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dc.contributor.authorAbeijon, Claudia
dc.contributor.authorYanagisawa, Ken
dc.contributor.authorMandon, Elisabet C.
dc.contributor.authorHausler, Alex
dc.contributor.authorMoremen, Kelley W.
dc.contributor.authorHirschberg, Carlos B.
dc.contributor.authorRobbins, Phillips W.
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:55:01Z
dc.date.available2022-08-23T16:55:01Z
dc.date.issued1993-07-01
dc.date.submitted2008-10-31
dc.identifier.citationJ Cell Biol. 1993 Jul;122(2):307-23.
dc.identifier.issn0021-9525 (Print)
dc.identifier.pmid8391537
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42628
dc.description.abstractCurrent models for nucleotide sugar use in the Golgi apparatus predict a critical role for the lumenal nucleoside diphosphatase. After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol. To test this model, we cloned the gene for the S. cerevisiae guanosine diphosphatase and constructed a null mutation. This mutation should reduce the concentrations of GDP-mannose and GMP and increase the concentration of GDP in the Golgi lumen. The alterations should in turn decrease mannosylation of proteins and lipids in this compartment. In fact, we found a partial block in O- and N-glycosylation of proteins such as chitinase and carboxypeptidase Y and underglycosylation of invertase. In addition, mannosylinositolphosphorylceramide levels were drastically reduced.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=8391537&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectAmino Acid Sequence
dc.subjectBase Sequence
dc.subjectCarboxypeptidases
dc.subjectCell Wall
dc.subjectCeramides
dc.subjectChitinase
dc.subjectCloning, Molecular
dc.subjectGenes, Fungal
dc.subjectGlycoside Hydrolases
dc.subjectGlycosylation
dc.subjectGolgi Apparatus
dc.subjectMannose
dc.subjectMolecular Sequence Data
dc.subjectMutation
dc.subjectProteins
dc.subjectPyrophosphatases
dc.subjectSaccharomyces cerevisiae
dc.subjectdevelopment
dc.subjectSaccharomyces cerevisiae Proteins
dc.subjectbeta-Fructofuranosidase
dc.subjectBiochemistry
dc.subjectCell Biology
dc.subjectMolecular Biology
dc.titleGuanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae
dc.typeArticle
dc.source.journaltitleThe Journal of cell biology
dc.source.volume122
dc.source.issue2
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1958&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/959
dc.identifier.contextkey659140
refterms.dateFOA2022-08-23T16:55:02Z
html.description.abstract<p>Current models for nucleotide sugar use in the Golgi apparatus predict a critical role for the lumenal nucleoside diphosphatase. After transfer of sugars to endogenous macromolecular acceptors, the enzyme converts nucleoside diphosphates to nucleoside monophosphates which in turn exit the Golgi lumen in a coupled antiporter reaction, allowing entry of additional nucleotide sugar from the cytosol. To test this model, we cloned the gene for the S. cerevisiae guanosine diphosphatase and constructed a null mutation. This mutation should reduce the concentrations of GDP-mannose and GMP and increase the concentration of GDP in the Golgi lumen. The alterations should in turn decrease mannosylation of proteins and lipids in this compartment. In fact, we found a partial block in O- and N-glycosylation of proteins such as chitinase and carboxypeptidase Y and underglycosylation of invertase. In addition, mannosylinositolphosphorylceramide levels were drastically reduced.</p>
dc.identifier.submissionpathoapubs/959
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology
dc.source.pages307-23


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