Premium
Mutations in TRAPPC11 are associated with a congenital disorder of glycosylation
Author(s) -
Matalonga Leslie,
Bravo Miren,
SerraPeinado Carla,
GarcíaPelegrí Elisabeth,
Ugarteburu Olatz,
Vidal Silvia,
Llambrich Maria,
Quintana Ester,
FusterJorge Pedro,
GonzalezBravo Maria Nieves,
Beltran Sergi,
Dopazo Joaquin,
GarciaGarcia Francisco,
Foulquier François,
Matthijs Gert,
Mills Philippa,
Ribes Antonia,
Egea Gustavo,
Briones Paz,
Tort Frederic,
Girós Marisa
Publication year - 2017
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.23145
Subject(s) - glycosylation , endoplasmic reticulum , golgi apparatus , biology , microbiology and biotechnology , transport protein , vesicular transport protein , protein subunit , mutation , compartment (ship) , gene , genetics , vesicle , oceanography , membrane , geology
Congenital disorders of glycosylation (CDG) are a heterogeneous and rapidly growing group of diseases caused by abnormal glycosylation of proteins and/or lipids. Mutations in genes involved in the homeostasis of the endoplasmic reticulum (ER), the Golgi apparatus (GA), and the vesicular trafficking from the ER to the ER–Golgi intermediate compartment (ERGIC) have been found to be associated with CDG. Here, we report a patient with defects in both N‐ and O‐glycosylation combined with a delayed vesicular transport in the GA due to mutations in TRAPPC11 , a subunit of the TRAPPIII complex. TRAPPIII is implicated in the anterograde transport from the ER to the ERGIC as well as in the vesicle export from the GA. This report expands the spectrum of genetic alterations associated with CDG, providing new insights for the diagnosis and the understanding of the physiopathological mechanisms underlying glycosylation disorders.