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Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes.

Authors: Morris, NJ  Ross, SA  Lane, WS  Moestrup, SK  Petersen, CM  Keller, SR  Lienhard, GE 
Citation: Morris NJ, etal., J Biol Chem 1998 Feb 6;273(6):3582-7.
Pubmed: (View Article at PubMed) PMID:9452485

Vesicles containing the glucose transporter GLUT4 from rat adipocytes contain a major protein of 110 kDa. We have isolated this protein, obtained the sequences of peptides, and cloned a large portion of its cDNA. This revealed that the protein is sortilin, a novel membrane protein that was cloned in another context from a human source while this work was in progress. Subcellular fractionation of rat and 3T3-L1 adipocytes, together with GLUT4 vesicle isolation, showed that sortilin was primarily located in the low density microsomes in vesicles containing GLUT4. Insulin caused a 1.7-fold increase in the amount of sortilin at the plasma membranes of 3T3-L1 adipocytes, as assessed by cell surface biotinylation. The expression of sortilin in 3T3-L1 cells occurred only upon differentiation. Previous characterization of sortilin has led to the suggestion that it functions to sort lumenal proteins from the trans Golgi. The significance of its insulin-stimulated increase at the cell surface and of its expression upon differentiation will require definitive delineation of its function.


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CRRD Object Information
CRRD ID: 730041
Created: 2003-12-01
Species: All species
Last Modified: 2006-04-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.