Title :

Newly characterized Golgi-localized family of proteins is involved in calcium and pH homeostasis in yeast and human cells

Author(s) :

Demaegd, Didier [Auteur]
Université Catholique de Louvain = Catholic University of Louvain [UCL]
Foulquier, Francois [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Colinet, Anne-Sophie [Auteur]
Université Catholique de Louvain = Catholic University of Louvain [UCL]
Gremillon, Louis [Auteur]
Université Catholique de Louvain = Catholic University of Louvain [UCL]
Legrand, Dominique [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Mariot, Pascal [Auteur]
Laboratoire de Physiologie Cellulaire - U 1003 [PHYCELL]
Peiter, Edgar [Auteur]
Martin-Luther-Universität Halle Wittenberg [MLU]
Van Schaftingen, Emile [Auteur]
Université Catholique de Louvain = Catholic University of Louvain [UCL]
Matthijs, Gert [Auteur]
Center for Human Genetics, University of Leuven School of Medicine
Morsomme, Pierre [Auteur]
Université Catholique de Louvain = Catholic University of Louvain [UCL]

Journal title :

Proceedings of the National Academy of Sciences of the United States of America

Abbreviated title :

Proc. Natl. Acad. Sci. U.S.A.

Volume number :

110

Pages :

6859-6864

Publication date :

2013-04-23

ISSN :

1091-6490

English keyword(s) :

Cell Fractionation
Calcium
Hydrogen
Humans
Gene Expression Regulation
Homeostasis
Blotting, Western
Saccharomycetales
Golgi Apparatus
Patch-Clamp Techniques
Flow Cytometry
Fluorescent Antibody Technique
Membrane Protein
RNA, Small Interfering
HeLa Cells
Antiporters
Hydrogen-Ion Concentration

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [en]

Defects in the human protein TMEM165 are known to cause a subtype of Congenital Disorders of Glycosylation. Transmembrane protein 165 (TMEM165) belongs to an uncharacterized family of membrane proteins called Uncharacterized ...
Show more >Defects in the human protein TMEM165 are known to cause a subtype of Congenital Disorders of Glycosylation. Transmembrane protein 165 (TMEM165) belongs to an uncharacterized family of membrane proteins called Uncharacterized Protein Family 0016, which are well conserved throughout evolution and share characteristics reminiscent of the cation/Ca(2+) exchanger superfamily. Gcr1 dependent translation factor 1 (Gdt1p), the budding yeast member of this family, contributes to Ca(2+) homeostasis via an uncharacterized Ca(2+) transport pathway localized in the Golgi apparatus. The gdt1Δ mutant was found to be sensitive to high concentrations of Ca(2+), and interestingly, this sensitivity was suppressed by expression of TMEM165, the human ortholog of Gdt1p, indicating conservation of function among the members of this family. Patch-clamp analyses on human cells indicated that TMEM165 expression is linked to Ca(2+) ion transport. Furthermore, defects in TMEM165 affected both Ca(2+) and pH homeostasis. Based on these results, we propose that Gdt1p and TMEM165 could be members of a unique family of Golgi-localized Ca(2+)/H(+) antiporters and that modification of the Golgi Ca(2+) and pH balance could explain the glycosylation defects observed in TMEM165-deficient patients.Show less >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

CNRS
Université de Lille
Inserm

Collections :

• Physiologie Cellulaire (PHYCELL) - U1003
• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Mécanismes moléculaires de la N-glycosylation et pathologies associées

Submission date :

2020-02-12T15:12:09Z
2021-03-04T14:34:48Z