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Volumn 5, Issue 2, 2011, Pages

The elusive role of the SPRY2 domain in RyR1

Author keywords

Alternatively spliced residues; Excitation contraction coupling; Single RyR1 channel activity; Skeletal muscle; SPRY domain in RyR1

Indexed keywords

RYANODINE RECEPTOR 1;

EID: 79952551568     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.5.2.14407     Document Type: Article
Times cited : (13)

References (40)
  • 1
    • 0025288735 scopus 로고
    • Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling
    • Tanabe T, Beam KG, Adams BA, Niidome T, Numa S. Regions of the skeletal muscle dihydropyridine receptor critical for excitation-contraction coupling. Nature 1990; 346:567-9.
    • (1990) Nature , vol.346 , pp. 567-569
    • Tanabe, T.1    Beam, K.G.2    Adams, B.A.3    Niidome, T.4    Numa, S.5
  • 3
    • 70450247255 scopus 로고    scopus 로고
    • Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor
    • Tae H, Casarotto MG, Dulhunty AF. Ubiquitous SPRY domains and their role in the skeletal type ryanodine receptor. Eur Biophys J 2009.
    • (2009) Eur Biophys J
    • Tae, H.1    Casarotto, M.G.2    Dulhunty, A.F.3
  • 6
    • 0032478812 scopus 로고    scopus 로고
    • A 37-amino acid sequence in the skeletal muscle ryanodine receptor interacts with the cytoplasmic loop between domains II and III in the skeletal muscle dihydropyridine receptor
    • DOI 10.1074/jbc.273.14.7791
    • Leong P, MacLennan DH. A 37-amino acid sequence in the skeletal muscle ryanodine receptor interacts with the cytoplasmic loop between domains II and III in the skeletal muscle dihydropyridine receptor. J Biol Chem 1998; 273:7791-4. (Pubitemid 28168820)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.14 , pp. 7791-7794
    • Leong, P.1    MacLennan, D.H.2
  • 8
    • 0038182563 scopus 로고    scopus 로고
    • Maurocalcine and peptide A stabilize distinct subconductance states of ryanodine receptor type 1, revealing a proportional gating mechanism
    • DOI 10.1074/jbc.M209501200
    • Chen L, Esteve E, Sabatier JM, Ronjat M, De Waard M, Allen PD, et al. Maurocalcine and peptide A stabilize distinct subconductance states of ryanodine receptor type 1, revealing a proportional gating mechanism. J Biol Chem 2003; 278:16095-106. (Pubitemid 36799731)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 16095-16106
    • Chen, L.1    Esteve, E.2    Sabatier, J.-M.3    Ronjat, M.4    De Waard, M.5    Allen, P.D.6    Pessah, I.N.7
  • 9
    • 1642456657 scopus 로고    scopus 로고
    • Removal of clustered positive charge from dihydropyridine receptor II-III loop peptide augments activation of ryanodine receptors
    • DOI 10.1016/j.bbrc.2003.12.128
    • Bannister ML, Williams AJ, Sitsapesan R. Removal of clustered positive charge from dihydropyridine receptor II-III loop peptide augments activation of ryanodine receptors. Biochem Biophys Res Commun 2004; 314:667-74. (Pubitemid 38112851)
    • (2004) Biochemical and Biophysical Research Communications , vol.314 , Issue.3 , pp. 667-674
    • Bannister, M.L.1    Williams, A.J.2    Sitsapesan, R.3
  • 10
    • 26044462648 scopus 로고    scopus 로고
    • 2+ release events in permeabilized skeletal muscle fibers
    • 2+ release events in permeabilized skeletal muscle fibers. Biol Res 2004; 37:613-6.
    • (2004) Biol Res , vol.37 , pp. 613-616
    • Schneider, M.F.1    Rodney, G.G.2
  • 13
    • 58149284005 scopus 로고    scopus 로고
    • A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor
    • Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, et al. A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. Int J Biochem Cell Biol 2009; 41:677-86.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 677-686
    • Cui, Y.1    Tae, H.S.2    Norris, N.C.3    Karunasekara, Y.4    Pouliquin, P.5    Board, P.G.6
  • 14
    • 61349201464 scopus 로고    scopus 로고
    • Molecular recognition of the disordered dihydropyridine receptor II-III loop by a conserved spry domain of the type 1 ryanodine receptor
    • Tae HS, Norris NC, Cui Y, Karunasekara Y, Board PG, Dulhunty AF, et al. Molecular recognition of the disordered dihydropyridine receptor II-III loop by a conserved spry domain of the type 1 ryanodine receptor. Clin Exp Pharmacol Physiol 2009; 36:346-9.
    • (2009) Clin Exp Pharmacol Physiol , vol.36 , pp. 346-349
    • Tae, H.S.1    Norris, N.C.2    Cui, Y.3    Karunasekara, Y.4    Board, P.G.5    Dulhunty, A.F.6
  • 15
    • 0032566748 scopus 로고    scopus 로고
    • Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling
    • DOI 10.1074/jbc.273.39.24983
    • Nakai J, Tanabe T, Konno T, Adams B, Beam KG. Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling. J Biol Chem 1998; 273:24983-6. (Pubitemid 28443252)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.39 , pp. 24983-24986
    • Nakai, J.1    Tanabe, T.2    Konno, T.3    Adams, B.4    Beam, K.G.5
  • 16
    • 0033618408 scopus 로고    scopus 로고
    • The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the Bi-directional coupling with the ryanodine receptor
    • Grabner M, Dirksen RT, Suda N, Beam KG. The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the Bi-directional coupling with the ryanodine receptor. J Biol Chem 1999; 274:21913-9.
    • (1999) J Biol Chem , vol.274 , pp. 21913-21919
    • Grabner, M.1    Dirksen, R.T.2    Suda, N.3    Beam, K.G.4
  • 18
    • 0028114269 scopus 로고
    • Identification of two ryanodine receptor transcripts in neonatal, slow-, and fast-twitch rabbit skeletal muscles
    • DOI 10.1006/bbrc.1994.2385
    • Zorzato F, Sacchetto R, Margreth A. Identification of two ryanodine receptor transcripts in neonatal, slow- and fast-twitch rabbit skeletal muscles. Biochem Biophys Res Commun 1994; 203:1725-30. (Pubitemid 24321563)
    • (1994) Biochemical and Biophysical Research Communications , vol.203 , Issue.3 , pp. 1725-1730
    • Zorzato, F.1    Sacchetto, R.2    Margreth, A.3
  • 19
    • 0028813820 scopus 로고
    • Tissue-specific and developmentally regulated alternative splicing in mouse skeletal muscle ryanodine receptor mRNA
    • Futatsugi A, Kuwajima G, Mikoshiba K. Tissue-specific and developmentally regulated alternative splicing in mouse skeletal muscle ryanodine receptor mRNA. Biochem J 1995; 305:373-8.
    • (1995) Biochem J , vol.305 , pp. 373-378
    • Futatsugi, A.1    Kuwajima, G.2    Mikoshiba, K.3
  • 21
    • 33846323688 scopus 로고    scopus 로고
    • A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction
    • DOI 10.1042/BJ20060686
    • Kimura T, Pace SM, Wei L, Beard NA, Dirksen RT, Dulhunty AF. A variably spliced region in the type 1 ryanodine receptor may participate in an inter-domain interaction. Biochem J 2007; 401:317-24. (Pubitemid 46114624)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 317-324
    • Kimura, T.1    Pace, S.M.2    Wei, L.3    Beard, N.A.4    Dirksen, R.T.5    Dulhunty, A.F.6
  • 23
    • 30044435649 scopus 로고    scopus 로고
    • 2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling
    • 2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction coupling. Proc Natl Acad Sci USA 2005; 102:19225-30.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 19225-19230
    • Cheng, W.1    Altafaj, X.2    Ronjat, M.3    Coronado, R.4
  • 24
    • 0033606795 scopus 로고    scopus 로고
    • Three-dimensional location of the imperatoxin A binding site on the ryanodine receptor
    • DOI 10.1083/jcb.146.2.493
    • Samso M, Trujillo R, Gurrola GB, Valdivia HH, Wagenknecht T. Three-dimensional location of the imperatoxin A binding site on the ryanodine receptor. J Cell Biol 1999; 146:493-9. (Pubitemid 29369783)
    • (1999) Journal of Cell Biology , vol.146 , Issue.2 , pp. 493-499
    • Samso, M.1    Trujillo, R.2    Gurrola, G.B.3    Valdivia, H.H.4    Wagenknecht, T.5
  • 25
    • 0037059329 scopus 로고    scopus 로고
    • 2+-calmodulin bind to neighboring locations on the ryanodine receptor
    • 2+-calmodulin bind to neighboring locations on the ryanodine receptor. J Biol Chem 2002; 277:1349-53.
    • (2002) J Biol Chem , vol.277 , pp. 1349-1353
    • Samso, M.1    Wagenknecht, T.2
  • 27
    • 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. Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin. Int J Biochem Cell Biol 2009; 41:2214-24.
    • (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
  • 28
    • 17644425846 scopus 로고    scopus 로고
    • Activating the ryanodine receptor with dihydropyridine receptor II-III loop segments: Size and charge do matter
    • Casarotto MG, Green D, Pace S, Young J, Dulhunty AF. Activating the ryanodine receptor with dihydropyridine receptor II-III loop segments: size and charge do matter. Front Biosci 2004; 9:2860-72.
    • (2004) Front Biosci , vol.9 , pp. 2860-2872
    • Casarotto, M.G.1    Green, D.2    Pace, S.3    Young, J.4    Dulhunty, A.F.5
  • 29
    • 0035016222 scopus 로고    scopus 로고
    • Structural determinants for activation or inhibition of ryanodine receptors by basic residues in the dihydropyridine receptor II-III loop
    • Casarotto MG, Green D, Pace SM, Curtis SM, Dulhunty AF. Structural determinants for activation or inhibition of ryanodine receptors by basic residues in the dihydropyridine receptor II-III loop. Biophys J 2001; 80:2715-26. (Pubitemid 32521646)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2715-2726
    • Casarotto, M.G.1    Green, D.2    Pace, S.M.3    Curtis, S.M.4    Dulhunty, A.F.5
  • 30
    • 0034697176 scopus 로고    scopus 로고
    • 2+ channel regulation
    • DOI 10.1074/jbc.275.16.11618
    • Yamamoto T, El-Hayek R, Ikemoto N. Postulated role of interdomain interaction within the ryanodine receptor in Ca2+ channel regulation. J Biol Chem 2000; 275:11618-25. (Pubitemid 30237720)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11618-11625
    • Yamamoto, T.1    El-Hayek, R.2    Ikemoto, N.3
  • 31
    • 2942711417 scopus 로고    scopus 로고
    • 2+ channel regulation by interdomain interaction within the ryanodine receptor
    • 2+ channel regulation by interdomain interaction within the ryanodine receptor. Biochem J 2004; 380:561-9.
    • (2004) Biochem J , vol.380 , pp. 561-569
    • Kobayashi, S.1    Yamamoto, T.2    Parness, J.3    Ikemoto, N.4
  • 36
    • 16344388804 scopus 로고    scopus 로고
    • 2+ handling caused by malignant hyperthermia and central core disease mutations in RyR1
    • DOI 10.1529/biophysj.104.048447
    • Dirksen RT, Avila G. Distinct effects on Ca2+ handling caused by malignant hyperthermia and central core disease mutations in RyR1. Biophys J 2004; 87:3193-204. (Pubitemid 40468576)
    • (2004) Biophysical Journal , vol.87 , Issue.5 , pp. 3193-3204
    • Dirksen, R.T.1    Avila, G.2
  • 37
    • 0021137066 scopus 로고
    • Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle
    • Saito A, Seiler S, Chu A, Fleischer S. Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle. J Cell Biol 1984; 99:875-85. (Pubitemid 14043345)
    • (1984) Journal of Cell Biology , vol.99 , Issue.3 , pp. 875-885
    • Saito, A.1    Seiler, S.2    Chu, A.3    Fleischer, S.4
  • 39
    • 33746839364 scopus 로고    scopus 로고
    • The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors
    • DOI 10.1529/biophysj.106.082610
    • Wei L, Varsanyi M, Dulhunty AF, Beard NA. The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors. Biophys J 2006; 91:1288-301. (Pubitemid 44174246)
    • (2006) Biophysical Journal , vol.91 , Issue.4 , pp. 1288-1301
    • Wei, L.1    Varsanyi, M.2    Dulhunty, A.F.3    Beard, N.A.4
  • 40
    • 34247882821 scopus 로고    scopus 로고
    • 2+ sites
    • 2+ sites. Biophys J 2007; 92:3541-55.
    • (2007) Biophys J , vol.92 , pp. 3541-3555
    • Laver, D.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.