Related Experiment Video
Updated: Dec 23, 2025

Analysis of SCAP N-glycosylation and Trafficking in Human Cells
Published on: November 8, 2016
TRAPγ-CDG shows asymmetric glycosylation and an effect on processing of proteins required in higher organisms
Sabine Dittner-Moormann1, Charles Marques Lourenco2, Janine Reunert1
1Department of Pediatrics, Universitätsklinikum Münster, Münster, Germany.
Abstract:
Newly synthesised glycoproteins enter the rough endoplasmic reticulum through a translocation pore. The translocon associated protein (TRAP) complex is located close to the pore. In a patient with a homozygous start codon variant in TRAPγ (SSR3), absence of TRAPγ causes disruption of the TRAP complex, impairs protein translocation into the endoplasmic reticulum and affects transport, for example, into the brush-border membrane. Furthermore, we observed an unbalanced non-occupancy of N-glycosylation sites. The major clinical features are intrauterine growth retardation, facial dysmorphism, congenital diarrhoea, failure to thrive, pulmonary disease and severe psychomotor disability.
More Related Videos
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Glycosylation
Glycosylation occurs in...
Protein Folding Quality Check in the RER
GPCRs Regulate Adenylyl Cylase Activity
Export of Misfolded Proteins out of the ER
Leaky Scanning

