Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
- PMID: 9497314
- DOI: 10.1074/jbc.273.11.6009
Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
Abstract
The endoplasmic reticulum is the site of folding, disulfide bond formation, and N-glycosylation of secretory proteins. Correctly folded proteins are exported from the endoplasmic reticulum, whereas incorrectly folded proteins are retained by a quality control system. The type I membrane-protein calnexin and its soluble homologue calreticulin are constituents of this system that recognize monoglucosylated N-linked glycans that are present on unfolded glycoproteins. Although several components of the quality control apparatus are well characterized, it is not known whether and how they interact with enzymes that catalyze protein folding. The endoplasmic reticulum protein ERp57 is homologous to protein-disulfide isomerase and can be cross-linked to the same monoglucosylated glycoproteins that bind to calnexin and calreticulin. The present study demonstrates that the disulfide isomerase activity of ERp57 on the refolding of monoglucosylated ribonuclease B is much greater when this glycoprotein is associated with calnexin or calreticulin. This result is in contrast to protein-disulfide isomerase, whose activity on monoglucosylated ribonuclease B is decreased in the presence of these lectins. No direct binding of monoglucosylated ribonuclease B or monoglucosylated glycans to ERp57 could be detected, but we show that ERp57 interacts directly with calnexin.
Similar articles
-
The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins.J Biol Chem. 1997 May 23;272(21):13849-55. doi: 10.1074/jbc.272.21.13849. J Biol Chem. 1997. PMID: 9153243
-
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.
-
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.
-
Association of ERp57 with mouse MHC class I molecules is tapasin dependent and mimics that of calreticulin and not calnexin.J Immunol. 2001 Jun 1;166(11):6686-92. doi: 10.4049/jimmunol.166.11.6686. J Immunol. 2001. PMID: 11359824
-
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.
Cited by
-
Adenovirus-mediated delivery of CALR and MAGE-A3 inhibits invasion and angiogenesis of glioblastoma cell line U87.J Exp Clin Cancer Res. 2012 Feb 1;31(1):8. doi: 10.1186/1756-9966-31-8. J Exp Clin Cancer Res. 2012. PMID: 22293781 Free PMC article.
-
Calnexin, More Than Just a Molecular Chaperone.Cells. 2023 Jan 24;12(3):403. doi: 10.3390/cells12030403. Cells. 2023. PMID: 36766745 Free PMC article. Review.
-
NMR structure of the calreticulin P-domain.Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3133-8. doi: 10.1073/pnas.051630098. Epub 2001 Mar 6. Proc Natl Acad Sci U S A. 2001. PMID: 11248044 Free PMC article.
-
Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly.J Biol Chem. 2007 Oct 26;282(43):31113-23. doi: 10.1074/jbc.M705369200. Epub 2007 Aug 29. J Biol Chem. 2007. PMID: 17728248 Free PMC article.
-
Protein Quality Control in the Endoplasmic Reticulum.Protein J. 2019 Jun;38(3):317-329. doi: 10.1007/s10930-019-09831-w. Protein J. 2019. PMID: 31004255 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous
