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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. © 2011 Stigliano et al.

Registro:

Documento: Artículo
Título:Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo
Autor:Stigliano, I.D.; Alculumbre, S.G.; Labriola, C.A.; Parodi, A.J.; D'Alessio, C.
Filiación:Laboratory of Glycobiology, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires-CONICET, C1405BWE, Buenos Aires, Argentina
School of Sciences, University of Buenos Aires, C1428EHA, Buenos Aires, Argentina
Palabras clave:alpha glucosidase ab; alpha mannosidase; calnexin; calreticulin; glucosidase II alpha; glucosidase IIbeta; glycan; glycan derivative; glycoprotein; mannose; n glycan mannose; unclassified drug; amino terminal sequence; article; endoplasmic reticulum; enzyme activity; glycosylation; nonhuman; priority journal; protein expression; protein folding; protein interaction; Schizosaccharomyces pombe; alpha-Glucosidases; alpha-Mannosidase; Carbohydrate Sequence; Endoplasmic Reticulum; Gene Knockout Techniques; Glucosyltransferases; Glycoproteins; Half-Life; Hexosyltransferases; Mannose; Molecular Sequence Data; Polysaccharides; Protein Folding; Protein Interaction Domains and Motifs; Protein Stability; Protein Structure, Tertiary; Schizosaccharomyces; Protista; Schizosaccharomyces pombe
Año:2011
Volumen:22
Número:11
Página de inicio:1810
Página de fin:1823
DOI: http://dx.doi.org/10.1091/mbc.E11-01-0019
Título revista:Molecular Biology of the Cell
Título revista abreviado:Mol. Biol. Cell
ISSN:10591524
CODEN:MBCEE
CAS:alpha mannosidase, 9025-42-7; calnexin, 139873-08-8; mannose, 31103-86-3, 3458-28-4; 4-nitrophenyl-alpha-glucosidase, 3.2.1.-; Glucosyltransferases, 2.4.1.-; Glycoproteins; Hexosyltransferases, 2.4.1.-; Mannose, 31103-86-3; Polysaccharides; alpha-Glucosidases, 3.2.1.20; alpha-Mannosidase, 3.2.1.24; glycoprotein glycosyltransferase, 2.4.1.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10591524_v22_n11_p1810_Stigliano

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Citas:

---------- APA ----------
Stigliano, I.D., Alculumbre, S.G., Labriola, C.A., Parodi, A.J. & D'Alessio, C. (2011) . Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo. Molecular Biology of the Cell, 22(11), 1810-1823.
http://dx.doi.org/10.1091/mbc.E11-01-0019
---------- CHICAGO ----------
Stigliano, I.D., Alculumbre, S.G., Labriola, C.A., Parodi, A.J., D'Alessio, C. "Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo" . Molecular Biology of the Cell 22, no. 11 (2011) : 1810-1823.
http://dx.doi.org/10.1091/mbc.E11-01-0019
---------- MLA ----------
Stigliano, I.D., Alculumbre, S.G., Labriola, C.A., Parodi, A.J., D'Alessio, C. "Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo" . Molecular Biology of the Cell, vol. 22, no. 11, 2011, pp. 1810-1823.
http://dx.doi.org/10.1091/mbc.E11-01-0019
---------- VANCOUVER ----------
Stigliano, I.D., Alculumbre, S.G., Labriola, C.A., Parodi, A.J., D'Alessio, C. Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo. Mol. Biol. Cell. 2011;22(11):1810-1823.
http://dx.doi.org/10.1091/mbc.E11-01-0019