RT Journal Article
SR Electronic
T1 TRAPγ-CDG shows asymmetric glycosylation and an effect on processing of proteins required in higher organisms
JF Journal of Medical Genetics
JO J Med Genet
FD BMJ Publishing Group Ltd
SP 213
OP 216
DO 10.1136/jmedgenet-2019-106279
VO 58
IS 3
A1 Dittner-Moormann, Sabine
A1 Lourenco, Charles Marques
A1 Reunert, Janine
A1 Nishinakamura, Ryuichi
A1 Tanaka, Satomi S
A1 Werner, Claudius
A1 Debus, Volker
A1 Zimmer, Klaus-Peter
A1 Wetzel, Gabriele
A1 Naim, Hassan Y
A1 Wada, Yoshinao
A1 Rust, Stephan
A1 Marquardt, Thorsten
YR 2021
UL http://jmg.bmj.com/content/58/3/213.abstract
AB 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.