Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals

Mostrar todas las versiones(2)

Glucosidase II (GII) plays a key role in glycoprotein biogenesis in the endoplasmic reticulum (ER). It is responsible for the sequential removal of the two innermost glucose residues from the glycan (Glc3Man9GlcNAc2) transferred to Asn residues in proteins. GII participates in the calnexin/calreticu...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Stigliano, I.D., Caramelo, J.J., Labriola, C.A., Parodi, A.J., D'Alessio, C.
Formato:	JOUR
Materias:	glucopyranoside glucosidase glucosidase II beta somatomedin B receptor unclassified drug article enzyme active site hydrolysis mammal nonhuman nucleotide sequence priority journal protein domain protein folding Schizosaccharomyces pombe alpha-Glucosidases Amino Acid Sequence Animals Carbohydrate Conformation Carbohydrate Sequence Catalytic Domain Glucosides Isoenzymes Molecular Sequence Data Mutagenesis Polysaccharides Protein Folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Rats Receptor, IGF Type 2 Schizosaccharomyces Schizosaccharomyces pombe Proteins Sequence Alignment Mammalia Schizosaccharomycetaceae
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_10591524_v20_n17_p3974_Stigliano
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_10591524_v20_n17_p3974_Stigliano
record_format	dspace
spelling	todo:paper_10591524_v20_n17_p3974_Stigliano2023-10-03T16:01:02Z Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals Stigliano, I.D. Caramelo, J.J. Labriola, C.A. Parodi, A.J. D'Alessio, C. glucopyranoside glucosidase glucosidase II beta somatomedin B receptor unclassified drug article enzyme active site hydrolysis mammal nonhuman nucleotide sequence priority journal protein domain protein folding Schizosaccharomyces pombe alpha-Glucosidases Amino Acid Sequence Animals Carbohydrate Conformation Carbohydrate Sequence Catalytic Domain Glucosides Isoenzymes Molecular Sequence Data Mutagenesis Polysaccharides Protein Folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Rats Receptor, IGF Type 2 Schizosaccharomyces Schizosaccharomyces pombe Proteins Sequence Alignment Mammalia Schizosaccharomyces pombe Schizosaccharomycetaceae Glucosidase II (GII) plays a key role in glycoprotein biogenesis in the endoplasmic reticulum (ER). It is responsible for the sequential removal of the two innermost glucose residues from the glycan (Glc3Man9GlcNAc2) transferred to Asn residues in proteins. GII participates in the calnexin/calreticulin cycle; it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. GII is a heterodimer whose α subunit (GIIα) bears the glycosyl hydrolase active site, whereas its β subunit (GIIβ) role is controversial and has been reported to be involved in GIIα ER retention and folding. Here, we report that in the absence of GIIβ, the catalytic subunit GIIα of the fission yeast Schizosaccharomyces pombe (an organism displaying a glycoprotein folding quality control mechanism similar to that occurring in mammalian cells) folds to an active conformation able to hydrolyze p-nitrophenyl α-D-glucopyranoside. However, the heterodimer is required to efficiently deglucosylate the physiological substrates Glc2Man 9GlcNAc2 (G2M9) and Glc1Man 9GlcNAc2 (G1M9). The interaction of the mannose 6-phosphate receptor homologous domain present in GIIβ and mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement. We present evidence that also in mammalian cells GIIβ modulates G2M9 and G1M9 trimming. © 2009 by The American Society for Cell Biology. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_10591524_v20_n17_p3974_Stigliano
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	glucopyranoside glucosidase glucosidase II beta somatomedin B receptor unclassified drug article enzyme active site hydrolysis mammal nonhuman nucleotide sequence priority journal protein domain protein folding Schizosaccharomyces pombe alpha-Glucosidases Amino Acid Sequence Animals Carbohydrate Conformation Carbohydrate Sequence Catalytic Domain Glucosides Isoenzymes Molecular Sequence Data Mutagenesis Polysaccharides Protein Folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Rats Receptor, IGF Type 2 Schizosaccharomyces Schizosaccharomyces pombe Proteins Sequence Alignment Mammalia Schizosaccharomyces pombe Schizosaccharomycetaceae
spellingShingle	glucopyranoside glucosidase glucosidase II beta somatomedin B receptor unclassified drug article enzyme active site hydrolysis mammal nonhuman nucleotide sequence priority journal protein domain protein folding Schizosaccharomyces pombe alpha-Glucosidases Amino Acid Sequence Animals Carbohydrate Conformation Carbohydrate Sequence Catalytic Domain Glucosides Isoenzymes Molecular Sequence Data Mutagenesis Polysaccharides Protein Folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Rats Receptor, IGF Type 2 Schizosaccharomyces Schizosaccharomyces pombe Proteins Sequence Alignment Mammalia Schizosaccharomyces pombe Schizosaccharomycetaceae Stigliano, I.D. Caramelo, J.J. Labriola, C.A. Parodi, A.J. D'Alessio, C. Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals
topic_facet	glucopyranoside glucosidase glucosidase II beta somatomedin B receptor unclassified drug article enzyme active site hydrolysis mammal nonhuman nucleotide sequence priority journal protein domain protein folding Schizosaccharomyces pombe alpha-Glucosidases Amino Acid Sequence Animals Carbohydrate Conformation Carbohydrate Sequence Catalytic Domain Glucosides Isoenzymes Molecular Sequence Data Mutagenesis Polysaccharides Protein Folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Tertiary Protein Subunits Rats Receptor, IGF Type 2 Schizosaccharomyces Schizosaccharomyces pombe Proteins Sequence Alignment Mammalia Schizosaccharomyces pombe Schizosaccharomycetaceae
description	Glucosidase II (GII) plays a key role in glycoprotein biogenesis in the endoplasmic reticulum (ER). It is responsible for the sequential removal of the two innermost glucose residues from the glycan (Glc3Man9GlcNAc2) transferred to Asn residues in proteins. GII participates in the calnexin/calreticulin cycle; it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. GII is a heterodimer whose α subunit (GIIα) bears the glycosyl hydrolase active site, whereas its β subunit (GIIβ) role is controversial and has been reported to be involved in GIIα ER retention and folding. Here, we report that in the absence of GIIβ, the catalytic subunit GIIα of the fission yeast Schizosaccharomyces pombe (an organism displaying a glycoprotein folding quality control mechanism similar to that occurring in mammalian cells) folds to an active conformation able to hydrolyze p-nitrophenyl α-D-glucopyranoside. However, the heterodimer is required to efficiently deglucosylate the physiological substrates Glc2Man 9GlcNAc2 (G2M9) and Glc1Man 9GlcNAc2 (G1M9). The interaction of the mannose 6-phosphate receptor homologous domain present in GIIβ and mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement. We present evidence that also in mammalian cells GIIβ modulates G2M9 and G1M9 trimming. © 2009 by The American Society for Cell Biology.
format	JOUR
author	Stigliano, I.D. Caramelo, J.J. Labriola, C.A. Parodi, A.J. D'Alessio, C.
author_facet	Stigliano, I.D. Caramelo, J.J. Labriola, C.A. Parodi, A.J. D'Alessio, C.
author_sort	Stigliano, I.D.
title	Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals
title_short	Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals
title_full	Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals
title_fullStr	Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals
title_full_unstemmed	Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals
title_sort	glucosidase ii β subunit modulates n-glycan trimming in fission yeasts and mammals
url	http://hdl.handle.net/20.500.12110/paper_10591524_v20_n17_p3974_Stigliano
work_keys_str_mv	AT stiglianoid glucosidaseiibsubunitmodulatesnglycantrimminginfissionyeastsandmammals AT caramelojj glucosidaseiibsubunitmodulatesnglycantrimminginfissionyeastsandmammals AT labriolaca glucosidaseiibsubunitmodulatesnglycantrimminginfissionyeastsandmammals AT parodiaj glucosidaseiibsubunitmodulatesnglycantrimminginfissionyeastsandmammals AT dalessioc glucosidaseiibsubunitmodulatesnglycantrimminginfissionyeastsandmammals
_version_	1807321997801160704

Glucosidase II β subunit modulates N-glycan trimming in fission yeasts and mammals

Ejemplares similares