RGD Reference Report - Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding. - Rat Genome Database

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Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding.

Authors: Fan, H  Meng, W  Kilian, C  Grams, S  Reutter, W 
Citation: Fan H, etal., Eur J Biochem. 1997 May 15;246(1):243-51.
RGD ID: 1626463
Pubmed: PMID:9210490   (View Abstract at PubMed)

Dipeptidyl peptidase IV (DPPIV, CD26) is an N-glycosylated type II plasma membrane protein. The primary structure of rat wild-type DPPIV contains eight potential N-glycosylation sites. To investigate the role of N-glycosylation in the function of DPPIV, three of its asparagine residues were separately converted to glutamine by site-directed mutagenesis. The resulting N-glycosylation mutants of rat DPPIV were studied in stable transfected Chinese hamster ovary cells. All three N-glycosylation mutants of DPPIV showed a reduced half-life, as well as differing degrees of inhibition of the processing of their N-glycans. Mutation of the first (Asn83-->Gln) or eighth (Asn686-->Gln) N-glycosylation site had only a small effect on its enzymatic activity, cell-surface expression and dimer formation, whereas the mutation of the sixth N-glycosylation site (Asn319-->Gln) abolished the enzymatic activity, eliminated cell-surface expression and prevented the dimerization of the DPPIV protein. The mutant [Gln319]DPPIV is retained in the cytoplasm and its degradation was drastically increased. Our data suggest that the N-glycosylation at Asn319 is involved in protein trafficking and correct protein folding.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
dipeptidyl-peptidase activity  IMP 1626463protein:Asn319Gln - mutation of the sixth out of eight potential N-glycosylation sitesRGD 
identical protein binding  IMP 1626463protein:Asn319Gln - mutation of the sixth out of eight potential N-glycosylation sitesRGD 

Objects Annotated

Genes (Rattus norvegicus)
Dpp4  (dipeptidylpeptidase 4)


Additional Information