Association of folding intermediates of glycoproteins with calnexin during protein maturation - PubMed (original) (raw)
. 1993 Aug 26;364(6440):771-6.
doi: 10.1038/364771a0.
Affiliations
- PMID: 8102790
- DOI: 10.1038/364771a0
Association of folding intermediates of glycoproteins with calnexin during protein maturation
W J Ou et al. Nature. 1993.
Abstract
Calnexin, an endoplasmic reticulum transmembrane protein, represents a new type of molecular chaperone that selectively associates in a transient fashion with newly synthesized monomeric glycoproteins in HepG2 cells. Calnexin only recognizes glycoproteins when they are incompletely folded. Dissociation of glycoproteins from calnexin occurs at different rates and is related to the time taken for their folding, which may then initiate their differential transport rates from the endoplasmic reticulum.
Similar articles
- EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin.
Oda Y, Hosokawa N, Wada I, Nagata K. Oda Y, et al. Science. 2003 Feb 28;299(5611):1394-7. doi: 10.1126/science.1079181. Science. 2003. PMID: 12610305 - Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum.
Williams DB. Williams DB. J Cell Sci. 2006 Feb 15;119(Pt 4):615-23. doi: 10.1242/jcs.02856. J Cell Sci. 2006. PMID: 16467570 Review. - Calnexin associates with the precursors of glycoproteins B, C, and D of herpes simplex virus type 1.
Yamashita Y, Yamada M, Daikoku T, Yamada H, Tadauchi A, Tsurumi T, Nishiyama Y. Yamashita Y, et al. Virology. 1996 Nov 1;225(1):216-22. doi: 10.1006/viro.1996.0590. Virology. 1996. PMID: 8918549 - Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle.
Molinari M, Calanca V, Galli C, Lucca P, Paganetti P. Molinari M, et al. Science. 2003 Feb 28;299(5611):1397-400. doi: 10.1126/science.1079474. Science. 2003. PMID: 12610306 - Lectins as chaperones in glycoprotein folding.
Trombetta ES, Helenius A. Trombetta ES, et al. 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.
Cited by
- A transporter's doom or destiny: SLC6A1 in health and disease, novel molecular targets and emerging therapeutic prospects.
Shah N, Kasture AS, Fischer FP, Sitte HH, Hummel T, Sucic S. Shah N, et al. Front Mol Neurosci. 2024 Aug 29;17:1466694. doi: 10.3389/fnmol.2024.1466694. eCollection 2024. Front Mol Neurosci. 2024. PMID: 39268250 Free PMC article. Review. - A genome-wide CRISPR/Cas9 screen identifies calreticulin as a selective repressor of ATF6α.
Tung J, Huang L, George G, Harding HP, Ron D, Ordonez A. Tung J, et al. Elife. 2024 Jul 29;13:RP96979. doi: 10.7554/eLife.96979. Elife. 2024. PMID: 39073063 Free PMC article. - α-Synuclein: Multiple pathogenic roles in trafficking and proteostasis pathways in Parkinson's disease.
Zalon AJ, Quiriconi DJ, Pitcairn C, Mazzulli JR. Zalon AJ, et al. Neuroscientist. 2024 Oct;30(5):612-635. doi: 10.1177/10738584241232963. Epub 2024 Feb 29. Neuroscientist. 2024. PMID: 38420922 Review. - The conformational landscape of a serpin N-terminal subdomain facilitates folding and in-cell quality control.
Kaur U, Kihn KC, Ke H, Kuo W, Gierasch LM, Hebert DN, Wintrode PL, Deredge D, Gershenson A. Kaur U, et al. bioRxiv [Preprint]. 2023 Apr 26:2023.04.24.537978. doi: 10.1101/2023.04.24.537978. bioRxiv. 2023. PMID: 37163105 Free PMC article. Preprint. - Activation of Ca2+ transport in cardiac microsomes enriches functional sets of ER and SR proteins.
Cala SE, Carruthers NJ, Stemmer PM, Chen Z, Chen X. Cala SE, et al. Mol Cell Biochem. 2024 Jan;479(1):85-98. doi: 10.1007/s11010-023-04708-0. Epub 2023 Apr 10. Mol Cell Biochem. 2024. PMID: 37036634 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources