dc.creator | Stigliano, Ivan Daniel | |
dc.creator | Alculumbre, Solana G. | |
dc.creator | Labriola, Carlos Alberto | |
dc.creator | Parodi, Armando José A. | |
dc.creator | D'Alessio, Cecilia | |
dc.date.accessioned | 2020-02-21T21:40:27Z | |
dc.date.accessioned | 2022-10-14T23:55:00Z | |
dc.date.available | 2020-02-21T21:40:27Z | |
dc.date.available | 2022-10-14T23:55:00Z | |
dc.date.created | 2020-02-21T21:40:27Z | |
dc.date.issued | 2011-06 | |
dc.identifier | Stigliano, Ivan Daniel; Alculumbre, Solana G.; Labriola, Carlos Alberto; Parodi, Armando José A.; D'Alessio, Cecilia; Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo; American Society for Cell Biology; Molecular Biology Of The Cell; 22; 11; 6-2011; 1810-1823 | |
dc.identifier | 1059-1524 | |
dc.identifier | http://hdl.handle.net/11336/98367 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4321863 | |
dc.description.abstract | Glucosidase II (GII) sequentially removes the two innermost glucose residues from the glycan (Glc3Man9GlcNAc2) transferred to proteins. GII also participates in cycles involving the lectin/chaperones calnexin (CNX) and calreticulin (CRT) as it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDPGlc: glycoprotein glucosyltransferase (UGGT). GII is a heterodimer in which the á subunit (GIIα) bears the active site, and the β subunit (GIIβ) modulates GIIα activity through its C-terminal mannose 6-phosphate receptor homologous (MRH) domain. Here we report that, as already described in cell-free assays, in live Schizosaccharomyces pombe cells a decrease in the number of mannoses in the glycan results in decreased GII activity. Contrary to previously reported cell-free experiments, however, no such effect was observed in vivo for UGGT. We propose that endoplasmic reticulum α-mannosidase-mediated N-glycan demannosylation of misfolded/slow-folding glycoproteins may favor their interaction with the lectin/chaperone CNX present in S. pombe by prolonging the half-lives of the monoglucosylated glycans (S. pombe lacks CRT). Moreover, we show that even N-glycans bearing five mannoses may interact in vivo with the GIIβ MRH domain and that the N-terminal GIIβ G2B domain is involved in the GIIα-GIIβ interaction. Finally, we report that protists that transfer glycans with low mannose content to proteins have nevertheless conserved the possibility of displaying relatively long-lived monoglucosylated glycans by expressing GIIβ MRH domains with a higher specificity for glycans with high mannose content. | |
dc.language | eng | |
dc.publisher | American Society for Cell Biology | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.molbiolcell.org/doi/10.1091/mbc.e11-01-0019 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1091/mbc.e11-01-0019 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | GLUCOSIDASE II BETA | |
dc.subject | ENDOPLASMIC RETICULUM | |
dc.subject | GLYCOPROTEIN FOLDING | |
dc.subject | GLUCOSYLTRANSFERASE | |
dc.title | Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |