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.
| Original language | English |
|---|---|
| Pages (from-to) | 91-121 |
| Number of pages | 31 |
| Journal | International Review of Cytology |
| Volume | 245 |
| DOIs | |
| Publication status | Published - 2005 |
| Externally published | Yes |
Bibliographical note
Funding Information:This work was supported by grants from the CIHR (to M.M. and M.O.) and from the Heart and Stroke Foundations of Ontario (to M.O.). M.M. is a CIHR Senior Investigator. M.O. is a member of the Heart & Stroke/Richard Lewar Centre of Excellence.
ASJC Scopus Subject Areas
- Histology
- Cell Biology