Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
ASSOCIATION OF TRIADIN WITH THE RYANODINE RECEPTOR AND CALSEQUESTRIN IN THE LUMEN OF THE SARCOPLASMIC-RETICULUM
Autore:
GUO W; CAMPBELL KP;
Indirizzi:
UNIV IOWA,COLL MED,HOWARD HUGHES MED INST,DEPT PHYS & BIOPHYS,400 EMRB IOWA CITY IA 52242 UNIV IOWA,COLL MED,HOWARD HUGHES MED INST,DEPT PHYS & BIOPHYS IOWA CITY IA 52242
Titolo Testata:
The Journal of biological chemistry
fascicolo: 16, volume: 270, anno: 1995,
pagine: 9027 - 9030
SICI:
0021-9258(1995)270:16<9027:AOTWTR>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALCIUM RELEASE CHANNEL; RABBIT SKELETAL-MUSCLE; 1,4-DIHYDROPYRIDINE RECEPTOR; BIOCHEMICAL-CHARACTERIZATION; DIHYDROPYRIDINE RECEPTORS; GLYCOPROTEIN TRIADIN; LOCALIZATION; PROTEIN; INVOLVEMENT; SUBUNITS;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
W. Guo e K.P. Campbell, "ASSOCIATION OF TRIADIN WITH THE RYANODINE RECEPTOR AND CALSEQUESTRIN IN THE LUMEN OF THE SARCOPLASMIC-RETICULUM", The Journal of biological chemistry, 270(16), 1995, pp. 9027-9030

Abstract

Triadin is a major membrane protein that is specifically localized inthe junctional sarcoplasmic reticulum of skeletal muscle and is thought to play an important role in muscle excitation-contraction coupling. In order to identify the proteins in the skeletal muscle that interact with triadin, the cytoplasmic and luminal domains of triadin were expressed as glutathione S-transferase fusion proteins and immobilized to glutathione-Sepharose to form affinity columns. Using these affinity columns, we find that triadin binds specifically to the ryanodine receptor/Ca2+ release channel and the Ca2+-binding protein calsequestrinfrom CHAPS (3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonicacid)-solubilized skeletal muscle homogenates. The luminal but not the cytoplasmic domain of triadin-glutathione S-transferase fusion protein binds [H-3]ryanodine receptor, whereas neither the cytoplasmic nor the luminal portion of triadin binds [H-3]PN-200-100-labeled dihydropyridine receptor, In addition, the luminal domain of triadin interacts with calsequestrin in a Ca2+-dependent manner and is capable of inhibiting the reassociation of calsequestrin to the junctional face membrane. These results suggest that triadin is the previously unidentified transmembrane protein that anchors calsequestrin to the junctional region of the sarcoplasmic reticulum, and is involved in the functional coupling between calsequestrin and the ryanodine receptor/Ca2+ release channel.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 21:27:58