Abstract
This review discusses the ER protein calnexin that is related in structure and function to calreticulin. In vivo and in vitro experiments from many laboratories have provided evidence that calnexin and calreticulin interact transiently with glycoproteins while they are folding in the ER a that this interaction is via a specific Glc1Man9GlcNAc2 glycoform. The structure of calnexin has recently been determined to 2.9Å resolution by X-ray crystallography and has a unique and remarkable structure a globular domain and an extended 140Å arm termed the P domain. The P domain recruits a member of the protein disulfide isomerase family, ERp57, that specifically catalyzes disulfide bond exchange on glycoproteins bound to calnexin. Calnexin links N-glycosylation and protein folding and forms the quality control system for glycoproteins. Mutant glycoproteins are the basis of many human protein trafficking diseases and the ER quality system is responsible for their retention in the ER and their proteolytic degradation in the cytosol.
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Bergeron, J.J.M., Thomas, D.Y. (2003). Calnexin, an ER Integral Membrane Chaperone in Health and Disease. In: Eggleton, P., Michalak, M. (eds) Calreticulin. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9258-1_4
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DOI: https://doi.org/10.1007/978-1-4419-9258-1_4
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