TRAPγ-CDG shows asymmetric glycosylation and an effect on processing of proteins required in higher organisms.
Child
Child, Preschool
Diarrhea
/ genetics
Endoplasmic Reticulum, Rough
/ genetics
Failure to Thrive
/ genetics
Female
Fetal Growth Retardation
/ genetics
Glycoproteins
/ biosynthesis
Glycosylation
Humans
Infant
Infant, Newborn
Lung Diseases
/ genetics
Male
Psychomotor Disorders
/ genetics
Tartrate-Resistant Acid Phosphatase
/ deficiency
CDG
TRAP
glycosylation
translocation
Journal
Journal of medical genetics
ISSN: 1468-6244
Titre abrégé: J Med Genet
Pays: England
ID NLM: 2985087R
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
received:
14
06
2019
revised:
19
03
2020
accepted:
21
03
2020
pubmed:
26
4
2020
medline:
4
9
2021
entrez:
26
4
2020
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32332102
pii: jmedgenet-2019-106279
doi: 10.1136/jmedgenet-2019-106279
doi:
Substances chimiques
Glycoproteins
0
ACP5 protein, human
EC 3.1.3.2
Tartrate-Resistant Acid Phosphatase
EC 3.1.3.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
213-216Informations de copyright
© Author(s) (or their employer(s)) 2021. No commercial re-use. See rights and permissions. Published by BMJ.
Déclaration de conflit d'intérêts
Competing interests: None declared.