Involvement of thapsigargin– and cyclopiazonic ...
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Article dans une revue scientifique
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Title :
Involvement of thapsigargin– and cyclopiazonic acid–sensitive pumps in the rescue of TMEM165‐associated glycosylation defects by Mn 2+
Author(s) :
Houdou, Marine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lebredonchel, Elodie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Garat, Anne [Auteur]
Impact de l'environnement chimique sur la santé humaine - ULR 4483 [IMPECS]
IMPact de l'Environnement Chimique sur la Santé humaine (IMPECS) - ULR 4483
Duvet, Sandrine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Legrand, Dominique [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Decool, Valérie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Klein, André [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ouzzine, Mohamed [Auteur]
Gasnier, Bruno [Auteur]
Potelle, Sven [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Foulquier, Francois [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lebredonchel, Elodie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Garat, Anne [Auteur]
Impact de l'environnement chimique sur la santé humaine - ULR 4483 [IMPECS]
IMPact de l'Environnement Chimique sur la Santé humaine (IMPECS) - ULR 4483
Duvet, Sandrine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Legrand, Dominique [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Decool, Valérie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Klein, André [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ouzzine, Mohamed [Auteur]
Gasnier, Bruno [Auteur]
Potelle, Sven [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Foulquier, Francois [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Journal title :
FASEB Journal
Abbreviated title :
FASEB j.
Volume number :
33
Pages :
2669-2679
Publisher :
Federation of American Society of Experimental Biology
Publication date :
2018-10-11
ISSN :
0892-6638
English keyword(s) :
Manganese homeostasis
Congenital Disorders of Glycosylation
TMEM165
Golgi apparatus
Congenital Disorders of Glycosylation
TMEM165
Golgi apparatus
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
Congenital disorders of glycosylation are severe inherited diseases in which aberrant protein glycosylation is a hallmark. Transmembrane protein 165 (TMEM165) is a novel Golgi transmembrane protein involved in type II ...
Show more >Congenital disorders of glycosylation are severe inherited diseases in which aberrant protein glycosylation is a hallmark. Transmembrane protein 165 (TMEM165) is a novel Golgi transmembrane protein involved in type II congenital disorders of glycosylation. Although its biologic function is still a controversial issue, we have demonstrated that the Golgi glycosylation defect due to TMEM165 deficiency resulted from a Golgi Mn2+ homeostasis defect. The goal of this study was to delineate the cellular pathway by which extracellular Mn2+ rescues N‐glycosylation in TMEM165 knockout (KO) cells. We first demonstrated that after extracellular exposure, Mn2+ uptake by HEK293 cells at the plasma membrane did not rely on endocytosis but was likely done by plasma membrane transporters. Second, we showed that the secretory pathway Ca2+‐ATPase 1, also known to mediate the influx of cytosolic Mn2+ into the lumen of the Golgi apparatus, is not crucial for the Mn2+‐induced rescue glycosylation of lysosomal‐associated membrane protein 2 (LAMP2). In contrast, our results demonstrate the involvement of cyclopiazonic acid—and thapsigargin (Tg)‐sensitive pumps in the rescue of TMEM165‐associated glycosylation defects by Mn2+. Interestingly, overexpression of sarco/endoplasmic reticulum Ca2+‐ATPase (SERCA) 2b isoform in TMEM165 KO cells partially rescues the observed LAMP2 glycosylation defect. Overall, this study indicates that the rescue of Golgi N‐glycosylation defects in TMEM165 KO cells by extracellular Mn2+ involves the activity of Tg and cyclopiazonic acid–sensitive pumps, probably the SERCA pumps.—Houdou, M., Lebredonchel, E., Garat, A., Duvet, S., Legrand, D., Decool, V., Klein, A., Ouzzine, M., Gasnier, B., Potelle, S., Foulquier, F. Involvement of thapsigargin—and cyclopiazonic acid–sensitive pumps in the rescue of TMEM165‐associated glycosylation defects by Mn2+.Show less >
Show more >Congenital disorders of glycosylation are severe inherited diseases in which aberrant protein glycosylation is a hallmark. Transmembrane protein 165 (TMEM165) is a novel Golgi transmembrane protein involved in type II congenital disorders of glycosylation. Although its biologic function is still a controversial issue, we have demonstrated that the Golgi glycosylation defect due to TMEM165 deficiency resulted from a Golgi Mn2+ homeostasis defect. The goal of this study was to delineate the cellular pathway by which extracellular Mn2+ rescues N‐glycosylation in TMEM165 knockout (KO) cells. We first demonstrated that after extracellular exposure, Mn2+ uptake by HEK293 cells at the plasma membrane did not rely on endocytosis but was likely done by plasma membrane transporters. Second, we showed that the secretory pathway Ca2+‐ATPase 1, also known to mediate the influx of cytosolic Mn2+ into the lumen of the Golgi apparatus, is not crucial for the Mn2+‐induced rescue glycosylation of lysosomal‐associated membrane protein 2 (LAMP2). In contrast, our results demonstrate the involvement of cyclopiazonic acid—and thapsigargin (Tg)‐sensitive pumps in the rescue of TMEM165‐associated glycosylation defects by Mn2+. Interestingly, overexpression of sarco/endoplasmic reticulum Ca2+‐ATPase (SERCA) 2b isoform in TMEM165 KO cells partially rescues the observed LAMP2 glycosylation defect. Overall, this study indicates that the rescue of Golgi N‐glycosylation defects in TMEM165 KO cells by extracellular Mn2+ involves the activity of Tg and cyclopiazonic acid–sensitive pumps, probably the SERCA pumps.—Houdou, M., Lebredonchel, E., Garat, A., Duvet, S., Legrand, D., Decool, V., Klein, A., Ouzzine, M., Gasnier, B., Potelle, S., Foulquier, F. Involvement of thapsigargin—and cyclopiazonic acid–sensitive pumps in the rescue of TMEM165‐associated glycosylation defects by Mn2+.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Collections :
Research team(s) :
Mécanismes moléculaires de la N-glycosylation et pathologies associées
Submission date :
2020-12-18T13:32:48Z
2021-01-07T08:46:16Z
2024-02-23T09:11:51Z
2021-01-07T08:46:16Z
2024-02-23T09:11:51Z
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