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

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 (Glc(3)Man(9)GlcNAc(2)) transferred to Asn residues in proteins. GII participates in the calnexin/cal...

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Detalles Bibliográficos
Autores: Stigliano, Ivan Daniel, Caramelo, Julio Javier, Labriola, Carlos Alberto, Parodi, Armando José A., D'Alessio, Cecilia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2009
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/28325
Acceso en línea:http://hdl.handle.net/11336/28325
Access Level:acceso abierto
Palabra clave:GLUCOSIDASE II
BETA SUBUNIT
SCHIZOSACCHAROMYCES POMBE
RAT LIVER
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
id AR_8a5928d3ae0804e10db9fb52daef27b9
oai_identifier_str oai:ri.conicet.gov.ar:11336/28325
network_acronym_str AR
network_name_str Argentina
repository_id_str
dc.title.none.fl_str_mv Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
title Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
spellingShingle Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
Stigliano, Ivan Daniel
GLUCOSIDASE II
BETA SUBUNIT
SCHIZOSACCHAROMYCES POMBE
RAT LIVER
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
title_short Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
title_full Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
title_fullStr Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
title_full_unstemmed Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
title_sort Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
dc.creator.none.fl_str_mv Stigliano, Ivan Daniel
Caramelo, Julio Javier
Labriola, Carlos Alberto
Parodi, Armando José A.
D'Alessio, Cecilia
author Stigliano, Ivan Daniel
author_facet Stigliano, Ivan Daniel
Caramelo, Julio Javier
Labriola, Carlos Alberto
Parodi, Armando José A.
D'Alessio, Cecilia
author_role author
author2 Caramelo, Julio Javier
Labriola, Carlos Alberto
Parodi, Armando José A.
D'Alessio, Cecilia
author2_role author
author
author
author
dc.subject.none.fl_str_mv GLUCOSIDASE II
BETA SUBUNIT
SCHIZOSACCHAROMYCES POMBE
RAT LIVER
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
topic GLUCOSIDASE II
BETA SUBUNIT
SCHIZOSACCHAROMYCES POMBE
RAT LIVER
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
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 (Glc(3)Man(9)GlcNAc(2)) 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 alpha subunit (GIIalpha) bears the glycosyl hydrolase active site, whereas its beta subunit (GIIbeta) role is controversial and has been reported to be involved in GIIalpha ER retention and folding. Here, we report that in the absence of GIIbeta, the catalytic subunit GIIalpha 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 alpha-d-glucopyranoside. However, the heterodimer is required to efficiently deglucosylate the physiological substrates Glc(2)Man(9)GlcNAc(2) (G2M9) and Glc(1)Man(9)GlcNAc(2) (G1M9). The interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta and mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement. We present evidence that also in mammalian cells GIIbeta modulates G2M9 and G1M9 trimming
publishDate 2009
dc.date.none.fl_str_mv 2009-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/28325
Stigliano, Ivan Daniel; Caramelo, Julio Javier; Labriola, Carlos Alberto; Parodi, Armando José A.; D'Alessio, Cecilia; Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals; American Society for Cell Biology; Molecular Biology Of The Cell; 20; 17; 7-2009; 3974-3984
1059-1524
1939-4586
CONICET Digital
CONICET
url http://hdl.handle.net/11336/28325
identifier_str_mv Stigliano, Ivan Daniel; Caramelo, Julio Javier; Labriola, Carlos Alberto; Parodi, Armando José A.; D'Alessio, Cecilia; Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals; American Society for Cell Biology; Molecular Biology Of The Cell; 20; 17; 7-2009; 3974-3984
1059-1524
1939-4586
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.molbiolcell.org/content/20/17/3974
info:eu-repo/semantics/altIdentifier/doi/10.1091/mbc.E09-04-0316
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Cell Biology
publisher.none.fl_str_mv American Society for Cell Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1799194596128849920
spelling Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammalsStigliano, Ivan DanielCaramelo, Julio JavierLabriola, Carlos AlbertoParodi, Armando José A.D'Alessio, CeciliaGLUCOSIDASE IIBETA SUBUNITSCHIZOSACCHAROMYCES POMBERAT LIVERhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glucosidase 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 (Glc(3)Man(9)GlcNAc(2)) 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 alpha subunit (GIIalpha) bears the glycosyl hydrolase active site, whereas its beta subunit (GIIbeta) role is controversial and has been reported to be involved in GIIalpha ER retention and folding. Here, we report that in the absence of GIIbeta, the catalytic subunit GIIalpha 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 alpha-d-glucopyranoside. However, the heterodimer is required to efficiently deglucosylate the physiological substrates Glc(2)Man(9)GlcNAc(2) (G2M9) and Glc(1)Man(9)GlcNAc(2) (G1M9). The interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta and mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement. We present evidence that also in mammalian cells GIIbeta modulates G2M9 and G1M9 trimmingFil: Stigliano, Ivan Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Caramelo, Julio Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires; ArgentinaFil: Labriola, Carlos Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Parodi, Armando José A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: D'Alessio, Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Universidad de Buenos Aires; ArgentinaAmerican Society for Cell Biology2009-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/28325Stigliano, Ivan Daniel; Caramelo, Julio Javier; Labriola, Carlos Alberto; Parodi, Armando José A.; D'Alessio, Cecilia; Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals; American Society for Cell Biology; Molecular Biology Of The Cell; 20; 17; 7-2009; 3974-39841059-15241939-4586CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.molbiolcell.org/content/20/17/3974info:eu-repo/semantics/altIdentifier/doi/10.1091/mbc.E09-04-0316info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:32:28Zoai:ri.conicet.gov.ar:11336/28325instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982024-05-08 13:32:28.697CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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