Sortilin Is the Major 110-kDa Protein in GLUT4 Vesicles from Adipocytes

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Sortilin is a major protein component of Glut4-containing vesicles.

In fat and skeletal muscle cells, glucose transporter isoform 4 (Glut4) is translocated to the cell surface in response to insulin via a system of specialized recycling vesicles. Besides Glut4, these vesicles include the novel insulin-regulatable aminopeptidase, receptors for insulin-like growth factor-II/Man-6-phosphate and transferrin, and a glycoprotein with the molecular mass of 110 kDa. We...

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Sortilin and retromer mediate retrograde transport of Glut4 in 3T3-L1 adipocytes

Sortilin is a multiligand sorting receptor responsible for the anterograde transport of lysosomal enzymes and substrates. Here we demonstrate that sortilin is also involved in retrograde protein traffic. In cultured 3T3-L1 adipocytes, sortilin together with retromer rescues Glut4 from degradation in lysosomes and retrieves it to the TGN, where insulin--responsive vesicles are formed. Mechanisti...

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The role of sortilin in the “Glut4 Pathway”.

ARTICLE HISTORY Received 9 October 2017 Revised 12 October 2017 Accepted 13 October 2017 ABSTRACT Sorting receptor, sortilin, is highly expressed in metabolically active tissues, such as brain, liver, skeletal muscle, and fat. Specifically in adipocytes, sortilin plays an important role in the “Glut4 pathway” by sorting the insulin-responsive glucose transporter, Glut4, in early endosomes and t...

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Characterization of insulin-responsive GLUT4 storage vesicles isolated from 3T3-L1 adipocytes.

Insulin regulates glucose transport in muscle and adipose tissue by triggering the translocation of a facilitative glucose transporter, GLUT4, from an intracellular compartment to the cell surface. It has previously been suggested that GLUT4 is segregated between endosomes, the trans-Golgi network (TGN), and a postendosomal storage compartment. The aim of the present study was to isolate the GL...

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The luminal Vps10p domain of sortilin plays the predominant role in targeting to insulin-responsive Glut4-containing vesicles.

In fat and skeletal muscle cells, insulin-responsive vesicles, or IRVs, deliver glucose transporter Glut4 and several associated proteins to the plasma membrane in response to hormonal stimulation. Although the protein composition of the IRVs is well studied, the mechanism of their formation is unknown. It is believed, however, that the cytoplasmic tails of the IRV component proteins carry targ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1998

ISSN: 0021-9258

DOI: 10.1074/jbc.273.6.3582