TRAPγ-CDG shows asymmetric glycosylation and an effect on processing of proteins required in higher organisms
TRAPγ-CDG shows asymmetric glycosylation and an effect on processing of proteins required in higher organisms
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DOI：
10.1136/jmedgenet-2019-106279
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发表时间：
2021-03-01
影响因子：
4
通讯作者：
Marquardt, Thorsten
中科院分区：
文献类型：
--
作者：
Dittner-Moormann, Sabine;Lourenco, Charles Marques;Marquardt, Thorsten
新合成的糖蛋白通过易位孔进入粗面内质网。转运子相关蛋白(TRAP)复合体位于毛孔附近。在具有TRAP伽马基因(SSR3)纯合子起始密码子变体的患者中，缺少TRAP伽马基因会导致TRAP复合体的破坏，损害蛋白质转位到内质网，并影响转运，例如进入刷状缘膜。此外，我们观察到N-糖基化位点的不平衡非占位。主要临床特征为胎儿宫内发育迟缓、面部畸形、先天性腹泻、发育迟缓、肺部疾病和严重的精神运动障碍。
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 TRAP gamma (SSR3), absence of TRAP gamma 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.