Abstract
Molecular chaperones assist the folding of nascent chains in the cell. Chaperones also aid in quality control decisions as persistent chaperone binding can help to sort terminal misfolded proteins for degradation. There are two major molecular chaperone families in the endoplasmic reticulum (ER) that assist proteins in reaching their native structure and evaluating the fidelity of the maturation process. The ER Hsp70 chaperone, BiP, supports adenine nucleotide-regulated binding to non-native proteins that possess exposed hydrophobic regions. In contrast, the carbohydrate-dependent chaperone system involving the membrane protein calnexin and its soluble paralogue calreticulin recognize a specific glycoform of an exposed hydrophilic protein modification for which the composition is controlled by a series of glycosidases and transferases. Here, we compare and contrast the properties, mechanisms of action and functions of these different chaperones systems that work in parallel, as well as together, to assist a large variety of substrates that traverse the eukaryotic secretory pathway.
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Abbreviations
- AMP:
-
Adenosine 5′-monophosphate
- ATP:
-
Adenosine triphosphate
- BiP:
-
Binding-immunoglobulin protein
- CNX:
-
Calnexin
- CRT:
-
Calreticulin
- CypB:
-
Cyclophilin B
- ER:
-
Endoplasmic reticulum
- ERdj:
-
ER-localized DNAJ
- NBD:
-
Nucleotide binding domain
- PDIA3:
-
Protein disulfide-isomerase A3
- PDIA9:
-
Protein disulfide-isomerase A9
- SBD:
-
Substrate binding domain
- Sep15:
-
Selenoprotein F
- TPR:
-
Tetratrico peptide repeat
- UGGT1(2):
-
UDP-glucose: glycoprotein glucosyltransferase I (II)
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Acknowledgements
This work was supported by the National Institutes of Health ((GM086874 to D.N.H.) and a Chemistry-Biology Interface program training grant (T32GM008515 to B.M.A. and N.P.C.)).
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Adams, B.M., Canniff, N.P., Guay, K.P., Hebert, D.N. (2021). The Role of Endoplasmic Reticulum Chaperones in Protein Folding and Quality Control. In: Agellon, L.B., Michalak, M. (eds) Cellular Biology of the Endoplasmic Reticulum . Progress in Molecular and Subcellular Biology, vol 59. Springer, Cham. https://doi.org/10.1007/978-3-030-67696-4_3
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