메뉴 건너뛰기




Volumn 15, Issue 18, 1996, Pages 4844-4851

Native structure and arrangement of inositol-1,4,5-trisphosphate receptor molecules in bovine cerebellar Purkinje cells as studied by quick-freeze deep-etch electron microscopy

Author keywords

Cerebellar Purkinje neuron; In situ structure; Inositol 1 4 5 trisphosphate receptor; Quick freeze deep etch electron microscopy; Ryanodine receptor

Indexed keywords

INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR;

EID: 0029791753     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00865.x     Document Type: Article
Times cited : (61)

References (51)
  • 1
    • 0024245148 scopus 로고
    • Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle
    • Block, B.A., Imagawa, T., Campbell, K.P. and Franzini-Armstrong, C. (1988) Structural evidence for direct interaction between the molecular components of the transverse tubule/sarcoplasmic reticulum junction in skeletal muscle. J. Cell Biol., 107, 2587-2600.
    • (1988) J. Cell Biol. , vol.107 , pp. 2587-2600
    • Block, B.A.1    Imagawa, T.2    Campbell, K.P.3    Franzini-Armstrong, C.4
  • 2
    • 0020805413 scopus 로고
    • Crystalline structure of sarcoplasmic reticulum from scallop
    • Castellani, L. and Hardwicke, M.D. (1983) Crystalline structure of sarcoplasmic reticulum from scallop. J. Cell Biol., 97, 557-561.
    • (1983) J. Cell Biol. , vol.97 , pp. 557-561
    • Castellani, L.1    Hardwicke, M.D.2
  • 3
    • 0021930155 scopus 로고
    • Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum
    • Castellani, L., Hardwicke, M.D. and Vibert, P. (1985) Dimer ribbons in the three-dimensional structure of sarcoplasmic reticulum. J. Mol. Biol., 185, 579-594.
    • (1985) J. Mol. Biol. , vol.185 , pp. 579-594
    • Castellani, L.1    Hardwicke, M.D.2    Vibert, P.3
  • 4
    • 0025246299 scopus 로고
    • Isolation and characterization of the inositol trisphosphate receptor from smooth muscle
    • Chadwick, C., Saito, A. and Fleischer, S. (1990) Isolation and characterization of the inositol trisphosphate receptor from smooth muscle. Proc. Natl Acad. Sci. USA, 87, 2132-2136.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2132-2136
    • Chadwick, C.1    Saito, A.2    Fleischer, S.3
  • 5
    • 0020580035 scopus 로고
    • 2+-ATPase vesicles treated with vanadate
    • 2+-ATPase vesicles treated with vanadate. J. Biol. Chem., 258, 2599-2603.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2599-2603
    • Dux, L.1    Martonosi, A.2
  • 6
    • 0024259980 scopus 로고
    • Inositol 1,4,5-trisphosphate activates a channel from smooth muscle sarcoplasmic reticulum
    • Ehrlich, B.E. and Watras, J. (1988) Inositol 1,4,5-trisphosphate activates a channel from smooth muscle sarcoplasmic reticulum. Nature, 336, 583-586.
    • (1988) Nature , vol.336 , pp. 583-586
    • Ehrlich, B.E.1    Watras, J.2
  • 8
    • 0024432233 scopus 로고
    • Purified inositol 1,4,5-trisphosphate receptor mediates calcium flux in reconstituted lipid vesicles
    • Ferris, C.D., Huganir, R.L., Supattapone, S. and Snyder, S.H. (1989) Purified inositol 1,4,5-trisphosphate receptor mediates calcium flux in reconstituted lipid vesicles. Nature, 342, 87-89.
    • (1989) Nature , vol.342 , pp. 87-89
    • Ferris, C.D.1    Huganir, R.L.2    Supattapone, S.3    Snyder, S.H.4
  • 9
    • 85006142608 scopus 로고
    • Studies of the triad. I. Structure of the junction in frog twitch fibers
    • Franzini-Armstrong, C. (1970) Studies of the triad. I. Structure of the junction in frog twitch fibers. J. Cell Biol., 47, 488-499.
    • (1970) J. Cell Biol. , vol.47 , pp. 488-499
    • Franzini-Armstrong, C.1
  • 10
    • 0020578983 scopus 로고
    • Junctional feet and particles in the triads of fast twitch muscle fibers
    • Franzini-Armstrong, C. and Nunzi, G. (1983) Junctional feet and particles in the triads of fast twitch muscle fibers. J. Muscle Res. Cell Motil., 4, 233-252.
    • (1983) J. Muscle Res. Cell Motil. , vol.4 , pp. 233-252
    • Franzini-Armstrong, C.1    Nunzi, G.2
  • 11
    • 0024432232 scopus 로고
    • Primary structure and functional expression of the inositol 1,4,5-trisphosphate binding protein P400
    • Furuichi, T., Yoshikawa, S., Miyawaki, A., Wada, K., Maeda, N. and Mikoshiba, K. (1989) Primary structure and functional expression of the inositol 1,4,5-trisphosphate binding protein P400. Nature, 342, 32-38.
    • (1989) Nature , vol.342 , pp. 32-38
    • Furuichi, T.1    Yoshikawa, S.2    Miyawaki, A.3    Wada, K.4    Maeda, N.5    Mikoshiba, K.6
  • 13
    • 0019462923 scopus 로고
    • Lamellar bodies in Purkinje nerve cells experimentally induced by electric field
    • Hansson, H.A. (1981) Lamellar bodies in Purkinje nerve cells experimentally induced by electric field. Brain Res., 216, 187-191.
    • (1981) Brain Res. , vol.216 , pp. 187-191
    • Hansson, H.A.1
  • 14
    • 0007486293 scopus 로고
    • Lamellar bodies, an unusual arrangement of the granular endoplasmic reticulum
    • Herndon, R. (1964) Lamellar bodies, an unusual arrangement of the granular endoplasmic reticulum. J. Cell Biol., 20, 338-342.
    • (1964) J. Cell Biol. , vol.20 , pp. 338-342
    • Herndon, R.1
  • 15
    • 49149135185 scopus 로고
    • Quick-freeze deep-etch preparation of samples for 3-D electron microscopy
    • Heuser, J.E. (1981) Quick-freeze deep-etch preparation of samples for 3-D electron microscopy. Trends Biochem. Sci., 6, 64-68.
    • (1981) Trends Biochem. Sci. , vol.6 , pp. 64-68
    • Heuser, J.E.1
  • 16
    • 0021095633 scopus 로고
    • Procedure of freeze-drying molecules adsorbed to mica flakes
    • Heuser, J.E. (1983) Procedure of freeze-drying molecules adsorbed to mica flakes. J. Mol. Biol., 169, 155-195.
    • (1983) J. Mol. Biol. , vol.169 , pp. 155-195
    • Heuser, J.E.1
  • 17
    • 0024416678 scopus 로고
    • Protocol for 3-D visualization of molecules on mica via the quick-freeze deep-etch technique
    • Heuser, J.E. (1989) Protocol for 3-D visualization of molecules on mica via the quick-freeze deep-etch technique. J. Electron Microsc. Techniques, 13, 244-263.
    • (1989) J. Electron Microsc. Techniques , vol.13 , pp. 244-263
    • Heuser, J.E.1
  • 18
    • 0018746093 scopus 로고
    • Synaptic vesicle exocytosis captured and correlated with quantal transmitter release
    • Heuser, J.E., Reese, T.S., Jan, L.Y., Jan, Y.N., Dennis, M.J. and Evans, L. (1979) Synaptic vesicle exocytosis captured and correlated with quantal transmitter release. J. Cell Biol., 81, 275-300.
    • (1979) J. Cell Biol. , vol.81 , pp. 275-300
    • Heuser, J.E.1    Reese, T.S.2    Jan, L.Y.3    Jan, Y.N.4    Dennis, M.J.5    Evans, L.6
  • 20
    • 0141755922 scopus 로고
    • Fixation of the central nervous system for electron microscopy by aldehyde perfusion. III. Structural changes after exanguination and delayed perfusion
    • Karlsson, U. and Schultz, R.L. (1966) Fixation of the central nervous system for electron microscopy by aldehyde perfusion. III. Structural changes after exanguination and delayed perfusion. J. Ultrastruct. Res., 14, 47-63.
    • (1966) J. Ultrastruct. Res. , vol.14 , pp. 47-63
    • Karlsson, U.1    Schultz, R.L.2
  • 21
    • 0024837628 scopus 로고
    • The effect of various nucleotides on the structure of actin-attached myosin subfragment-1 studied by quick-freeze deep-etch electron microscopy
    • Katayama, E. (1989) The effect of various nucleotides on the structure of actin-attached myosin subfragment-1 studied by quick-freeze deep-etch electron microscopy. J. Biochem., 106, 751-770.
    • (1989) J. Biochem. , vol.106 , pp. 751-770
    • Katayama, E.1
  • 22
    • 0018539004 scopus 로고
    • Electron microscopic analysis of tropomyosin paracrystals
    • Katayama, E. and Nonomura, Y. (1979) Electron microscopic analysis of tropomyosin paracrystals. J. Biochem., 86, 1511-1522.
    • (1979) J. Biochem. , vol.86 , pp. 1511-1522
    • Katayama, E.1    Nonomura, Y.2
  • 23
    • 0029978352 scopus 로고    scopus 로고
    • Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images
    • Katayama, E., Shiraishi, T., Oosawa, K., Baba, N. and Aizawa, S.-I. (1996) Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images. J. Mol. Biol., 255, 458-475.
    • (1996) J. Mol. Biol. , vol.255 , pp. 458-475
    • Katayama, E.1    Shiraishi, T.2    Oosawa, K.3    Baba, N.4    Aizawa, S.-I.5
  • 24
    • 0027102174 scopus 로고
    • Two types of ryanodine receptors in mouse brain: Skeletal muscle type exclusively in Purkinje cells and cardiac muscle type in various neurons
    • Kuwajima, G., Futatsugi, A., Niinobe, M., Nakanishi, S. and Mikoshiba, K. (1992) Two types of ryanodine receptors in mouse brain: skeletal muscle type exclusively in Purkinje cells and cardiac muscle type in various neurons. Neuron, 9, 1133-1142.
    • (1992) Neuron , vol.9 , pp. 1133-1142
    • Kuwajima, G.1    Futatsugi, A.2    Niinobe, M.3    Nakanishi, S.4    Mikoshiba, K.5
  • 26
    • 0026033046 scopus 로고
    • Structural and functional characterization of inositol 1,4,5-trisphosphate receptor channel from mouse cerebellum
    • Maeda, N., Kawasaki, T., Nakade, S., Yokota, N., Taguchi, T., Kasai, M. and Mikoshiba, K. (1991a) Structural and functional characterization of inositol 1,4,5-trisphosphate receptor channel from mouse cerebellum. J. Biol. Chem., 266, 1109-1116.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1109-1116
    • Maeda, N.1    Kawasaki, T.2    Nakade, S.3    Yokota, N.4    Taguchi, T.5    Kasai, M.6    Mikoshiba, K.7
  • 29
    • 0020956541 scopus 로고
    • Ultrastructural aspect of rapid-frozen, deep-etched and rotary-shadowed synaptosomes
    • Meller, K. (1983) Ultrastructural aspect of rapid-frozen, deep-etched and rotary-shadowed synaptosomes. Cell Tissue Res., 231, 347-355.
    • (1983) Cell Tissue Res. , vol.231 , pp. 347-355
    • Meller, K.1
  • 30
    • 0025332712 scopus 로고
    • Structure and expression of the rat inositol 1,4,5-trisphosphate receptor
    • Mignery, G.A., Newton, C.L., Archer, B.T. and Südhof, T.C. (1990) Structure and expression of the rat inositol 1,4,5-trisphosphate receptor. J. Biol. Chem., 265, 12679-12685.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12679-12685
    • Mignery, G.A.1    Newton, C.L.2    Archer, B.T.3    Südhof, T.C.4
  • 32
    • 0028568387 scopus 로고
    • Evaluation of high-resolution shadowing applied to freeze-fractured deep-etched particles: 3-D helical reconstruction of shadowed actin filaments
    • Morris, E.P., Katayama, E. and Squire, J.M. (1994) Evaluation of high-resolution shadowing applied to freeze-fractured deep-etched particles: 3-D helical reconstruction of shadowed actin filaments. J. Struct. Biol., 113, 47-55.
    • (1994) J. Struct. Biol. , vol.113 , pp. 47-55
    • Morris, E.P.1    Katayama, E.2    Squire, J.M.3
  • 35
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan, T., Rizzuto, R., Volpe, P. and Meldolesi, J. (1994) Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev., 74, 595-636.
    • (1994) Physiol. Rev. , vol.74 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4
  • 36
    • 0028004249 scopus 로고
    • Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle
    • Radermacher, M., Rao, V., Grassucci, R., Frank, J., Timerman, P., Fleischer, S. and Wagenknecht, T. (1994) Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle. J. Cell Biol., 127, 411-423.
    • (1994) J. Cell Biol. , vol.127 , pp. 411-423
    • Radermacher, M.1    Rao, V.2    Grassucci, R.3    Frank, J.4    Timerman, P.5    Fleischer, S.6    Wagenknecht, T.7
  • 37
    • 0027394852 scopus 로고
    • Tridimensional organization of Purkinje neuron cisternal stacks, a specialized endoplasmic reticulum subcompartment rich in inositol 1,4,5-trisphosphate receptors
    • Rusakov, D.A., Podini, P., Villa, A. and Meldolesi, J. (1993) Tridimensional organization of Purkinje neuron cisternal stacks, a specialized endoplasmic reticulum subcompartment rich in inositol 1,4,5-trisphosphate receptors. J. Neurocytol., 22, 273-282.
    • (1993) J. Neurocytol. , vol.22 , pp. 273-282
    • Rusakov, D.A.1    Podini, P.2    Villa, A.3    Meldolesi, J.4
  • 38
    • 0023690937 scopus 로고
    • Ultrastructure of calcium release channel of sarcoplasmic reticulum
    • Saito, A., Inui, M., Radermacher, M., Frank, J. and Fleischer, S. (1988) Ultrastructure of calcium release channel of sarcoplasmic reticulum. J. Cell Biol., 107, 211-219.
    • (1988) J. Cell Biol. , vol.107 , pp. 211-219
    • Saito, A.1    Inui, M.2    Radermacher, M.3    Frank, J.4    Fleischer, S.5
  • 40
    • 0028348910 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor causes formation of ER cisternal stacks in transfected fibroblasts and in cerebellar Purkinje cells
    • Takei, K., Mignery, G.A., Mugnaini, E., Südhof, T.C. and De Camilli, P. (1994) Inositol 1,4,5-trisphosphate receptor causes formation of ER cisternal stacks in transfected fibroblasts and in cerebellar Purkinje cells. Neuron, 12, 327-342.
    • (1994) Neuron , vol.12 , pp. 327-342
    • Takei, K.1    Mignery, G.A.2    Mugnaini, E.3    Südhof, T.C.4    De Camilli, P.5
  • 41
    • 0024318429 scopus 로고
    • Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
    • Takeshima, H. et al. (1989) Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor. Nature, 339, 439-444.
    • (1989) Nature , vol.339 , pp. 439-444
    • Takeshima, H.1
  • 43
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • Toyoshima, C., Sasabe, H. and Stokes, D.L. (1993) Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature, 362, 469-471.
    • (1993) Nature , vol.362 , pp. 469-471
    • Toyoshima, C.1    Sasabe, H.2    Stokes, D.L.3
  • 44
    • 0017769888 scopus 로고
    • Three-dimensional model of membrane-bound ribosomes obtained by electron microscopy
    • Unwin, P.N.T. (1977) Three-dimensional model of membrane-bound ribosomes obtained by electron microscopy. Nature, 269, 118-122.
    • (1977) Nature , vol.269 , pp. 118-122
    • Unwin, P.N.T.1
  • 45
    • 0007384051 scopus 로고
    • Rapid freezing and subsequent preparation methods in retinal cell biology
    • Usukura, J. (1993) Rapid freezing and subsequent preparation methods in retinal cell biology. Methods Neurosci., 13, 37-53.
    • (1993) Methods Neurosci. , vol.13 , pp. 37-53
    • Usukura, J.1
  • 46
    • 0141755923 scopus 로고
    • Early postmortem changes in cerebellar neurons of rat
    • Van Nimvegen, D. and Sheldon, H. (1966) Early postmortem changes in cerebellar neurons of rat. J. Ultrastruct. Res., 14, 36-46.
    • (1966) J. Ultrastruct. Res. , vol.14 , pp. 36-46
    • Van Nimvegen, D.1    Sheldon, H.2
  • 48
    • 0024566091 scopus 로고
    • Three-dimensional architecture of the calcium/foot structure of sarcoplasmic reticulum
    • Wagenknecht, T., Grassucci, R., Frank, J., Saito, A., Inui, M. and Fleischer, S. (1989) Three-dimensional architecture of the calcium/foot structure of sarcoplasmic reticulum. Nature, 338, 167-170.
    • (1989) Nature , vol.338 , pp. 167-170
    • Wagenknecht, T.1    Grassucci, R.2    Frank, J.3    Saito, A.4    Inui, M.5    Fleischer, S.6
  • 50
    • 0026092128 scopus 로고
    • Inositol 1,4,5-trisphosphate-gated channels in cerebellum: Presence of multiple conductance states
    • Watras, J., Bezprozvanni, I. and Ehrlich, B.E. (1991) Inositol 1,4,5-trisphosphate-gated channels in cerebellum: presence of multiple conductance states. J. Neurosci., 11, 3239-3245.
    • (1991) J. Neurosci. , vol.11 , pp. 3239-3245
    • Watras, J.1    Bezprozvanni, I.2    Ehrlich, B.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.