The glut 1 glucose transporter interacts with calnexin and calreticulin.

Calnexin is an integral membrane protein that acts as a chaperone during glycoprotein folding in the endoplasmic reticulum. Cross-linking studies were carried out with the aim of investigating the interactions of calnexin with glycoproteins in vitro. A truncated version of the integral membrane glycoprotein Glut 1 (GT155) was synthesized in ...
a rabbit reticulocyte translation system in the presence of canine pancreatic microsomes. Following immunoprecipitation with an anticalnexin antiserum, a cross-linker-independent association was observed between GT155 and calnexin. In addition, the anti-calnexin antiserum immunoprecipitated a UV-dependent cross-linking product consisting of GT155 and a protein of approximately 60 kDa designated CAP-60 (calnexin-associated protein of 60 kDa). Both the GT155-calnexin and the GT155-CAP-60 interactions were dependent on the presence of a correctly modified oligosaccharide group on GT155, a characteristic of many calnexin interactions. A GT155 mutant that was not glycosylated (AGGT155) did not associate with calnexin or CAP-60. Calreticulin, the soluble homologue of calnexin, was also shown to interact with GT155 only when the protein bore a correctly modified oligosaccharide group. Thus, our data show that both calnexin and calreticulin with Glut 1 in a glycosylation-dependent manner.
Mesh Terms:
Animals, Calcium-Binding Proteins, Calnexin, Calreticulin, Cross-Linking Reagents, Dogs, Glucose Transporter Type 1, Glycosylation, Humans, Microsomes, Molecular Chaperones, Monosaccharide Transport Proteins, Mutation, Peptide Fragments, Protein Binding, Rabbits, Recombinant Proteins, Reticulocytes, Ribonucleoproteins, Ultraviolet Rays
J. Biol. Chem.
Date: Jun. 07, 1996
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