ER quality control: towards an understanding at the molecular level
- PMID: 11454449
- DOI: 10.1016/s0955-0674(00)00233-7
ER quality control: towards an understanding at the molecular level
Abstract
The process of 'quality control' in the endoplasmic reticulum (ER) involves a variety of mechanisms that collectively ensure that only correctly folded, assembled and modified proteins are transported along the secretory pathway. In contrast, non-native proteins are retained and eventually _targeted for degradation. Recent work provides the first structural insights into the process of glycoprotein folding in the ER involving the lectin chaperones calnexin and calreticulin. Underlying principles governing the choice of chaperone system engaged by different proteins have also been discovered.
Similar articles
-
Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?FEBS Lett. 2000 Jun 30;476(1-2):38-41. doi: 10.1016/s0014-5793(00)01666-5. FEBS Lett. 2000. PMID: 10878246 Review.
-
Lectins as chaperones in glycoprotein folding.Curr Opin Struct Biol. 1998 Oct;8(5):587-92. doi: 10.1016/s0959-440x(98)80148-6. Curr Opin Struct Biol. 1998. PMID: 9818262 Review.
-
Lectins of the ER quality control machinery.Results Probl Cell Differ. 2001;33:1-17. doi: 10.1007/978-3-540-46410-5_1. Results Probl Cell Differ. 2001. PMID: 11190669 Review. No abstract available.
-
Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57.J Biol Chem. 1998 Mar 13;273(11):6009-12. doi: 10.1074/jbc.273.11.6009. J Biol Chem. 1998. PMID: 9497314
-
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.Mol Biol Cell. 1999 Aug;10(8):2573-82. doi: 10.1091/mbc.10.8.2573. Mol Biol Cell. 1999. PMID: 10436013 Free PMC article.
Cited by
-
Functional characterization of a loss-of-function mutant I324M of arginine vasopressin receptor 2 in X-linked nephrogenic diabetes insipidus.Sci Rep. 2021 May 26;11(1):11057. doi: 10.1038/s41598-021-90736-z. Sci Rep. 2021. PMID: 34040143 Free PMC article.
-
Cellular chaperones and folding enzymes are vital contributors to membrane bound replication and movement complexes during plant RNA virus infection.Front Plant Sci. 2012 Dec 6;3:275. doi: 10.3389/fpls.2012.00275. eCollection 2012. Front Plant Sci. 2012. PMID: 23230447 Free PMC article.
-
CFTR and chaperones: processing and degradation.J Mol Neurosci. 2004;23(1-2):41-8. doi: 10.1385/JMN:23:1-2:041. J Mol Neurosci. 2004. PMID: 15126691 Review.
-
Cytoplasmic streaming enables the distribution of molecules and vesicles in large plant cells.Protoplasma. 2010 Apr;240(1-4):99-107. doi: 10.1007/s00709-009-0088-x. Epub 2009 Nov 25. Protoplasma. 2010. PMID: 19937356 Review.
-
Myelin biogenesis: vesicle transport in oligodendrocytes.Neurochem Res. 2002 Nov;27(11):1313-29. doi: 10.1023/a:1021667515030. Neurochem Res. 2002. PMID: 12512937 Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials