메뉴 건너뛰기




Volumn 7, Issue 8, 2012, Pages

A skeletal muscle ryanodine receptor interaction domain in triadin

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; RYANODINE RECEPTOR; TRIADIN PROTEIN; TRISK 95 PROTEIN; UNCLASSIFIED DRUG;

EID: 84865288571     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0043817     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 0025718478 scopus 로고
    • Localization and partial characterization of the oligomeric disulfide-linked molecular weight 95,000 protein (triadin) which binds the ryanodine and dihydropyridine receptors in skeletal muscle triadic vesicles
    • Caswell AH, Brandt NR, Brunschwig JP, Purkerson S, (1991) Localization and partial characterization of the oligomeric disulfide-linked molecular weight 95,000 protein (triadin) which binds the ryanodine and dihydropyridine receptors in skeletal muscle triadic vesicles. Biochem 30: 7507-7513.
    • (1991) Biochem , vol.30 , pp. 7507-7513
    • Caswell, A.H.1    Brandt, N.R.2    Brunschwig, J.P.3    Purkerson, S.4
  • 2
    • 0027302407 scopus 로고
    • Biochemical characterization of ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin)
    • Knudson CM, Stang KK, Jorgensen AO, Campbell KP, (1993a) Biochemical characterization of ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin). J Biol Chem 268: 12637-12645.
    • (1993) J Biol Chem , vol.268 , pp. 12637-12645
    • Knudson, C.M.1    Stang, K.K.2    Jorgensen, A.O.3    Campbell, K.P.4
  • 3
    • 0027242015 scopus 로고
    • Primary structure and topological analysis of a skeletal muscle-specific junctional sarcoplasmic reticulum glycoprotein (triadin)
    • Knudson CM, Stang KK, Moomaw CR, Slaughter CA, Campbell KP, (1993b) Primary structure and topological analysis of a skeletal muscle-specific junctional sarcoplasmic reticulum glycoprotein (triadin). J Biol Chem 268: 12646-12654.
    • (1993) J Biol Chem , vol.268 , pp. 12646-12654
    • Knudson, C.M.1    Stang, K.K.2    Moomaw, C.R.3    Slaughter, C.A.4    Campbell, K.P.5
  • 5
    • 23344454364 scopus 로고    scopus 로고
    • Triadins are not triad specific proteins: Two new skeletal muscle triadins possibly involved in the architecture of sarcoplasmic reticulum
    • Vassilopoulos S, Thevenon D, Smida Rezgui S, Brocard J, Chapel A, et al. (2005) Triadins are not triad specific proteins: Two new skeletal muscle triadins possibly involved in the architecture of sarcoplasmic reticulum. J Biol Chem 280: 28601-28609.
    • (2005) J Biol Chem , vol.280 , pp. 28601-28609
    • Vassilopoulos, S.1    Thevenon, D.2    Smida Rezgui, S.3    Brocard, J.4    Chapel, A.5
  • 6
    • 0033214441 scopus 로고    scopus 로고
    • Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium
    • Kobayashi YM, Jones LR, (1999) Identification of triadin 1 as the predominant triadin isoform expressed in mammalian myocardium. Journal of Biological Chemistry 274: 28660-28668.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 28660-28668
    • Kobayashi, Y.M.1    Jones, L.R.2
  • 7
    • 0030039603 scopus 로고    scopus 로고
    • Biochemical characterization and molecular cloning of cardiac triadin
    • Guo W, Jorgensen AO, Jones LR, Campbell KP, (1996) Biochemical characterization and molecular cloning of cardiac triadin. J Biol Chem 271: 458-465.
    • (1996) J Biol Chem , vol.271 , pp. 458-465
    • Guo, W.1    Jorgensen, A.O.2    Jones, L.R.3    Campbell, K.P.4
  • 9
    • 17844372494 scopus 로고    scopus 로고
    • Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation
    • Beard NA, Casarotto MG, Wei L, Varsányi M, Laver DR, et al. (2005) Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation. Biophys J 88: 3444-3454.
    • (2005) Biophys J , vol.88 , pp. 3444-3454
    • Beard, N.A.1    Casarotto, M.G.2    Wei, L.3    Varsányi, M.4    Laver, D.R.5
  • 10
    • 0141448292 scopus 로고    scopus 로고
    • Regulation of the cardiac ryanodine receptor channel by luminal Ca2+ involves luminal Ca2+ sensing sites
    • Gyorke I, Gyorke S, (1998) Regulation of the cardiac ryanodine receptor channel by luminal Ca2+ involves luminal Ca2+ sensing sites. Biophys J 75: 2801-2810.
    • (1998) Biophys J , vol.75 , pp. 2801-2810
    • Gyorke, I.1    Gyorke, S.2
  • 11
    • 33746839364 scopus 로고    scopus 로고
    • The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors
    • Wei L, Varsanyi M, Dulhunty AF, Beard NA, (2006) The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors. Biophys J 91: 1288-1301.
    • (2006) Biophys J , vol.91 , pp. 1288-1301
    • Wei, L.1    Varsanyi, M.2    Dulhunty, A.F.3    Beard, N.A.4
  • 12
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • Zhang L, Kelley J, Schmeisser G, Kobayashi YM, Jones LR, (1997) Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J Biol Chem 272: 23389-23397.
    • (1997) J Biol Chem , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3    Kobayashi, Y.M.4    Jones, L.R.5
  • 13
    • 67650464941 scopus 로고    scopus 로고
    • Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin
    • Wei L, Gallant EM, Dulhunty AF, Beard NA, (2009) Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin. Int J Biochem Cell Biol 41: 2214-2224.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 2214-2224
    • Wei, L.1    Gallant, E.M.2    Dulhunty, A.F.3    Beard, N.A.4
  • 14
    • 0034624196 scopus 로고    scopus 로고
    • The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin
    • Shin DW, Ma J, Kim DH, (2000) The asp-rich region at the carboxyl-terminus of calsequestrin binds to Ca(2+) and interacts with triadin. FEBS Lett 486: 178-182.
    • (2000) FEBS Lett , vol.486 , pp. 178-182
    • Shin, D.W.1    Ma, J.2    Kim, D.H.3
  • 15
    • 0028906807 scopus 로고
    • Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum
    • Guo W, Campbell KP, (1995) Association of triadin with the ryanodine receptor and calsequestrin in the lumen of the sarcoplasmic reticulum. J Biol Chem 270: 9027-9030.
    • (1995) J Biol Chem , vol.270 , pp. 9027-9030
    • Guo, W.1    Campbell, K.P.2
  • 16
    • 50249174570 scopus 로고    scopus 로고
    • Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding capacity and promotes its association with junctin
    • Beard NA, Wei L, Cheung SN, Kimura T, Varsanyi M, et al. (2008) Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding capacity and promotes its association with junctin. Cell Calcium 44: 363-373.
    • (2008) Cell Calcium , vol.44 , pp. 363-373
    • Beard, N.A.1    Wei, L.2    Cheung, S.N.3    Kimura, T.4    Varsanyi, M.5
  • 17
    • 1342282949 scopus 로고    scopus 로고
    • Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin
    • Lee JM, Rho SH, Shin DW, Cho C, Park WJ, et al. (2004) Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin. J Biol Chem 279: 6994-7000.
    • (2004) J Biol Chem , vol.279 , pp. 6994-7000
    • Lee, J.M.1    Rho, S.H.2    Shin, D.W.3    Cho, C.4    Park, W.J.5
  • 18
    • 34748893872 scopus 로고    scopus 로고
    • Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling
    • Goonasekera SA, Beard NA, Groom L, Kimura T, Lyfenko AD, et al. (2007) Triadin binding to the C-terminal luminal loop of the ryanodine receptor is important for skeletal muscle excitation contraction coupling. J Gen Physiol 130: 365-378.
    • (2007) J Gen Physiol , vol.130 , pp. 365-378
    • Goonasekera, S.A.1    Beard, N.A.2    Groom, L.3    Kimura, T.4    Lyfenko, A.D.5
  • 19
    • 58149110941 scopus 로고    scopus 로고
    • Altered stored calcium release in skeletal myotubes deficient of triadin and junctin
    • Wang Y, Li X, Duan H, Fulton TR, Eu JP, et al. (2009) Altered stored calcium release in skeletal myotubes deficient of triadin and junctin. Cell Calcium 45: 29-37.
    • (2009) Cell Calcium , vol.45 , pp. 29-37
    • Wang, Y.1    Li, X.2    Duan, H.3    Fulton, T.R.4    Eu, J.P.5
  • 21
    • 38049173391 scopus 로고    scopus 로고
    • Triadins modulate intracellular Ca(2+) homeostasis but are not essential for excitation-contraction coupling in skeletal muscle
    • Shen X, Franzini-Armstrong C, Lopez JR, Jones LR, Kobayashi YM, et al. (2007) Triadins modulate intracellular Ca(2+) homeostasis but are not essential for excitation-contraction coupling in skeletal muscle. J Biol Chem 282: 37864-37874.
    • (2007) J Biol Chem , vol.282 , pp. 37864-37874
    • Shen, X.1    Franzini-Armstrong, C.2    Lopez, J.R.3    Jones, L.R.4    Kobayashi, Y.M.5
  • 22
    • 0033524473 scopus 로고    scopus 로고
    • Location of ryanodine receptor binding site on skeletal muscle triadin
    • Caswell AH, Motoike HK, Fan H, Brandt NR, (1999) Location of ryanodine receptor binding site on skeletal muscle triadin. Biochem 38: 90-97.
    • (1999) Biochem , vol.38 , pp. 90-97
    • Caswell, A.H.1    Motoike, H.K.2    Fan, H.3    Brandt, N.R.4
  • 23
    • 0035955601 scopus 로고    scopus 로고
    • Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum
    • Lee HG, Kang H, Kim DH, Park WJ, (2001) Interaction of HRC (histidine-rich Ca(2+)-binding protein) and triadin in the lumen of sarcoplasmic reticulum. J Biol Chem 276: 39533-39538.
    • (2001) J Biol Chem , vol.276 , pp. 39533-39538
    • Lee, H.G.1    Kang, H.2    Kim, D.H.3    Park, W.J.4
  • 24
    • 67349175061 scopus 로고    scopus 로고
    • Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle
    • Wei L, Hanna AD, Beard NA, Dulhunty AF, (2009) Unique isoform-specific properties of calsequestrin in the heart and skeletal muscle. Cell Calcium 45: 474-484.
    • (2009) Cell Calcium , vol.45 , pp. 474-484
    • Wei, L.1    Hanna, A.D.2    Beard, N.A.3    Dulhunty, A.F.4
  • 25
    • 1942423621 scopus 로고    scopus 로고
    • The Role of Calsequestrin, Triadin, and Junctin in Conferring Cardiac Ryanodine Receptor Responsiveness to Luminal Calcium
    • Gyorke I, Hester NA, Jones LR, Gyorke S, (2004) The Role of Calsequestrin, Triadin, and Junctin in Conferring Cardiac Ryanodine Receptor Responsiveness to Luminal Calcium. Biophys J 86: 2121-2128.
    • (2004) Biophys J , vol.86 , pp. 2121-2128
    • Gyorke, I.1    Hester, N.A.2    Jones, L.R.3    Gyorke, S.4
  • 26
    • 0027988041 scopus 로고
    • Polar zippers: their role in human disease
    • Perutz M, (1994) Polar zippers: their role in human disease. Protein Sci 3: 1629-1637.
    • (1994) Protein Sci , vol.3 , pp. 1629-1637
    • Perutz, M.1
  • 27
    • 0034625374 scopus 로고    scopus 로고
    • Localization and characterization of the calsequestrin-binding domain of triadin 1. Evidence for a charged beta-strand in mediating the protein-protein interaction
    • Kobayashi YM, Alseikhan BA, Jones LR, (2000) 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: 17639-17646.
    • (2000) J Biol Chem , vol.275 , pp. 17639-17646
    • Kobayashi, Y.M.1    Alseikhan, B.A.2    Jones, L.R.3
  • 29
    • 0028291932 scopus 로고
    • KEKE motifs. Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors
    • Realini C, Rogers SW, Rechsteiner M, (1994) KEKE motifs. Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors. FEBS Lett 348: 109-113.
    • (1994) FEBS Lett , vol.348 , pp. 109-113
    • Realini, C.1    Rogers, S.W.2    Rechsteiner, M.3
  • 31
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai FA, Erickson HP, Rousseau E, Liu QY, Meissner G, (1988) Purification and reconstitution of the calcium release channel from skeletal muscle. Nature 331: 315-319.
    • (1988) Nature , vol.331 , pp. 315-319
    • Lai, F.A.1    Erickson, H.P.2    Rousseau, E.3    Liu, Q.Y.4    Meissner, G.5
  • 32
    • 0036219539 scopus 로고    scopus 로고
    • Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels
    • Beard NA, Sakowska MM, Dulhunty AF, Laver DR, (2002) Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels. Biophysical Journal 82: 310-320.
    • (2002) Biophysical Journal , vol.82 , pp. 310-320
    • Beard, N.A.1    Sakowska, M.M.2    Dulhunty, A.F.3    Laver, D.R.4
  • 33
    • 33846323688 scopus 로고    scopus 로고
    • A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction
    • Kimura T, Pace SM, Wei L, Beard NA, Dirksen RT, et al. (2007) A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction. Biochem J 401: 317-324.
    • (2007) Biochem J , vol.401 , pp. 317-324
    • Kimura, T.1    Pace, S.M.2    Wei, L.3    Beard, N.A.4    Dirksen, R.T.5
  • 34
    • 0023758114 scopus 로고
    • Purified ryanodine receptor of skeletal muscle sarcoplasmic reticulum forms Ca2+-activated oligomeric Ca2+ channels in planar bilayers
    • Hymel L, Inui M, Fleischer S, Schindler H, (1988) Purified ryanodine receptor of skeletal muscle sarcoplasmic reticulum forms Ca2+-activated oligomeric Ca2+ channels in planar bilayers. Proc Natl Acad Sci U S A 85: 441-445.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 441-445
    • Hymel, L.1    Inui, M.2    Fleischer, S.3    Schindler, H.4
  • 35
    • 0028180422 scopus 로고
    • Ryanodine receptor/Ca2+ release channels and their regulation by endogenous effectors
    • Meissner G, (1994) Ryanodine receptor/Ca2+ release channels and their regulation by endogenous effectors. Annu Rev Physiol 56: 485-508.
    • (1994) Annu Rev Physiol , vol.56 , pp. 485-508
    • Meissner, G.1
  • 36
    • 0028933416 scopus 로고
    • Ammonium ion at low concentration stabilizes the G-quadruplex formation by telomeric sequence
    • Nagesh N, Chatterji D, (1995) Ammonium ion at low concentration stabilizes the G-quadruplex formation by telomeric sequence. J Biochem Biophys Methods 30: 1-8.
    • (1995) J Biochem Biophys Methods , vol.30 , pp. 1-8
    • Nagesh, N.1    Chatterji, D.2
  • 37
    • 0022322597 scopus 로고
    • Design and characterization of peptides with amphiphilic beta-strand structures
    • Osterman DG, Kaiser ET, (1985) Design and characterization of peptides with amphiphilic beta-strand structures. J Cell Biochem 29: 57-72.
    • (1985) J Cell Biochem , vol.29 , pp. 57-72
    • Osterman, D.G.1    Kaiser, E.T.2
  • 38
    • 0028567151 scopus 로고
    • Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls
    • Liu G, Pessah IN, (1994) Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls. J Biol Chem 269: 33028-33034.
    • (1994) J Biol Chem , vol.269 , pp. 33028-33034
    • Liu, G.1    Pessah, I.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.