Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation
- Autores
- D'Alessio, Cecilia; Caramelo, Julio Javier; Parodi, Armando José A.
- Año de publicación
- 2005
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- It is accepted that glycosyltransferase-generated nucleoside diphosphates are converted to monophosphates in the secretory pathway by nucleoside diphosphatases (NDPases) to provide substrates for antiport transport systems by which entrance of nucleotide sugars from the cytosol into the lumen is coupled to exit of nucleoside monophosphates. Working with Saccharomyces cerevisiae mutants affected in anterograde and/or retrograde endoplasmic reticulum (ER)-Golgi vesicular traffic and/or defective in one or both secretory pathway (Golgi) NDPases, we show that UDP-Glc: glycoprotein glucosyltransferase-mediated glucosylation is not dependent on the presence of NDPases or on ER-Golgi vesicular traffic and that GDP-Man-dependent N- and O-mannosylations are reduced but not abolished in the absence of NDPases in the secretory pathway. Further, the absence of the main Man-1-P transferase (a Golgi GMP-generating enzyme) does not modify the limited mannosylation observed in the absence of NDPases. Based on these results and on available additional information, we suggest that in the absence of NDPases, the already characterized nucleotide sugar transporters allow entrance of nucleotide sugars into the luminal compartments and that resulting nucleoside diphosphates exit to the cytosol by a still unknown mechanism. Further, an unexpected side result suggests that formation of Ser/Thr-Man(2) may occur in the ER and not exclusively in the Golgi.
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
Fil: 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
Fil: 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; Argentina - Materia
-
NDPases
ER-GOLGI VESICULAR TRAFFIC
GLUCOSYLTRANSFERASE
YEAST - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/41568
Ver los metadatos del registro completo
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Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein GlycosylationD'Alessio, CeciliaCaramelo, Julio JavierParodi, Armando José A.NDPasesER-GOLGI VESICULAR TRAFFICGLUCOSYLTRANSFERASEYEASThttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1It is accepted that glycosyltransferase-generated nucleoside diphosphates are converted to monophosphates in the secretory pathway by nucleoside diphosphatases (NDPases) to provide substrates for antiport transport systems by which entrance of nucleotide sugars from the cytosol into the lumen is coupled to exit of nucleoside monophosphates. Working with Saccharomyces cerevisiae mutants affected in anterograde and/or retrograde endoplasmic reticulum (ER)-Golgi vesicular traffic and/or defective in one or both secretory pathway (Golgi) NDPases, we show that UDP-Glc: glycoprotein glucosyltransferase-mediated glucosylation is not dependent on the presence of NDPases or on ER-Golgi vesicular traffic and that GDP-Man-dependent N- and O-mannosylations are reduced but not abolished in the absence of NDPases in the secretory pathway. Further, the absence of the main Man-1-P transferase (a Golgi GMP-generating enzyme) does not modify the limited mannosylation observed in the absence of NDPases. Based on these results and on available additional information, we suggest that in the absence of NDPases, the already characterized nucleotide sugar transporters allow entrance of nucleotide sugars into the luminal compartments and that resulting nucleoside diphosphates exit to the cytosol by a still unknown mechanism. Further, an unexpected side result suggests that formation of Ser/Thr-Man(2) may occur in the ER and not exclusively in the Golgi.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; 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; 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; ArgentinaAmerican Society for Biochemistry and Molecular Biology2005-12info: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/11336/41568D'Alessio, Cecilia; Caramelo, Julio Javier; Parodi, Armando José A.; Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 280; 49; 12-2005; 40417-404270021-92581083-351XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/280/49/40417.longinfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M503149200info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:04:09Zoai:ri.conicet.gov.ar:11336/41568instacron: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:34982025-10-22 12:04:09.436CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation |
| title |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation |
| spellingShingle |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation D'Alessio, Cecilia NDPases ER-GOLGI VESICULAR TRAFFIC GLUCOSYLTRANSFERASE YEAST |
| title_short |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation |
| title_full |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation |
| title_fullStr |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation |
| title_full_unstemmed |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation |
| title_sort |
Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation |
| dc.creator.none.fl_str_mv |
D'Alessio, Cecilia Caramelo, Julio Javier Parodi, Armando José A. |
| author |
D'Alessio, Cecilia |
| author_facet |
D'Alessio, Cecilia Caramelo, Julio Javier Parodi, Armando José A. |
| author_role |
author |
| author2 |
Caramelo, Julio Javier Parodi, Armando José A. |
| author2_role |
author author |
| dc.subject.none.fl_str_mv |
NDPases ER-GOLGI VESICULAR TRAFFIC GLUCOSYLTRANSFERASE YEAST |
| topic |
NDPases ER-GOLGI VESICULAR TRAFFIC GLUCOSYLTRANSFERASE 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 |
It is accepted that glycosyltransferase-generated nucleoside diphosphates are converted to monophosphates in the secretory pathway by nucleoside diphosphatases (NDPases) to provide substrates for antiport transport systems by which entrance of nucleotide sugars from the cytosol into the lumen is coupled to exit of nucleoside monophosphates. Working with Saccharomyces cerevisiae mutants affected in anterograde and/or retrograde endoplasmic reticulum (ER)-Golgi vesicular traffic and/or defective in one or both secretory pathway (Golgi) NDPases, we show that UDP-Glc: glycoprotein glucosyltransferase-mediated glucosylation is not dependent on the presence of NDPases or on ER-Golgi vesicular traffic and that GDP-Man-dependent N- and O-mannosylations are reduced but not abolished in the absence of NDPases in the secretory pathway. Further, the absence of the main Man-1-P transferase (a Golgi GMP-generating enzyme) does not modify the limited mannosylation observed in the absence of NDPases. Based on these results and on available additional information, we suggest that in the absence of NDPases, the already characterized nucleotide sugar transporters allow entrance of nucleotide sugars into the luminal compartments and that resulting nucleoside diphosphates exit to the cytosol by a still unknown mechanism. Further, an unexpected side result suggests that formation of Ser/Thr-Man(2) may occur in the ER and not exclusively in the Golgi. 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 Fil: 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 Fil: 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; Argentina |
| description |
It is accepted that glycosyltransferase-generated nucleoside diphosphates are converted to monophosphates in the secretory pathway by nucleoside diphosphatases (NDPases) to provide substrates for antiport transport systems by which entrance of nucleotide sugars from the cytosol into the lumen is coupled to exit of nucleoside monophosphates. Working with Saccharomyces cerevisiae mutants affected in anterograde and/or retrograde endoplasmic reticulum (ER)-Golgi vesicular traffic and/or defective in one or both secretory pathway (Golgi) NDPases, we show that UDP-Glc: glycoprotein glucosyltransferase-mediated glucosylation is not dependent on the presence of NDPases or on ER-Golgi vesicular traffic and that GDP-Man-dependent N- and O-mannosylations are reduced but not abolished in the absence of NDPases in the secretory pathway. Further, the absence of the main Man-1-P transferase (a Golgi GMP-generating enzyme) does not modify the limited mannosylation observed in the absence of NDPases. Based on these results and on available additional information, we suggest that in the absence of NDPases, the already characterized nucleotide sugar transporters allow entrance of nucleotide sugars into the luminal compartments and that resulting nucleoside diphosphates exit to the cytosol by a still unknown mechanism. Further, an unexpected side result suggests that formation of Ser/Thr-Man(2) may occur in the ER and not exclusively in the Golgi. |
| publishDate |
2005 |
| dc.date.none.fl_str_mv |
2005-12 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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http://hdl.handle.net/11336/41568 D'Alessio, Cecilia; Caramelo, Julio Javier; Parodi, Armando José A.; Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 280; 49; 12-2005; 40417-40427 0021-9258 1083-351X CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/41568 |
| identifier_str_mv |
D'Alessio, Cecilia; Caramelo, Julio Javier; Parodi, Armando José A.; Absence of Nucleoside Diphosphatase Activities in the Yeast Secretory Pathway Does Not Abolish Nucleotide Sugar-dependent Protein Glycosylation; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 280; 49; 12-2005; 40417-40427 0021-9258 1083-351X CONICET Digital CONICET |
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eng |
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eng |
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info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/280/49/40417.long info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M503149200 |
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American Society for Biochemistry and Molecular Biology |
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American Society for Biochemistry and Molecular Biology |
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