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Titolo:
Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase inrabbit fast-twitch muscle sarcoplasmic reticulum
Autore:
Colpo, P; Nori, A; Sacchetto, R; Damiani, E; Margreth, A;
Indirizzi:
Univ Padua, Dept Expt Biomed Sci, NRC Unit Muscle Biol & Physiopathol, I-35121 Padua, Italy Univ Padua Padua Italy I-35121 Biol & Physiopathol, I-35121 Padua, Italy
Titolo Testata:
MOLECULAR AND CELLULAR BIOCHEMISTRY
fascicolo: 1-2, volume: 223, anno: 2001,
pagine: 139 - 145
SICI:
0300-8177(200107)223:1-2<139:POTTCD>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
SKELETAL RYANODINE RECEPTOR; RICH CA2+-BINDING PROTEIN; TERMINAL CISTERNAE; CA2+-RELEASE CHANNEL; GLYCOPROTEIN TRIADIN; JUNCTIONAL-MEMBRANE; CALSEQUESTRIN; MECHANISM; RELEASE;
Keywords:
Ca2+-release channel; calmodulin protein kinase; sarcoplasmic reticulum; triadin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Margreth, A Univ Padua, Dept Expt Biomed Sci, NRC Unit Muscle Biol & Physiopathol, Viale Giuseppe Colombo 3, I-35121 Padua, Italy Univ Padua Viale Giuseppe Colombo 3 Padua Italy I-35121 Italy
Citazione:
P. Colpo et al., "Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase inrabbit fast-twitch muscle sarcoplasmic reticulum", MOL C BIOCH, 223(1-2), 2001, pp. 139-145

Abstract

Skeletal muscle triadin is a sarcoplasmic reticulum (SR) membrane protein that had been shown to interact structurally and functionally at the cytoplasmic domain (amino acid residues 1-47) with the ryanodine receptor (RyR1),and to undergo phosphorylation by endogenous calmodulin protein kinase (CaM K II) in isolated terminal cisternae from rabbit fast-twitch muscle. Herewe show that triadin cytoplasmic domain expressed as glutathione-S-transferase fusion protein, is a substrate of the protein kinase. This finding is corroborated by identification of a specific consensus sequence in the deduced amino sequence between residue 34 and 37 of triadin. Confirming the regulatory features of CaM K II, we show the phosphorylation of triadin cytoplasmic segment by the kinase, when converted to the autonomous form. We propose that triadin modulates RyR1 in a phosphorylation-dependent manner.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 08:24:42