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Titolo:
Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system
Autore:
Furukawa, T; Ono, Y; Tsuchiya, H; Katayama, Y; Bang, ML; Labeit, D; Labeit, S; Inagaki, N; Gregorio, CC;
Indirizzi:
Univ Arizona, Dept Cell Biol & Anat, Tucson, AZ 85724 USA Univ Arizona Tucson AZ USA 85724 t Cell Biol & Anat, Tucson, AZ 85724 USA Akita Univ, Sch Med, Dept Physiol, Akita 0108543, Japan Akita Univ AkitaJapan 0108543 h Med, Dept Physiol, Akita 0108543, Japan Japan Sci & Technol Corp, CREST, Akita 0108543, Japan Japan Sci & Technol Corp Akita Japan 0108543 CREST, Akita 0108543, Japan Tokyo Med & Dent Univ, Med Res Inst, Dept Autonom Physiol, Tokyo 1010062, Japan Tokyo Med & Dent Univ Tokyo Japan 1010062 Physiol, Tokyo 1010062, Japan European Mol Biol Lab, D-69117 Heidelberg, Germany European Mol Biol Lab Heidelberg Germany D-69117 117 Heidelberg, Germany Univ Klinikum Mannheim, Inst Anasthesiol & Operat Intens Med, D-68135 Mannheim, Germany Univ Klinikum Mannheim Mannheim Germany D-68135 -68135 Mannheim, Germany Univ Arizona, Dept Mol & Cellular Biol, Tucson, AZ 85724 USA Univ ArizonaTucson AZ USA 85724 ol & Cellular Biol, Tucson, AZ 85724 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 4, volume: 313, anno: 2001,
pagine: 775 - 784
SICI:
0022-2836(20011102)313:4<775:SIOTPC>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
LANGE-NIELSEN-SYNDROME; LONG-QT SYNDROME; MECHANOELECTRICAL FEEDBACK; SKELETAL-MUSCLE; SODIUM-CHANNEL; CAUSE JERVELL; K+-CHANNEL; KINASE-C; Z-DISC; ISK;
Keywords:
minK; T-cap/telethonin; titin; Z-lines; T-tubules;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Gregorio, CC Univ Arizona, Dept Cell Biol & Anat, Tucson, AZ 85724 USA Univ Arizona Tucson AZ USA 85724 Anat, Tucson, AZ 85724 USA
Citazione:
T. Furukawa et al., "Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system", J MOL BIOL, 313(4), 2001, pp. 775-784

Abstract

Ion-channel beta -subunits are ancillary proteins that co-assemble with alpha -subunits to modulate gating kinetics and enhance stability of multimeric channel complexes. They provide binding sites for other regulatory proteins and a-re medically important as the targets of many pharmacological compounds. MinK is the beta -subunit of the slow activating component of the delayed rectifier potassium current (I-Ks) channel, and associates with the alpha -subunit, KvLQT1. We report here that minK specifically interacts with the sarcomeric Z-Line component, T-cap (also called telethonin). In vitrointeraction studies indicated that the cytoplasmic domain of minK specifically binds to the sixteen C-terminal residues of T-cap; these residues are sufficient for its interaction with minK. Consistent with our in vitro studies, immunofluorescence staining followedby confocal analysis revealed that both minK and T-cap are localized within the Z-line region in cardiac muscle. Striated staining of minK was observed in non-washed, membrane-intact cardiac myofibrils, but not in well-washed, membrane-removed cardiac myofibrils, suggesting that minK localizes on T-tubular membranes surrounding the Z-line in the inner ventricular myocardium. Together with our previous data on the colocalization and interaction of T-cap with the N-terminus of the giant protein titin in the periphery of theZ-line, these data suggest that T-cap functions as an adapter protein to link together myofibrillar components with the membranous beta -subunit of the I-Ks channel. We speculate that this interaction may contribute to a stretch-dependent regulation of potassium flux in cardiac muscle, providing a "mechano-electrical feedback" system. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 11:23:49