Mutations in TRAPPC11 are associated with ...
Document type :
Article dans une revue scientifique
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Title :
Mutations in TRAPPC11 are associated with a congenital disorder of glycosylation
Author(s) :
Matalonga, Leslie [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Bravo, Miren [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Serra-Peinado, Carla [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
García-Pelegrí, Elisabeth [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Ugarteburu, Olatz [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Vidal, Silvia [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Llambrich, Maria [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Quintana, Ester [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Fuster-Jorge, Pedro [Auteur]
Gonzalez-Bravo, Maria Nieves [Auteur]
Beltran, Sergi [Auteur]
Centro Nacional de Analisis Genomico [Barcelona] [CNAG]
Dopazo, Joaquin [Auteur]
Garcia-Garcia, Francisco [Auteur]
Foulquier, Francois [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Matthijs, Gert [Auteur]
Center for Human Genetics, University of Leuven School of Medicine
Mills, Philippa [Auteur]
Institute of Child Health [London]
Ribes, Antonia [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Egea, Gustavo [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Briones, Paz [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Tort, Frederic [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Girós, Marisa [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Bravo, Miren [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Serra-Peinado, Carla [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
García-Pelegrí, Elisabeth [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Ugarteburu, Olatz [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Vidal, Silvia [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Llambrich, Maria [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Quintana, Ester [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Fuster-Jorge, Pedro [Auteur]
Gonzalez-Bravo, Maria Nieves [Auteur]
Beltran, Sergi [Auteur]
Centro Nacional de Analisis Genomico [Barcelona] [CNAG]
Dopazo, Joaquin [Auteur]
Garcia-Garcia, Francisco [Auteur]
Foulquier, Francois [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Matthijs, Gert [Auteur]
Center for Human Genetics, University of Leuven School of Medicine
Mills, Philippa [Auteur]
Institute of Child Health [London]
Ribes, Antonia [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Egea, Gustavo [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Briones, Paz [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Tort, Frederic [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Girós, Marisa [Auteur]
Institut d'Investigacions Biomèdiques August Pi i Sunyer [IDIBAPS]
Journal title :
Human mutation
Abbreviated title :
Hum. Mutat.
Volume number :
38
Pages :
148-151
Publication date :
2017-02
ISSN :
1098-1004
English keyword(s) :
Brain
Humans
CDG
Abnormalities, Multiple
Male
Genotype
Endoplasmic Reticulum
Whole Genome Sequencing
Magnetic Resonance Imaging
Phenotype
Congenital Disorders of Glycosylation
Alleles
TRAPPC11
Golgi
Mutation
Amino Acid Substitution
vesicle trafficking
Vesicular Transport Proteins
Humans
CDG
Abnormalities, Multiple
Male
Genotype
Endoplasmic Reticulum
Whole Genome Sequencing
Magnetic Resonance Imaging
Phenotype
Congenital Disorders of Glycosylation
Alleles
TRAPPC11
Golgi
Mutation
Amino Acid Substitution
vesicle trafficking
Vesicular Transport Proteins
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
Mécanismes moléculaires de la N-glycosylation et pathologies associées
Submission date :
2020-02-12T15:11:57Z
2021-07-13T06:53:06Z
2021-07-13T06:53:06Z