N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway

Autores
D'alessio, Cecilia
Año de publicación
2019
Idioma
español castellano
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
N-glycans transferred to proteins are remodeled in the endoplasmic reticulum (ER) producing structures that determine the fate of the glycoproteins within the secretory pathway. Glucosidase II (GII) is a key player in N-glycan processing as it removes the two inner glucose residues from the glycan transferred to proteins during N-glycosylation and the glucose residue added back to not yet properly folded proteins during the quality control of glycoprotein folding in the ER. GII is a heterodimer whose alpha subunit bears the catalytic site while its beta subunit enhances deglucosylation activity through its Cterminal Mannose-6-phosphate (M6P) receptor homology (MRH) domain. A family of glycan receptors bearing MRH domains, including CD-MPR & CI-MPR (responsible for delivering acidic hydrolases with M6P signal to lysosomes), N-acetylglucosamine-1- phosphotransferase g subunit (responsible of generating the M6P signal), OS-9 (involved in the glycoprotein degradation pathway) and GII beta subunit recognize subtle differences in the N-glycan structures. Comparison of their structures showed a similar overall fold and identified conserved residues critical for the structural integrity of the carbohydrate binding pocket. Nonetheless, each one has its unique substrate specificity and its binding defines if the protein will continue in the folding process, will be delivered to lysosomes or will be degraded in proteasomes. In the present work, we show the effects on GII activity of swapping its own GII beta MRH domain for those MRH domains present in other lectins of the secretory pathway.
Fil: 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
XLVIII Reunión Anual de la Sociedad Argentina de Biofísica
San Luis
Argentina
Sociedad Argentina de Biofísica
Universidad Nacional de San Luis
Materia
Glycosylation
MRH domain
secretory pathway
yeast
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/174497
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathwayD'alessio, CeciliaGlycosylationMRH domainsecretory pathwayyeasthttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1N-glycans transferred to proteins are remodeled in the endoplasmic reticulum (ER) producing structures that determine the fate of the glycoproteins within the secretory pathway. Glucosidase II (GII) is a key player in N-glycan processing as it removes the two inner glucose residues from the glycan transferred to proteins during N-glycosylation and the glucose residue added back to not yet properly folded proteins during the quality control of glycoprotein folding in the ER. GII is a heterodimer whose alpha subunit bears the catalytic site while its beta subunit enhances deglucosylation activity through its Cterminal Mannose-6-phosphate (M6P) receptor homology (MRH) domain. A family of glycan receptors bearing MRH domains, including CD-MPR & CI-MPR (responsible for delivering acidic hydrolases with M6P signal to lysosomes), N-acetylglucosamine-1- phosphotransferase g subunit (responsible of generating the M6P signal), OS-9 (involved in the glycoprotein degradation pathway) and GII beta subunit recognize subtle differences in the N-glycan structures. Comparison of their structures showed a similar overall fold and identified conserved residues critical for the structural integrity of the carbohydrate binding pocket. Nonetheless, each one has its unique substrate specificity and its binding defines if the protein will continue in the folding process, will be delivered to lysosomes or will be degraded in proteasomes. In the present work, we show the effects on GII activity of swapping its own GII beta MRH domain for those MRH domains present in other lectins of the secretory pathway.Fil: 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; ArgentinaXLVIII Reunión Anual de la Sociedad Argentina de BiofísicaSan LuisArgentinaSociedad Argentina de BiofísicaUniversidad Nacional de San LuisSociedad Argentina de BiofísicaAndujar, Sebastian Antonio2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/174497N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 1-1978-987-27591-7-9CONICET DigitalCONICETspainfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:37:19Zoai:ri.conicet.gov.ar:11336/174497instacron: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:34982025-10-15 14:37:20.144CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
title N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
spellingShingle N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
D'alessio, Cecilia
Glycosylation
MRH domain
secretory pathway
yeast
title_short N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
title_full N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
title_fullStr N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
title_full_unstemmed N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
title_sort N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway
dc.creator.none.fl_str_mv D'alessio, Cecilia
author D'alessio, Cecilia
author_facet D'alessio, Cecilia
author_role author
dc.contributor.none.fl_str_mv Andujar, Sebastian Antonio
dc.subject.none.fl_str_mv Glycosylation
MRH domain
secretory pathway
yeast
topic Glycosylation
MRH domain
secretory pathway
yeast
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv N-glycans transferred to proteins are remodeled in the endoplasmic reticulum (ER) producing structures that determine the fate of the glycoproteins within the secretory pathway. Glucosidase II (GII) is a key player in N-glycan processing as it removes the two inner glucose residues from the glycan transferred to proteins during N-glycosylation and the glucose residue added back to not yet properly folded proteins during the quality control of glycoprotein folding in the ER. GII is a heterodimer whose alpha subunit bears the catalytic site while its beta subunit enhances deglucosylation activity through its Cterminal Mannose-6-phosphate (M6P) receptor homology (MRH) domain. A family of glycan receptors bearing MRH domains, including CD-MPR & CI-MPR (responsible for delivering acidic hydrolases with M6P signal to lysosomes), N-acetylglucosamine-1- phosphotransferase g subunit (responsible of generating the M6P signal), OS-9 (involved in the glycoprotein degradation pathway) and GII beta subunit recognize subtle differences in the N-glycan structures. Comparison of their structures showed a similar overall fold and identified conserved residues critical for the structural integrity of the carbohydrate binding pocket. Nonetheless, each one has its unique substrate specificity and its binding defines if the protein will continue in the folding process, will be delivered to lysosomes or will be degraded in proteasomes. In the present work, we show the effects on GII activity of swapping its own GII beta MRH domain for those MRH domains present in other lectins of the secretory pathway.
Fil: 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
XLVIII Reunión Anual de la Sociedad Argentina de Biofísica
San Luis
Argentina
Sociedad Argentina de Biofísica
Universidad Nacional de San Luis
description N-glycans transferred to proteins are remodeled in the endoplasmic reticulum (ER) producing structures that determine the fate of the glycoproteins within the secretory pathway. Glucosidase II (GII) is a key player in N-glycan processing as it removes the two inner glucose residues from the glycan transferred to proteins during N-glycosylation and the glucose residue added back to not yet properly folded proteins during the quality control of glycoprotein folding in the ER. GII is a heterodimer whose alpha subunit bears the catalytic site while its beta subunit enhances deglucosylation activity through its Cterminal Mannose-6-phosphate (M6P) receptor homology (MRH) domain. A family of glycan receptors bearing MRH domains, including CD-MPR & CI-MPR (responsible for delivering acidic hydrolases with M6P signal to lysosomes), N-acetylglucosamine-1- phosphotransferase g subunit (responsible of generating the M6P signal), OS-9 (involved in the glycoprotein degradation pathway) and GII beta subunit recognize subtle differences in the N-glycan structures. Comparison of their structures showed a similar overall fold and identified conserved residues critical for the structural integrity of the carbohydrate binding pocket. Nonetheless, each one has its unique substrate specificity and its binding defines if the protein will continue in the folding process, will be delivered to lysosomes or will be degraded in proteasomes. In the present work, we show the effects on GII activity of swapping its own GII beta MRH domain for those MRH domains present in other lectins of the secretory pathway.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/174497
N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 1-1
978-987-27591-7-9
CONICET Digital
CONICET
url http://hdl.handle.net/11336/174497
identifier_str_mv N-glycan structures, lectin domains, and glycoprotein’s fate in the secretory pathway; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 1-1
978-987-27591-7-9
CONICET Digital
CONICET
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/
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/vnd.openxmlformats-officedocument.wordprocessingml.document
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Sociedad Argentina de Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
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
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score 13.22299

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