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  • Title: Influence of N-glycan chain length on chaperone association and intracellular transport of major histocompatibility complex class I proteins.
    Author: Bennett MJ, Kearse KP.
    Journal: Biochem Biophys Res Commun; 1999 Aug 27; 262(2):473-8. PubMed ID: 10462499.
    Abstract:
    Recent studies demonstrate that processing of N-linked glycans plays an important role in the quality control of major histocompatibility complex (MHC) class I transport from the endoplasmic reticulum (ER) to the Golgi complex and beyond. Here, we investigated the importance of oligosaccharide chain length on the association of MHC class I proteins with molecular chaperones and their intracellular transport from the ER to the Golgi. These data show that calnexin interaction with class I proteins having truncated N-glycans was reduced compared to normal class I molecules, whereas the assembly of class I with calreticulin and TAP was unperturbed by N-glycan chain length. Additionally, these results demonstrate that class I proteins containing truncated N-glycans showed decreased detachment from calreticulin and TAP relative to class I proteins bearing typical oligosaccharides. Taken together, these studies show that N-glycan chain length is an important determinant for the quality control of newly synthesized MHC class I proteins in the ER.
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