Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells
- Autores
- Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; Pfrengle, Fabian; Bacic, Antony; Estevez, Jose Manuel
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.
Fil: Strasser, Richard. University of Natural Resources and Life Sciences; Suiza
Fil: Seifert, Georg. University of Natural Resources and Life Sciences; Suiza
Fil: Doblin, Monika S.. La Trobe University; Australia
Fil: Johnson, Kim L.. La Trobe University; Australia
Fil: Ruprecht, Colin. University of Natural Resources and Life Sciences; Suiza
Fil: Pfrengle, Fabian. University of Natural Resources and Life Sciences; Suiza
Fil: Bacic, Antony. La Trobe University; Australia
Fil: Estevez, Jose Manuel. 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 - Materia
-
ARABIDOPSIS
GLYCAN ARRAYS
GLYCAN FUNCTIONS
GLYCOSYL HYDROLASES
GLYCOSYLTRANSFERASES
N-GLYCOSYLATION
O-GLYCOSYLATION
PLANT PROTEIN GLYCOSYLATION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/141685
Ver los metadatos del registro completo
id |
CONICETDig_77d2014df98d456b77d31ba04f6fbc04 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/141685 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants CellsStrasser, RichardSeifert, GeorgDoblin, Monika S.Johnson, Kim L.Ruprecht, ColinPfrengle, FabianBacic, AntonyEstevez, Jose ManuelARABIDOPSISGLYCAN ARRAYSGLYCAN FUNCTIONSGLYCOSYL HYDROLASESGLYCOSYLTRANSFERASESN-GLYCOSYLATIONO-GLYCOSYLATIONPLANT PROTEIN GLYCOSYLATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized.Fil: Strasser, Richard. University of Natural Resources and Life Sciences; SuizaFil: Seifert, Georg. University of Natural Resources and Life Sciences; SuizaFil: Doblin, Monika S.. La Trobe University; AustraliaFil: Johnson, Kim L.. La Trobe University; AustraliaFil: Ruprecht, Colin. University of Natural Resources and Life Sciences; SuizaFil: Pfrengle, Fabian. University of Natural Resources and Life Sciences; SuizaFil: Bacic, Antony. La Trobe University; AustraliaFil: Estevez, Jose Manuel. 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; ArgentinaFrontiers Media2021-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/141685Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; et al.; Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells; Frontiers Media; Frontiers in Plant Science; 12; 2-2021; 1-191664-462XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2021.640919/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2021.640919info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:04:59Zoai:ri.conicet.gov.ar:11336/141685instacron: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:34982025-09-03 10:04:59.445CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells |
title |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells |
spellingShingle |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells Strasser, Richard ARABIDOPSIS GLYCAN ARRAYS GLYCAN FUNCTIONS GLYCOSYL HYDROLASES GLYCOSYLTRANSFERASES N-GLYCOSYLATION O-GLYCOSYLATION PLANT PROTEIN GLYCOSYLATION |
title_short |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells |
title_full |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells |
title_fullStr |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells |
title_full_unstemmed |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells |
title_sort |
Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells |
dc.creator.none.fl_str_mv |
Strasser, Richard Seifert, Georg Doblin, Monika S. Johnson, Kim L. Ruprecht, Colin Pfrengle, Fabian Bacic, Antony Estevez, Jose Manuel |
author |
Strasser, Richard |
author_facet |
Strasser, Richard Seifert, Georg Doblin, Monika S. Johnson, Kim L. Ruprecht, Colin Pfrengle, Fabian Bacic, Antony Estevez, Jose Manuel |
author_role |
author |
author2 |
Seifert, Georg Doblin, Monika S. Johnson, Kim L. Ruprecht, Colin Pfrengle, Fabian Bacic, Antony Estevez, Jose Manuel |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
ARABIDOPSIS GLYCAN ARRAYS GLYCAN FUNCTIONS GLYCOSYL HYDROLASES GLYCOSYLTRANSFERASES N-GLYCOSYLATION O-GLYCOSYLATION PLANT PROTEIN GLYCOSYLATION |
topic |
ARABIDOPSIS GLYCAN ARRAYS GLYCAN FUNCTIONS GLYCOSYL HYDROLASES GLYCOSYLTRANSFERASES N-GLYCOSYLATION O-GLYCOSYLATION PLANT PROTEIN GLYCOSYLATION |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized. Fil: Strasser, Richard. University of Natural Resources and Life Sciences; Suiza Fil: Seifert, Georg. University of Natural Resources and Life Sciences; Suiza Fil: Doblin, Monika S.. La Trobe University; Australia Fil: Johnson, Kim L.. La Trobe University; Australia Fil: Ruprecht, Colin. University of Natural Resources and Life Sciences; Suiza Fil: Pfrengle, Fabian. University of Natural Resources and Life Sciences; Suiza Fil: Bacic, Antony. La Trobe University; Australia Fil: Estevez, Jose Manuel. 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 |
description |
Glycosylation is a fundamental co-translational and/or post-translational modification process where an attachment of sugars onto either proteins or lipids can alter their biological function, subcellular location and modulate the development and physiology of an organism. Glycosylation is not a template driven process and as such produces a vastly larger array of glycan structures through combinatorial use of enzymes and of repeated common scaffolds and as a consequence it provides a huge expansion of both the proteome and lipidome. While the essential role of N- and O-glycan modifications on mammalian glycoproteins is already well documented, we are just starting to decode their biological functions in plants. Although significant advances have been made in plant glycobiology in the last decades, there are still key challenges impeding progress in the field and, as such, holistic modern high throughput approaches may help to address these conceptual gaps. In this snapshot, we present an update of the most common O- and N-glycan structures present on plant glycoproteins as well as (1) the plant glycosyltransferases (GTs) and glycosyl hydrolases (GHs) responsible for their biosynthesis; (2) a summary of microorganism-derived GHs characterized to cleave specific glycosidic linkages; (3) a summary of the available tools ranging from monoclonal antibodies (mAbs), lectins to chemical probes for the detection of specific sugar moieties within these complex macromolecules; (4) selected examples of N- and O-glycoproteins as well as in their related GTs to illustrate the complexity on their mode of action in plant cell growth and stress responses processes, and finally (5) we present the carbohydrate microarray approach that could revolutionize the way in which unknown plant GTs and GHs are identified and their specificities characterized. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-02 |
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/11336/141685 Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; et al.; Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells; Frontiers Media; Frontiers in Plant Science; 12; 2-2021; 1-19 1664-462X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/141685 |
identifier_str_mv |
Strasser, Richard; Seifert, Georg; Doblin, Monika S.; Johnson, Kim L.; Ruprecht, Colin; et al.; Cracking the “Sugar Code”: A Snapshot of N- and O-Glycosylation Pathways and Functions in Plants Cells; Frontiers Media; Frontiers in Plant Science; 12; 2-2021; 1-19 1664-462X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2021.640919/full info:eu-repo/semantics/altIdentifier/doi/10.3389/fpls.2021.640919 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Frontiers Media |
publisher.none.fl_str_mv |
Frontiers Media |
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 |
_version_ |
1842269884964143104 |
score |
13.13397 |