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Am J Physiol Endocrinol Metab (May 31, 2005). doi:10.1152/ajpendo.00175.2005
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Submitted on April 22, 2005
Accepted on May 25, 2005

Initial Entry of IRAP into the Insulin-Responsive Storage Compartment Occurs Prior to Basal or Insulin-Stimulated Plasma Membrane Recycling

Gang Liu1, June Chunqiu Hou1, Robert T Watson2, and Jeffrey E Pessin2*

1 Department of Pediatric and Adolescent Medicine, Mayo Clinic College of Medicine, Rochester, MN, USA; Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY, USA
2 Department of Pharmacological Sciences, Stony Brook University, Stony Brook, NY, USA

* To whom correspondence should be addressed. E-mail: pessin{at}pharm.sunysb.edu.

To examine the acquisition of insulin sensitivity following the initial biosynthesis of the insulin-responsive aminopeptidase (IRAP), 3T3L1 adipocytes were transfected with an Enhanced Green Fluorescent Protein-IRAP (EGFP-IRAP) fusion protein. In the absence of insulin, IRAP was rapidly localized (1-3 h) to secretory membranes and retained in these intracellular membrane compartments with little accumulation at the plasma membrane. However, insulin was unable to induce translocation to the plasma membrane until 6-9 h following biosynthesis. This was in marked contrast to another type II membrane protein (Syntaxin 3) that rapidly defaulted to the plasma membrane 3 h following expression. In parallel with the time-dependent acquisition of insulin responsiveness, the newly synthesized IRAP protein converted from a Brefeldin A sensitive to a Brefeldin A insensitive state. The initial trafficking of IRAP to the insulin-responsive compartment was independent of plasma membrane endocytosis as expression of a dominant-interfering dynamin mutant (Dyn/K44A) inhibited transferrin receptor endocytosis but had no effect on the insulin-stimulated translocation of the newly synthesized IRAP protein.




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