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Titolo:
Localization and characterization of the calsequestrin-binding domain of triadin 1 - Evidence for a charged beta-strand in mediating the protein-protein interaction
Autore:
Kobayashi, YM; Alseikhan, BA; Jones, LR;
Indirizzi:
Indiana Univ, Sch Med, Krannert Inst Cardiol, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 ardiol, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Med, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 pt Med, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Biochem, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 iochem, Indianapolis, IN 46202 USA Indiana Univ, Sch Med, Dept Mol Biol, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 l Biol, Indianapolis, IN 46202 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 23, volume: 275, anno: 2000,
pagine: 17639 - 17646
SICI:
0021-9258(20000609)275:23<17639:LACOTC>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
JUNCTIONAL SARCOPLASMIC-RETICULUM; CANINE CARDIAC CALSEQUESTRIN; SKELETAL-MUSCLE; BIOCHEMICAL-CHARACTERIZATION; GLYCOPROTEIN TRIADIN; RYANODINE RECEPTOR; MOLECULAR-CLONING; VESICLES; PURIFICATION; ASSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Jones, LR Indiana Univ, Sch Med, Krannert Inst Cardiol, 1111 W 10th St, Indianapolis, IN 46202 USA Indiana Univ 1111 W 10th St Indianapolis IN USA 46202 46202 USA
Citazione:
Y.M. Kobayashi et al., "Localization and characterization of the calsequestrin-binding domain of triadin 1 - Evidence for a charged beta-strand in mediating the protein-protein interaction", J BIOL CHEM, 275(23), 2000, pp. 17639-17646

Abstract

Triadin is an integral membrane protein of the junctional sarcoplasmic reticulum that binds to the high capacity Ca2+-binding protein calsequestrin and anchors it to the ryanodine receptor. The lumenal domain of triadin contains multiple repeats of alternating lysine and glutamic acid residues, which have been defined as KEKE motifs and have been proposed to promote protein associations. Here we identified the specific residues of triadin responsible for binding to calsequestrin by mutational analysis of triadin 1, themajor cardiac isoform. A series of deletional fusion proteins of triadin 1was generated, and by using metabolically labeled calsequestrin in filter-overlay assays, the calsequestrin-binding domain of triadin 1 was localizedto a single HERE motif comprised of 25 amino acids. Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), LyS(212), GlU(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(221). Replacement of the odd-numbered residues within this motif by alanine had no effect on calsequestrin binding to triadin. The results suggest a model in which residues 210-224 of triadin form a beta-strand, with the even-numbered residues inthe strand interacting with charged residues of calsequestrin, stabilizinga "polar zipper" that links the two proteins together, This small, highly charged P-strand of triadin may tether calsequestrin to the junctional facemembrane, allowing calsequestrin to sequester Ca2+ in the vicinity of the ryanodine receptor during Ca2+ uptake and Ca2+ release.

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Documento generato il 14/07/20 alle ore 02:42:51