| Literature DB >> 16125546 |
Karen Bedard1, Eva Szabo, Marek Michalak, Michal Opas.
Abstract
Glycosylated proteins destined for the cell surface or to be secreted from the cell are trafficked through the endoplasmic reticulum during synthesis and folding. Correct folding is determined in large part by the sequence of the protein, but it is also assisted by interaction with enzymes and chaperones of the endoplasmic reticulum. Calreticulin, calnexin, and ERp57 are among the endoplasmic chaperones that interact with partially folded glycoproteins and determine if the proteins are to be released from the endoplasmic reticulum to be expressed, or alternatively, if they are to be sent to the proteosome for degradation. Studies on the effect of alterations in the expression and function of these proteins are providing information about the importance of this quality control system, as well as uncovering other important functions these proteins play outside of the endoplasmic reticulum.Entities:
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Year: 2005 PMID： 16125546 DOI： 10.1016/S0074-7696(05)45004-4
Source DB: PubMed Journal: Int Rev Cytol ISSN： 0074-7696