
2009
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)