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A role for calnexin (IP90) in the assembly of class II MHC molecules.

1994; Springer Nature; Volume: 13; Issue: 3 Linguagem: Inglês

10.1002/j.1460-2075.1994.tb06306.x

1460-2075

Karen S. Anderson, Peter Cresswell,

Galectins and Cancer Biology

Research Article1 February 1994free access A role for calnexin (IP90) in the assembly of class II MHC molecules. K.S. Anderson K.S. Anderson Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author P. Cresswell P. Cresswell Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author K.S. Anderson K.S. Anderson Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author P. Cresswell P. Cresswell Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510. Search for more papers by this author Author Information K.S. Anderson1 and P. Cresswell1 1Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510. The EMBO Journal (1994)13:675-682https://doi.org/10.1002/j.1460-2075.1994.tb06306.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Major histocompatibility complex (MHC) class II antigens consist of alpha and beta chains that associate intracellularly with the invariant (I) chain. The HLA-DR alpha beta I complex assembles in the endoplasmic reticulum (ER) into a nonameric structure via progressive addition of three alpha beta dimers to a core invariant chain trimer. We have examined intracellular association of alpha beta I complexes with the resident ER protein calnexin. Calnexin associates rapidly (within 3 min) with newly synthesized alpha, beta and I chains, and remains associated with the assembling alpha beta I complex until the final alpha beta dimer is added, forming the complete nonamer. Dissociation of calnexin parallels egress of alpha beta I from the ER. These results suggest that calnexin retains and stabilizes both free class II subunits and partially assembled class II-I chain complexes until assembly of the nonamer is complete. Previous ArticleNext Article Volume 13Issue 31 February 1994In this issue RelatedDetailsLoading ...