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- Title
Distinct regions of triadin are required for targeting and retention at the junctional domain of the sarcoplasmic reticulum.
- Authors
ROSSI, Daniela; BENCINI, Cristina; MARITATI, Marina; BENINI, Francesca; LORENZINI, Stefania; PIERANTOZZI, Enrico; SCARCELLA, Angela Maria; PAOLINI, Cecilia; PROTASI, Feliciano; SORRENTINO, Vincenzo
- Abstract
Ca2+ release, which is necessary for muscle contraction, occurs at the j-SR (junctional domain of the sarcoplasmic reticulum). It requires the assembly of a large multiprotein complex containing the RyR (ryanodine receptor) and additional proteins, including triadin and calsequestrin. The signals which drive these proteins to the j-SR and howthey assemble to form this multiprotein complex are poorly understood. To address aspects of these questions we studied the localization, dynamic properties and molecular interactions of triadin. We identified three regions, named TR1 (targeting region 1), TR2 and TR3, that contribute to the localization of triadin at the j-SR. FRAP experiments showed that triadin is stably associated with the j-SR and that this association is mediated by TR3. Protein pull-down experiments indicated that TR3 contains binding sites for calsequestrin-1 and that triadin clustering can be enhanced by binding to calsequestrin-1. These findings were confirmed by FRET experiments. Interestingly, the stable association of triadin to the j-SRwas significantly decreased in myotubes from calsequestrin-1 knockout mice. Taken together, these results identify three regions in triadin thatmediate targeting to the j-SR and reveal a role for calsequestrin-1 in promoting the stable association of triadin to the multiprotein complex associated with RyR.
- Subjects
SARCOPLASMIC reticulum; RYANODINE receptors; PROTEINS; CALSEQUESTRIN; MOLECULAR interactions
- Publication
Biochemical Journal, 2014, Vol 458, Issue 2, p407
- ISSN
0264-6021
- Publication type
Article
- DOI
10.1042/BJ20130719