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

نویسندگان

  • B Z Lin
  • P F Pilch
  • K V Kandror
چکیده

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 report here by the criteria of the partial protein sequencing and subsequent cDNA cloning that glycoprotein 110, the last unidentified major protein component of Glut4-containing vesicles, is sortilin, a novel type I receptor-like protein recently cloned from human brain (Petersen, C. M., Nielsen, M. S., Nykjar, A., Jacobsen, L., Tommerup, N., Rasmussen, H. H., Roigaard, H., Gliemann, J., Madsen, P., and Moestrup, S. K. (1997) J. Biol. Chem. 272, 3599-3605). This protein is highly expressed in fat, brain, and lung and is dramatically up-regulated during differentiation of adipocytes in vitro.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

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...

متن کامل

Alternative routes to the cell surface underpin insulin-regulated membrane trafficking of GLUT4

Insulin-stimulated delivery of glucose transporters (GLUT4, also known as SLC2A4) from specialized intracellular GLUT4 storage vesicles (GSVs) to the surface of fat and muscle cells is central to whole-body glucose regulation. This translocation and subsequent internalization of GLUT4 back into intracellular stores transits through numerous small membrane-bound compartments (internal GLUT4-cont...

متن کامل

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...

متن کامل

Insulin responsiveness of glucose transporter 4 in 3T3-L1 cells depends on the presence of sortilin

Insulin-dependent translocation of glucose transporter 4 (Glut4) to the plasma membrane of fat and skeletal muscle cells plays the key role in postprandial clearance of blood glucose. Glut4 represents the major cell-specific component of the insulin-responsive vesicles (IRVs). It is not clear, however, whether the presence of Glut4 in the IRVs is essential for their ability to respond to insuli...

متن کامل

Functional role of sortilin in myogenesis and development of insulin-responsive glucose transport system in C2C12 myocytes.

Sortilin has been implicated in the formation of insulin-responsive GLUT4 storage vesicles in adipocytes by regulating sorting events between the trans-Golgi-network and endosomes. We herein show that sortilin serves as a potent myogenic differentiation stimulator for C2C12 myocytes by cooperatively functioning with p75NTR, which subsequently further contributes to development of the insulin-re...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 272 39  شماره 

صفحات  -

تاریخ انتشار 1997