Role of triadin in the organization of reticulum membrane at the muscle triad.

Anne Fourest-Lieuvin 1 John Rendu 2 Alexis Osseni 3 Karine Pernet-Gallay 3 Daniella Rossi 4 Sarah Oddoux 3 Julie Brocard 3 Vincenzo Sorrentino 4 Isabelle Marty 3 Julien Fauré 2, *
* Auteur correspondant
1 INSERM U836, équipe 4, Muscles et pathologies
BIG - Institut de Biosciences et de Biotechnologies de Grenoble (ex-IRTSV), GIN - Grenoble Institut des Neurosciences
2 INSERM U836, équipe 4, Muscles et pathologies
GIN - Grenoble Institut des Neurosciences, Biochimie et Génétique Moléculaire
3 INSERM U836, équipe 4, Muscles et pathologies
GIN - Grenoble Institut des Neurosciences
Abstract : The terminal cisternae represent one of the functional domains of the skeletal muscle sarcoplasmic reticulum (SR). They are closely apposed to plasma membrane invaginations, the T-tubules, with which they form structures called triads. In triads, the physical interaction between the T-tubule-anchored voltage-sensing channel DHPR and the SR calcium channel RyR1 is essential because it allows the depolarization-induced calcium release that triggers muscle contraction. This interaction between DHPR and RyR1 is based on the peculiar membrane structures of both T-tubules and SR terminal cisternae. However, little is known about the molecular mechanisms governing the formation of SR terminal cisternae. We have previously shown that ablation of triadins, a family of SR transmembrane proteins that interact with RyR1, induced skeletal muscle weakness in knockout mice as well as a modification of the shape of triads. Here we explore the intrinsic molecular properties of the longest triadin isoform Trisk 95. We show that when ectopically expressed, Trisk 95 can modulate reticulum membrane morphology. The membrane deformations induced by Trisk 95 are accompanied by modifications of the microtubule network organization. We show that multimerization of Trisk 95 by disulfide bridges, together with interaction with microtubules, are responsible for the ability of Trisk 95 to structure reticulum membrane. When domains responsible for these molecular properties are deleted, anchoring of Trisk 95 to the triads in muscle cells is strongly decreased, suggesting that oligomers of Trisk 95 and microtubules contribute to the organization of the SR terminal cisternae in a triad.
Type de document :
Article dans une revue
Journal of Cell Science, Company of Biologists, 2012, 125 (Pt 14), pp.3443-53. 〈10.1242/jcs.100958〉
Liste complète des métadonnées

Littérature citée [42 références]  Voir  Masquer  Télécharger

http://www.hal.inserm.fr/inserm-00763148
Contributeur : Nathalie Roux-Buisson <>
Soumis le : lundi 1 juillet 2013 - 07:00:17
Dernière modification le : vendredi 29 juin 2018 - 01:17:13
Document(s) archivé(s) le : mercredi 2 octobre 2013 - 02:30:12

Fichier

Fourest-Lieuvin_2012_Role_of_T...
Fichiers éditeurs autorisés sur une archive ouverte

Identifiants

Collections

CEA | U836 | UGA | CEA-DRF | BIG

Citation

Anne Fourest-Lieuvin, John Rendu, Alexis Osseni, Karine Pernet-Gallay, Daniella Rossi, et al.. Role of triadin in the organization of reticulum membrane at the muscle triad.. Journal of Cell Science, Company of Biologists, 2012, 125 (Pt 14), pp.3443-53. 〈10.1242/jcs.100958〉. 〈inserm-00763148〉

Partager

Métriques

Consultations de la notice

591

Téléchargements de fichiers

213