A double leucine within the GLUT4 glucose transporter COOH-terminal domain functions as an endocytosis signal - PubMed (original) (raw)

Comparative Study

A double leucine within the GLUT4 glucose transporter COOH-terminal domain functions as an endocytosis signal

S Corvera et al. J Cell Biol. 1994 Aug.

Erratum in

• A double leucine within the GLUT4 glucose transporter COOH-terminal domain functions as an endocytosis signal.
  Corvera S, Chawla A, Chakrabarti R, Joly M, Buxton J, Czech MP. Corvera S, et al. J Cell Biol. 1994 Sep;126(6):1625. doi: 10.1083/jcb.126.6.1625. J Cell Biol. 1994. PMID: 8089191 Free PMC article. No abstract available.

Abstract

The unique COOH-terminal 30-amino acid region of the adipocyte/skeletal muscle glucose transporter (GLUT4) appears to be a major structural determinant of this protein's perinuclear localization, from where it is redistributed to the cell surface in response to insulin. To test whether an underlying mechanism of this domain's function involves glucose transporter endocytosis rates, transfected cells were generated expressing exofacial hemagglutinin epitope (HA)-tagged erythrocyte/brain glucose transporter (GLUT1) or a chimera containing the COOH-terminal 30 amino acids of GLUT4 substituted onto this GLUT1 construct. Incubation of COS-7 or CHO cells expressing the HA-tagged chimera with anti-HA antibody at 37 degrees resulted in an increased rate of antibody internalization compared to cells expressing similar levels of HA-tagged GLUT1, which displays a cell surface disposition. Colocalization of the internalized anti-HA antibody in vesicular structures with internalized transferrin and with total transporters was established by digital imaging microscopy, suggesting the total cellular pool of transporters are continuously recycling through the coated pit endocytosis pathway. Mutation of the unique double leucines 489 and 490 in the rat GLUT4 COOH-terminal domain to alanines caused the HA-tagged chimera to revert to the slow endocytosis rate and steady-state cell surface display characteristic of GLUT1. These results support the hypothesis that the double leucine motif in the GLUT4 COOH terminus operates as a rapid endocytosis and retention signal in the GLUT4 transporter, causing its localization to intracellular compartments in the absence of insulin.

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