메뉴 건너뛰기




Volumn 342, Issue 1, 2004, Pages 145-153

The relative position of RyR feet and DHPR tetrads in skeletal muscle

Author keywords

calcium release units; dihydropyridine receptors; excitation contraction coupling; ryanodine receptors; skeletal muscle

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; CALCIUM; RECEPTOR SUBUNIT; RYANODINE RECEPTOR;

EID: 4143110231     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.07.035     Document Type: Article
Times cited : (71)

References (36)
  • 1
    • 0025869296 scopus 로고
    • The mechanical hypothesis of excitation-contraction
    • E. Rios, J. Ma, and A. Gonzales The mechanical hypothesis of excitation-contraction J. Muscle Res. Cell Motil. 12 1991 127 135
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 127-135
    • Rios, E.1    Ma2    Gonzales, A.J.3
  • 2
    • 0028324398 scopus 로고
    • Control of calcium release in functioning skeletal muscle fibers
    • M.F. Schneider Control of calcium release in functioning skeletal muscle fibers Annu. Rev. Physiol. 56 1994 463 484
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 463-484
    • Schneider, M.F.1
  • 3
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • B.A. Block, T. Imagawa, K.P. Campbell, and C. Franzini-Armstrong Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle J. Cell Biol. 107 1988 2587 2600
    • (1988) J. Cell Biol. , vol.107 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell3    Franzini-Armstrong, C.K.P.4
  • 4
    • 0028065352 scopus 로고
    • Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA
    • H. Takekura, L. Bennett, T. Tanabe, K.G. Beam, and C. Franzini-Armstrong Restoration of junctional tetrads in dysgenic myotubes by dihydropyridine receptor cDNA Biophys. J. 67 1994 793 804
    • (1994) Biophys. J. , vol.67 , pp. 793-804
    • Takekura, H.1    Bennett, L.2    Tanabe, T.3    Beam4    Franzini-Armstrong, C.K.G.5
  • 5
    • 0032559585 scopus 로고    scopus 로고
    • Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle
    • F. Protasi, C. Franzini-Armstrong, and P.D. Allen Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle J. Cell Biol. 140 1998 831 842
    • (1998) J. Cell Biol. , vol.140 , pp. 831-842
    • Protasi, F.1    Franzini-Armstrong2    Allen, P.D.C.3
  • 6
    • 0032566748 scopus 로고    scopus 로고
    • Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling
    • J. Nakai, T. Tanabe, T. Konno, B. Adams, and K.G. Beam Localization in the II-III loop of the dihydropyridine receptor of a sequence critical for excitation-contraction coupling J. Biol. Chem. 273 1998 24983 24986
    • (1998) J. Biol. Chem. , vol.273 , pp. 24983-24986
    • Nakai, J.1    Tanabe, T.2    Konno, T.3    Adams4    Beam, K.G.B.5
  • 7
    • 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
    • M. Grabner, R.T. Dirksen, N. Suda, and K.G. Beam The II-III loop of the skeletal muscle dihydropyridine receptor is responsible for the Bi-directional coupling with the ryanodine receptor J. Biol. Chem. 274 1999 21913 21919
    • (1999) J. Biol. Chem. , vol.274 , pp. 21913-21919
    • Grabner, M.1    Dirksen, R.T.2    Suda3    Beam, K.G.N.4
  • 8
    • 85006142608 scopus 로고
    • I. Structure of the junction in frog twitch fibers
    • C. Franzini-Armstrong I. Structure of the junction in frog twitch fibers J. Cell Biol. 47 1970 488 499
    • (1970) J. Cell Biol. , vol.47 , pp. 488-499
    • Franzini-Armstrong, C.1
  • 9
    • 0021137066 scopus 로고
    • Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle
    • A. Saito, S. Seiler, A. Chu, and S. Fleischer Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle J. Cell Biol. 99 1984 875 885
    • (1984) J. Cell Biol. , vol.99 , pp. 875-885
    • Saito, A.1    Seiler, S.2    Chu3    Fleischer, S.A.4
  • 10
    • 0021738923 scopus 로고
    • Subunit structure of junctional feet in triads of skeletal muscle. A freeze-drying, rotary-shadowing study
    • D.G. Ferguson, H. Schwartz, and C. Franzini-Armstrong Subunit structure of junctional feet in triads of skeletal muscle. A freeze-drying, rotary-shadowing study J. Cell Biol. 99 1984 1735 1742
    • (1984) J. Cell Biol. , vol.99 , pp. 1735-1742
    • Ferguson, D.G.1    Schwartz2    Franzini-Armstrong, C.H.3
  • 11
    • 0034281991 scopus 로고    scopus 로고
    • Intrinsic lattice formation by the ryanodine receptor calcium-release channel
    • C.C. Yin, and F.A. Lai Intrinsic lattice formation by the ryanodine receptor calcium-release channel Nature Cell Biol. 2 2000 669 671
    • (2000) Nature Cell Biol. , vol.2 , pp. 669-671
    • Yin1    Lai, F.A.C.C.2
  • 13
    • 0028919291 scopus 로고
    • Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted for the ryanodine receptor
    • H. Takekura, M. Nishi, T. Noda, H. Takeshima, and C. Franzini-Armstrong Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted for the ryanodine receptor Proc. Natl Acad. Sci. USA 92 1995 3381 3385
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3381-3385
    • Takekura, H.1    Nishi, M.2    Noda, T.3    Takeshima4    Franzini-Armstrong, C.H.5
  • 15
    • 0036930754 scopus 로고    scopus 로고
    • Multiple regions of RYR1 mediate functional and structural interactions with α1s DHPR in skeletal muscle
    • F. Protasi, C. Paolini, J. Nakai, K.J. Beam, C. Franzini-Armstrong, and P.D. Allen Multiple regions of RYR1 mediate functional and structural interactions with α1s DHPR in skeletal muscle Biophys. J. 83 2002 3230 3244
    • (2002) Biophys. J. , vol.83 , pp. 3230-3244
    • Protasi, F.1    Paolini, C.2    Nakai, J.3    Beam, K.J.4    Franzini-Armstrong5    Allen, P.D.C.6
  • 16
    • 0028004249 scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle
    • M. Radermacher, V. Rao, R. Grassucci, J. Frank, A.P. Timerman, S. Fleischer, and T. Wagenknecht Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle J. Cell Biol. 127 1994 411 423
    • (1994) J. Cell Biol. , vol.127 , pp. 411-423
    • Radermacher, M.1    Rao, V.2    Grassucci, R.3    Frank, J.4    Timerman, A.P.5    Fleischer6    Wagenknecht, T.S.7
  • 18
    • 0035932955 scopus 로고    scopus 로고
    • Three dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus
    • Z. Liu, J. Zhang, M.R. Sharma, S.R.W. Chen, P. Li, and T. Wagenknecht Three dimensional reconstruction of the recombinant type 3 ryanodine receptor and localization of its amino terminus Proc. Natl Acad. Sci. USA 98 2001 6104 6109
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6104-6109
    • Liu, Z.1    Zhang, J.2    Sharma, M.R.3    Chen, S.R.W.4    Li5    Wagenknecht, T.P.6
  • 19
    • 2242464846 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the recombinant type 2 ryanodine receptor and localization of its divergent region 1
    • Z. Liu, J. Zhang, P. Li, S.R. Chen, and T. Wagenknecht Three-dimensional reconstruction of the recombinant type 2 ryanodine receptor and localization of its divergent region 1 J. Biol. Chem. 277 2002 46712 46719
    • (2002) J. Biol. Chem. , vol.277 , pp. 46712-46719
    • Liu, Z.1    Zhang, J.2    Li, P.3    Chen4    Wagenknecht, T.S.R.5
  • 20
    • 0023850808 scopus 로고
    • Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 subunit
    • A. Leung, T. Imagawa, B. Block, C. Franzini-Armstrong, and K.P. Campbell Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 subunit J. Biol. Chem. 263 1988 994 1001
    • (1988) J. Biol. Chem. , vol.263 , pp. 994-1001
    • Leung, A.1    Imagawa, T.2    Block, B.3    Franzini-Armstrong4    Campbell, K.P.C.5
  • 25
    • 0029060579 scopus 로고
    • Alternate disposition of tetrads in peripheral couplings of skeletal muscle
    • C. Franzini-Armstrong, and C.W. Kish Alternate disposition of tetrads in peripheral couplings of skeletal muscle J. Muscle Res. Cell Motil. 16 1995 19 324
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 19-324
    • Franzini-Armstrong1    Kish, C.W.C.2
  • 26
    • 0036841939 scopus 로고    scopus 로고
    • Electron tomography of frozen-hydrated isolated triad junctions
    • T. Wagenknecht, C.E. Hsieh, B.K. Rath, S. Fleischer, and M. Marko Electron tomography of frozen-hydrated isolated triad junctions Biophys. J. 83 2002 2491 2501
    • (2002) Biophys. J. , vol.83 , pp. 2491-2501
    • Wagenknecht, T.1    Hsieh, C.E.2    Rath, B.K.3    Fleischer4    Marko, M.S.5
  • 28
    • 0025900714 scopus 로고
    • The ryanodine receptor/junctional channel complex is regulated by growth factors in a myogenic cell line
    • A.R. Marks, M.B. Taubman, A. Saito, Y. Dai, and S. Fleischer The ryanodine receptor/junctional channel complex is regulated by growth factors in a myogenic cell line J. Cell Biol. 114 1991 303 312
    • (1991) J. Cell Biol. , vol.114 , pp. 303-312
    • Marks, A.R.1    Taubman, M.B.2    Saito, A.3    Dai4    Fleischer, S.Y.5
  • 29
    • 0028937373 scopus 로고
    • Electron cryomicroscopy and angular reconstruction used to visualize the skeletal muscle calcium release channel
    • I.I. Serysheva, E.V. Orlova, W. Chiu, M.B. Sherman, S.L. Hamilton, and M. van Heel Electron cryomicroscopy and angular reconstruction used to visualize the skeletal muscle calcium release channel Struct. Biol. 2 1995 18 24
    • (1995) Struct. Biol. , vol.2 , pp. 18-24
    • Serysheva, I.I.1    Orlova, E.V.2    Chiu, W.3    Sherman, M.B.4    Hamilton5    Van Heel, M.S.L.6
  • 31
    • 0031464972 scopus 로고    scopus 로고
    • Locations of calmodulin and FK506-binding protein on the three dimensional architecture of the skeletal muscle ryanodine receptor
    • T. Wagenknecht, M. Radermacher, R. Grassucci, J. Berkowitz, H.B. Xin, and S. Fleischer Locations of calmodulin and FK506-binding protein on the three dimensional architecture of the skeletal muscle ryanodine receptor J. Biol. Chem. 272 1997 32463 32471
    • (1997) J. Biol. Chem. , vol.272 , pp. 32463-32471
    • Wagenknecht, T.1    Radermacher, M.2    Grassucci, R.3    Berkowitz, J.4    Xin5    Fleischer, S.H.B.6
  • 32
    • 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. 277 2002 1349 1353
    • (2002) J. Biol. Chem. , vol.277 , pp. 1349-1353
    • Samso1    Wagenknecht, T.M.2
  • 34
    • 0036617107 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of ryanodine receptor
    • T. Wagenknecht, and M. Samso Three-dimensional reconstruction of ryanodine receptor Front. Biosci. 7 2002 d1464 d1474
    • (2002) Front. Biosci. , vol.7
    • Wagenknecht1    Samso, M.T.2
  • 35
    • 0019412624 scopus 로고
    • Freeze-fracture electron microscopic analysis of plasma membranes of cultured muscle cells in Duchenne dystrophy
    • M. Osame, A.G. Engel, C.J. Rebouche, and R.E. Scott Freeze-fracture electron microscopic analysis of plasma membranes of cultured muscle cells in Duchenne dystrophy Neurology 31 1981 972 979
    • (1981) Neurology , vol.31 , pp. 972-979
    • Osame, M.1    Engel, A.G.2    Rebouche3    Scott, R.E.C.J.4
  • 36
    • 0025362753 scopus 로고
    • A simple method for freeze-drying of macromolecules and macromolecular complexes
    • K.E. Loesser, and C. Franzini-Armstrong A simple method for freeze-drying of macromolecules and macromolecular complexes J. Struct. Biol. 103 1990 48 56
    • (1990) J. Struct. Biol. , vol.103 , pp. 48-56
    • Loesser1    Franzini-Armstrong, C.K.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.