Abrogation of glucosidase I–mediated glycoprotein deglucosylation results in a sick phenotype in fission yeasts: Model for the human MOGS-CDG disorder
Glucosidase I (GI) removes the outermost glucose from protein-linked Glc 3 Man 9 GlcNAc 2 (G3M9) in the endoplasmic reticulum (ER). Individuals with congenital disorders of glycosylation MOGS-CDG bear mutations in the GI-encoding gene (gls1). Although GI absence has been reported to produce lethalit...
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American Society for Biochemistry and Molecular Biology Inc.
2018
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| LEADER | 16835caa a22013937a 4500 | ||
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| 001 | PAPER-25352 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205723.0 | ||
| 008 | 190410s2018 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-85059236352 | |
| 024 | 7 | |2 cas |a glucosidase, 9033-06-1; glucosyltransferase, 9031-48-5 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a JBCHA | ||
| 100 | 1 | |a Gallo, G.L. | |
| 245 | 1 | 0 | |a Abrogation of glucosidase I–mediated glycoprotein deglucosylation results in a sick phenotype in fission yeasts: Model for the human MOGS-CDG disorder |
| 260 | |b American Society for Biochemistry and Molecular Biology Inc. |c 2018 | ||
| 270 | 1 | 0 | |m D’Alessio, C.; Fundación Instituto Leloir–IIBBA, CONICETArgentina; email: cdalessio@leloir.org.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 520 | 3 | |a Glucosidase I (GI) removes the outermost glucose from protein-linked Glc 3 Man 9 GlcNAc 2 (G3M9) in the endoplasmic reticulum (ER). Individuals with congenital disorders of glycosylation MOGS-CDG bear mutations in the GI-encoding gene (gls1). Although GI absence has been reported to produce lethality in Schizosaccharomyces pombe yeasts, here we obtained two viable gls1 mutants, one with a very sick but not lethal phenotype (gls1-S) and the other with a healthier one (gls1-H). The sick strain displayed only G3M9 as an ER protein–linked oligosaccharide, whereas the healthier strain had both G3M9 and Man 9 GlcNAc 2 . The lipid-linked oligosaccharide patterns of the two strains revealed that the most abundantly formed glycans were G3M9 in gls1-S and Glc 2 Man 9 GlcNAc 2 in gls1-H, suggesting reduced Alg10p glucosyltransferase activity in the gls1-H strain. A mutation in the alg10 gene was indeed observed in this strain. Our results indicated that abrogated G3M9 deglucosylation was responsible for the severe defects observed in gls1-S cells. Further studies disclosed that the defects could not be ascribed to disruption of glycoprotein entrance into calnexin-folding cycles, inhibition of the oligosaccharyltransferase by transfer reaction products, or reduced proteasomal degradation of misfolded glycoproteins. Lack of triglucosylated glycoprotein deglucosylation neither significantly prevented glycan elongation in the Golgi nor modified the overall cell wall monosaccharide composition. Nevertheless, it resulted in a distorted cell wall and in the absence of underlying ER membranes. Furthermore, Golgi expression of human endomannosidase partially restored normal growth in gls1-S cells. We propose that accumulation of G3M9-bearing glycoproteins is toxic and at least partially responsible for defects observed in MOGS-CDG. © 2018 Gallo et al. |l eng | |
| 536 | |a Detalles de la financiación: National Research Council | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, PIP-11220150100759, 3Both | ||
| 536 | |a Detalles de la financiación: This work was supported in part by the National Research Council (CONICET, Argentina) Grant PIP-11220150100759. The authors declare that they have no conflicts of interest with the contents of this article. This article contains Figs. S1–S5 and Table S1. 1 Both authors are CONICET fellows. 2 These authors contributed equally to this work. 3Both authors are Career Investigators of the National Research Council (CONICET, Argentina). 4 To whom correspondence should be addressed: Fundación Instituto Leloir, Av. Patricias Argentinas 435, Buenos Aires C1405BWE, Argentina. Tel.: 5411-5238-7500 (Ext. 2302); Fax: 5411-5238-7501; E-mail: cdalessio@ leloir.org.ar. | ||
| 593 | |a Fundación Instituto Leloir–IIBBA, CONICET, Buenos Aires, C1405BWE, Argentina | ||
| 593 | |a Institute of Biochemistry and Molecular Biology Medical Faculty, University of Bonn, Bonn, 53115, Germany | ||
| 593 | |a Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EGA, Argentina | ||
| 593 | |a Fundación Instituto Leloir, Av. Patricias Argentinas 435, Buenos Aires, C1405BWE, Argentina | ||
| 690 | 1 | 0 | |a GLUCOSIDASE |
| 690 | 1 | 0 | |a GLUCOSIDASE I |
| 690 | 1 | 0 | |a GLUCOSYLTRANSFERASE |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BIOACCUMULATION |
| 690 | 1 | 0 | |a CELL DEATH |
| 690 | 1 | 0 | |a CELL ELONGATION |
| 690 | 1 | 0 | |a CELLULAR DISTRIBUTION |
| 690 | 1 | 0 | |a CHEMICAL MODIFICATION |
| 690 | 1 | 0 | |a CONFORMATION |
| 690 | 1 | 0 | |a CONGENITAL DISORDER OF GLYCOSYLATION |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a DEGLUCOSYLATION |
| 690 | 1 | 0 | |a ENDOPLASMIC RETICULUM |
| 690 | 1 | 0 | |a ENZYME ACTIVITY |
| 690 | 1 | 0 | |a FUNGAL CELL |
| 690 | 1 | 0 | |a FUNGAL CELL WALL |
| 690 | 1 | 0 | |a FUNGUS GROWTH |
| 690 | 1 | 0 | |a GENE MUTATION |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PHENOTYPE |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN DEGRADATION |
| 690 | 1 | 0 | |a PROTEIN EXPRESSION |
| 690 | 1 | 0 | |a PROTEIN FOLDING |
| 690 | 1 | 0 | |a PROTEIN MISFOLDING |
| 690 | 1 | 0 | |a SCHIZOSACCHAROMYCES POMBE |
| 690 | 1 | 0 | |a TRANSMISSION ELECTRON MICROSCOPY |
| 700 | 1 | |a Valko, A. | |
| 700 | 1 | |a Aramburu, S.I. | |
| 700 | 1 | |a Etchegaray, E. | |
| 700 | 1 | |a Völker, C. | |
| 700 | 1 | |a Parodi, A.J. | |
| 700 | 1 | |a D’Alessio, C. | |
| 773 | 0 | |d American Society for Biochemistry and Molecular Biology Inc., 2018 |g v. 293 |h pp. 19957-19973 |k n. 52 |p J. Biol. Chem. |x 00219258 |w (AR-BaUEN)CENRE-175 |t Journal of Biological Chemistry | |
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| 856 | 4 | 0 | |u https://doi.org/10.1074/jbc.RA118.004844 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_00219258_v293_n52_p19957_Gallo |y Handle |
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