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A more recent version of this article appeared on December 1, 2006
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Submitted on May 4, 2006
Revised on September 6, 2006
Accepted on October 6, 2006
*Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11794; Section of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536; Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205
Monitoring Editor: Vivek Malhotra
The peripheral Golgi protein golgin-160 is induced during 3T3L1 adipogenesis and is primarily localized to the Golgi cisternae distinct from the TGN in a general distribution similar to p115. siRNA mediated reduction in golgin-160 protein resulted in an increase accumulation of the insulin-responsive amino peptidase (IRAP) and the insulin-regulated glucose transporter (GLUT4) at the plasma membrane concomitant with enhanced glucose uptake in the basal state. The redistribution of GLUT4 was rescued by expression of a siRNA resistant golgin-160 cDNA. The basal state accumulation of plasma membrane GLUT4 occurred due to an increased rate of exocytosis without any significant effect on the rate of endocytosis. This GLUT4 trafficking to the plasma membrane in the absence of golgin-160 was independent of TGN/Golgi sorting, as it was no longer inhibited by the expression of a dominant-interfering GGA mutant and displayed reduced binding to the lectin, Wheat Germ Agglutinin. Moreover, expression of the amino terminal head domain (amino acids 1-393) had no significant effect on the distribution or insulin-regulated trafficking of GLUT4 or IRAP. In contrast, expression of carboxyl 
helical region (393-1498) inhibited insulin-stimulated GLUT4 and IRAP translocation but had no effect on the sorting of constitutive membrane trafficking proteins, the transferrin receptor or vesicular stomatitis virus G (VSV-G) protein. Taken together these data demonstrate that golgin-160 plays an important role in directing insulin-regulated trafficking proteins toward the insulin-responsive compartment in adipocytes.
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