Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor
Autore:
Groh, S; Marty, I; Ottolia, M; Prestipino, G; Chapel, A; Villaz, M; Ronjat, M;
Indirizzi:
CEA, DBMS, Lab Canaux Ion & Signalisat, F-38054 Grenoble, France CEA Grenoble France F-38054 x Ion & Signalisat, F-38054 Grenoble, France CNR, Ist Cibernet & Biofis, I-16149 Genoa, Italy CNR Genoa Italy I-16149CNR, Ist Cibernet & Biofis, I-16149 Genoa, Italy CEA, DBMS, Lab Chim Prot, F-38054 Grenoble, France CEA Grenoble France F-38054 BMS, Lab Chim Prot, F-38054 Grenoble, France
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 18, volume: 274, anno: 1999,
pagine: 12278 - 12283
SICI:
0021-9258(19990430)274:18<12278:FIOTCD>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
JUNCTIONAL SARCOPLASMIC-RETICULUM; CALCIUM-RELEASE CHANNEL; CA2+ RELEASE; DIHYDROPYRIDINE RECEPTOR; GLYCOPROTEIN TRIADIN; CA-2+ RELEASE; MUSCLE; CALSEQUESTRIN; VESICLES; PROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Ronjat, M CEA,rance, Lab Canaux Ion & Signalisat, 17 Rue Martyrs, F-38054 Grenoble, F CEA 17 Rue Martyrs Grenoble France F-38054 F-38054 Grenoble, F
Citazione:
S. Groh et al., "Functional interaction of the cytoplasmic domain of triadin with the skeletal ryanodine receptor", J BIOL CHEM, 274(18), 1999, pp. 12278-12283

Abstract

Triadin has been shown to co-localize with the ryanodine receptor in the sarcoplasmic reticulum membrane. We show that immunoprecipitation of solubilized sarcoplasmic reticulum membrane with antibodies directed against triadin or ryanodine receptor, leads to the coimmunoprecipitation of ryanodine receptor and triadin, We then investigated the functional importance of the cytoplasmic domain of triadin (residues 1-47) in the control of Ca2+ release from sarcoplasmic reticulum, We show that antibodies directed against a synthetic peptide encompassing residues 2-17, induce a decrease in the rate of Ca2+ release from sarcoplasmic reticulum vesicles as well as a decrease in the open probability of the ryanodine receptor Ca2+ channel incorporatedin lipid bilayers, Using surface plasmon resonance spectroscopy, we defined a discrete domain (residues 18-46) of the cytoplasmic part of triadin interacting with the purified ryanodine receptor. This interaction is optimal at low Ca2+ concentration (up to pCa 5) and inhibited by increasing calciumconcentration (IC50 of 300 mu M). The direct molecular interaction of thistriadin domain with the ryanodine receptor was confirmed by overlay assay and shown to induce the inhibition of the Ca2+ channel activity of purifiedRyR in bilayer, We propose that this interaction plays a critical role in the control, by triadin, of the Ca2+ channel behavior of the ryanodine receptor and therefore may represent an important step in the regulation process of excitation-contraction coupling in skeletal muscle.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 05:30:04