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- W2005527680 abstract "Translocation of Glut4 to the plasma membrane of fat and skeletal muscle cells is mediated by specialized insulin‐responsive vesicles (IRVs), whose protein composition consists primarily of glucose transporter isoform 4 (Glut4), insulin‐responsive amino peptidase (IRAP), sortilin, lipoprotein receptor‐related protein 1 (LRP1) and v‐SNAREs. How can these proteins find each other in the cell and form functional vesicles after endocytosis from the plasma membrane? We are proposing a model according to which the IRV component proteins are internalized into sorting endosomes and are delivered to the IRV donor compartment(s), recycling endosomes and/or the trans ‐Golgi network (TGN), by cellugyrin‐positive transport vesicles. The cytoplasmic tails of Glut4, IRAP, LRP1 and sortilin play an important targeting role in this process. Once these proteins arrive in the donor compartment, they interact with each other via their lumenal domains. This facilitates clustering of the IRV proteins into an oligomeric complex, which can then be distributed from the donor membranes to the IRV as a single entity with the help of adaptors, such as Golgi‐localized, gamma‐adaptin ear‐containing, ARF‐binding (GGA)." @default.
- W2005527680 created "2016-06-24" @default.
- W2005527680 creator A5058516278 @default.
- W2005527680 creator A5059860261 @default.
- W2005527680 date "2011-03-15" @default.
- W2005527680 modified "2023-10-16" @default.
- W2005527680 title "The Sugar Is sIRVed: Sorting Glut4 and Its Fellow Travelers" @default.
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- W2005527680 doi "https://doi.org/10.1111/j.1600-0854.2011.01175.x" @default.
- W2005527680 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21306486" @default.
- W2005527680 hasPublicationYear "2011" @default.
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