메뉴 건너뛰기




Volumn 125, Issue 14, 2012, Pages 3443-3453

Role of triadin in the organization of reticulum membrane at the muscle triad

Author keywords

Calcium release; Microtubule; Muscle; Reticulum; Triad; Triadin

Indexed keywords

DISULFIDE; MEMBRANE PROTEIN; TRISK 95 PROTEIN; UNCLASSIFIED DRUG;

EID: 84869102955     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.100958     Document Type: Article
Times cited : (19)

References (45)
  • 1
    • 0028089697 scopus 로고
    • Characterization Of The Sarcoplasmic Reticulum Proteins In The Thermogenic Muscles Of Fish
    • Block, B. A., O'Brien, J. And Meissner, G. (1994). Characterization Of The Sarcoplasmic Reticulum Proteins In The Thermogenic Muscles Of Fish. J. Cell Biol. 127, 1275-1287.
    • (1994) J. Cell Biol. , vol.127 , pp. 1275-1287
    • Block, B.A.1    O'Brien, J.2    Meissner, G.3
  • 2
    • 0025139194 scopus 로고
    • Molecular Interactions Of The Junctional Foot Protein And Dihydropyridine Receptor In Skeletal Muscle Triads
    • Brandt, N. R., Caswell, A. H., Wen, S. R. And Talvenheimo, J. A. (1990). Molecular Interactions Of The Junctional Foot Protein And Dihydropyridine Receptor In Skeletal Muscle Triads. J. Membr. Biol. 113, 237-251.
    • (1990) J. Membr. Biol. , vol.113 , pp. 237-251
    • Brandt, N.R.1    Caswell, A.H.2    Wen, S.R.3    Talvenheimo, J.A.4
  • 3
    • 0034677672 scopus 로고    scopus 로고
    • A Reassessment Of The Factors Affecting Microtubule Assembly And Disassembly In Vitro
    • Caudron, N., Valiron, O., Usson, Y., Valiron, P. And Job, D. (2000). A Reassessment Of The Factors Affecting Microtubule Assembly And Disassembly In Vitro. J. Mol. Biol. 297, 211-220.
    • (2000) J. Mol. Biol. , vol.297 , pp. 211-220
    • Caudron, N.1    Valiron, O.2    Usson, Y.3    Valiron, P.4    Job, D.5
  • 4
    • 63849206564 scopus 로고    scopus 로고
    • Assembly And Dynamics Of Proteins Of The Longitudinal And Junctional Sarcoplasmic Reticulum In Skeletal Muscle Cells
    • Cusimano, V., Pampinella, F., Giacomello, E. And Sorrentino, V. (2009). Assembly And Dynamics Of Proteins Of The Longitudinal And Junctional Sarcoplasmic Reticulum In Skeletal Muscle Cells. Proc. Natl. Acad. Sci. USA 106, 4695-4700.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 4695-4700
    • Cusimano, V.1    Pampinella, F.2    Giacomello, E.3    Sorrentino, V.4
  • 5
    • 0036112245 scopus 로고    scopus 로고
    • Morphology And Molecular Composition Of Sarcoplasmic Reticulum Surface Junctions In The Absence Of DHPR And Ryr In Mouse Skeletal Muscle
    • Felder, E., Protasi, F., Hirsch, R., Franzini-Armstrong, C. And Allen, P. D. (2002). Morphology And Molecular Composition Of Sarcoplasmic Reticulum Surface Junctions In The Absence Of DHPR And Ryr In Mouse Skeletal Muscle. Biophys. J. 82, 3144- 3149.
    • (2002) Biophys. J. , vol.82 , pp. 3144-3149
    • Felder, E.1    Protasi, F.2    Hirsch, R.3    Franzini-Armstrong, C.4    Allen, P.D.5
  • 6
    • 0026469638 scopus 로고
    • Structural Analysis Of Muscle Development: Transverse Tubules, Sarcoplasmic Reticulum
    • Flucher, B. E. (1992). Structural Analysis Of Muscle Development: Transverse Tubules, Sarcoplasmic Reticulum, And The Triad. Dev. Biol. 154, 245-260.
    • (1992) And The Triad. Dev. Biol. , vol.154 , pp. 245-260
    • Flucher, B.E.1
  • 7
    • 0029842873 scopus 로고    scopus 로고
    • Formation Of Junctions Involved In Excitation-Contraction Coupling In Skeletal And Cardiac Muscle
    • Flucher, B. E. And Franzini-Armstrong, C. (1996). Formation Of Junctions Involved In Excitation-Contraction Coupling In Skeletal And Cardiac Muscle. Proc. Natl. Acad. Sci. USA 93, 8101-8106.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8101-8106
    • Flucher, B.E.1    Franzini-Armstrong, C.2
  • 8
    • 0026518735 scopus 로고
    • Coordinated Development Of Myofibrils, Sarcoplasmic Reticulum And Transverse Tubules In Normal And Dysgenic Mouse Skeletal Muscle
    • Flucher, B. E., Phillips, J. L., Powell, J. A., Andrews, S. B. And Daniels, M. P. (1992). Coordinated Development Of Myofibrils, Sarcoplasmic Reticulum And Transverse Tubules In Normal And Dysgenic Mouse Skeletal Muscle, In Vivo And In Vitro. Dev. Biol. 150, 266-280.
    • (1992) In Vivo And In Vitro. Dev. Biol. , vol.150 , pp. 266-280
    • Flucher, B.E.1    Phillips, J.L.2    Powell, J.A.3    Andrews, S.B.4    Daniels, M.P.5
  • 10
    • 0032934834 scopus 로고    scopus 로고
    • Self-Aggregation Of Triadin In The Sarcoplasmic Reticulum Of Rabbit Skeletal Muscle
    • Froemming, G. R., Murray, B. E. And Ohlendieck, K. (1999). Self-Aggregation Of Triadin In The Sarcoplasmic Reticulum Of Rabbit Skeletal Muscle. Biochim. Biophys. Acta 1418, 197-205.
    • (1999) Biochim. Biophys. Acta , vol.1418 , pp. 197-205
    • Froemming, G.R.1    Murray, B.E.2    Ohlendieck, K.3
  • 11
    • 0343938808 scopus 로고    scopus 로고
    • Microtubule Disruption Modulates Ca(2+) Signaling In Rat Cardiac Myocytes
    • Gómez, A. M., Kerfant, B. G. And Vassort, G. (2000). Microtubule Disruption Modulates Ca(2+) Signaling In Rat Cardiac Myocytes. Circ. Res. 86, 30-36.
    • (2000) Circ. Res. , vol.86 , pp. 30-36
    • Gómez, A.M.1    Kerfant, B.G.2    Vassort, G.3
  • 13
    • 0035802106 scopus 로고    scopus 로고
    • Deficiency Of Triad Junction And Contraction In Mutant Skeletal Muscle Lacking Junctophilin Type 1
    • Ito, K., Komazaki, S., Sasamoto, K., Yoshida, M., Nishi, M., Kitamura, K. And Takeshima, H. (2001). Deficiency Of Triad Junction And Contraction In Mutant Skeletal Muscle Lacking Junctophilin Type 1. J. Cell Biol. 154, 1059-1068.
    • (2001) J. Cell Biol. , vol.154 , pp. 1059-1068
    • Ito, K.1    Komazaki, S.2    Sasamoto, K.3    Yoshida, M.4    Nishi, M.5    Kitamura, K.6    Takeshima, H.7
  • 14
    • 0024992021 scopus 로고
    • Isolation Of A Terminal Cisterna Protein Which May Link The Dihydropyridine Receptor To The Junctional Foot Protein In Skeletal Muscle
    • Kim, K. C., Caswell, A. H., Talvenheimo, J. A. And Brandt, N. R. (1990). Isolation Of A Terminal Cisterna Protein Which May Link The Dihydropyridine Receptor To The Junctional Foot Protein In Skeletal Muscle. Biochemistry 29, 9281-9289.
    • (1990) Biochemistry , vol.29 , pp. 9281-9289
    • Kim, K.C.1    Caswell, A.H.2    Talvenheimo, J.A.3    Brandt, N.R.4
  • 15
    • 0032476663 scopus 로고    scopus 로고
    • A Novel Direct Interaction Of Endoplasmic Reticulum With Microtubules
    • Klopfenstein, D. R., Kappeler, F. And Hauri, H. P. (1998). A Novel Direct Interaction Of Endoplasmic Reticulum With Microtubules. EMBO J. 17, 6168-6177.
    • (1998) EMBO J , vol.17 , pp. 6168-6177
    • Klopfenstein, D.R.1    Kappeler, F.2    Hauri, H.P.3
  • 16
    • 0035844877 scopus 로고    scopus 로고
    • Subdomain-Specific Localization Of CLIMP-63 (P63) In The Endoplasmic Reticulum Is Mediated By Its Luminal Alpha-Helical Segment
    • Klopfenstein, D. R., Klumperman, J., Lustig, A., Kammerer, R. A., Oorschot, V. And Hauri, H. P. (2001). Subdomain-Specific Localization Of CLIMP-63 (P63) In The Endoplasmic Reticulum Is Mediated By Its Luminal Alpha-Helical Segment. J. Cell Biol. 153, 1287-1300.
    • (2001) J. Cell Biol. , vol.153 , pp. 1287-1300
    • Klopfenstein, D.R.1    Klumperman, J.2    Lustig, A.3    Kammerer, R.A.4    Oorschot, V.5    Hauri, H.P.6
  • 17
    • 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, Y. M., Alseikhan, B. A. And Jones, L. R. (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
  • 19
    • 1342282949 scopus 로고    scopus 로고
    • Negatively Charged Amino Acids Within The Intraluminal Loop Of Ryanodine Receptor Are Involved In The Interaction With Triadin
    • Lee, J. M., Rho, S. H., Shin, D. W., Cho, C., Park, W. J., Eom, S. H., Ma, J. And Kim, D. H. (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    Eom, S.H.6    Ma, J.7    Kim, D.H.8
  • 20
    • 0028223232 scopus 로고
    • Intrinsic Microtubule Stability In Interphase Cells
    • Lieuvin, A., Labbé, J. C., Dorée, M. And Job, D. (1994). Intrinsic Microtubule Stability In Interphase Cells. J. Cell Biol. 124, 985-996.
    • (1994) J. Cell Biol. , vol.124 , pp. 985-996
    • Lieuvin, A.1    Labbé, J.C.2    Dorée, M.3    Job, D.4
  • 21
    • 0029762913 scopus 로고    scopus 로고
    • Improving Structural Integrity Of Cryosections For Immunogold Labeling
    • Liou, W., Geuze, H. J. And Slot, J. W. (1996). Improving Structural Integrity Of Cryosections For Immunogold Labeling. Histochem. Cell Biol. 106, 41-58.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3
  • 22
    • 0028289310 scopus 로고
    • Biochemical Evidence For A Complex Involving Dihydropyridine Receptor And Ryanodine Receptor In Triad Junctions Of Skeletal Muscle
    • Marty, I., Robert, M., Villaz, M., De Jongh, K., Lai, Y., Catterall, W. A. And Ronjat, M. (1994). Biochemical Evidence For A Complex Involving Dihydropyridine Receptor And Ryanodine Receptor In Triad Junctions Of Skeletal Muscle. Proc. Natl. Acad. Sci. USA 91, 2270-2274.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2270-2274
    • Marty, I.1    Robert, M.2    Villaz, M.3    De Jongh, K.4    Lai, Y.5    Catterall, W.A.6    Ronjat, M.7
  • 23
    • 0029066367 scopus 로고
    • Localization Of The N-Terminal And C-Terminal Ends Of Triadin With Respect To The Sarcoplasmic Reticulum Membrane Of Rabbit Skeletal Muscle
    • Marty, I., Robert, M., Ronjat, M., Bally, I., Arlaud, G. And Villaz, M. (1995). Localization Of The N-Terminal And C-Terminal Ends Of Triadin With Respect To The Sarcoplasmic Reticulum Membrane Of Rabbit Skeletal Muscle. Biochem. J. 307, 769- 774.
    • (1995) Biochem. J. , vol.307 , pp. 769-774
    • Marty, I.1    Robert, M.2    Ronjat, M.3    Bally, I.4    Arlaud, G.5    Villaz, M.6
  • 29
    • 77954218288 scopus 로고    scopus 로고
    • Further Assembly Required: Construction And Dynamics Of The Endoplasmic Reticulum Network
    • Park, S. H. And Blackstone, C. (2010). Further Assembly Required: Construction And Dynamics Of The Endoplasmic Reticulum Network. EMBO Rep. 11, 515-521.
    • (2010) EMBO Rep , vol.11 , pp. 515-521
    • Park, S.H.1    Blackstone, C.2
  • 31
    • 34247644350 scopus 로고    scopus 로고
    • Ca(2+) Sparks Operated By Membrane Depolarization Require Isoform 3 Ryanodine Receptor Channels In Skeletal Muscle
    • Pouvreau, S., Royer, L., Yi, J., Brum, G., Meissner, G., Ríos, E. And Zhou, J. (2007). Ca(2+) Sparks Operated By Membrane Depolarization Require Isoform 3 Ryanodine Receptor Channels In Skeletal Muscle. Proc. Natl. Acad. Sci. USA 104, 5235-5240.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5235-5240
    • Pouvreau, S.1    Royer, L.2    Yi, J.3    Brum, G.4    Meissner, G.5    Ríos, E.6    Zhou, J.7
  • 33
    • 0033573371 scopus 로고    scopus 로고
    • The Organization Of The Golgi Complex And Microtubules In Skeletal Muscle Is Fiber Type-Dependent
    • Ralston, E., Lu, Z. And Ploug, T. (1999). The Organization Of The Golgi Complex And Microtubules In Skeletal Muscle Is Fiber Type-Dependent. J. Neurosci. 19, 10694- 10705.
    • (1999) J. Neurosci. , vol.19 , pp. 10694-10705
    • Ralston, E.1    Lu, Z.2    Ploug, T.3
  • 38
    • 49649084487 scopus 로고    scopus 로고
    • The Reticulon And DP1/Yop1p Proteins Form Immobile Oligomers In The Tubular Endoplasmic Reticulum
    • Shibata, Y., Voss, C., Rist, J. M., Hu, J., Rapoport, T. A., Prinz, W. A. And Voeltz, G. K. (2008). The Reticulon And DP1/Yop1p Proteins Form Immobile Oligomers In The Tubular Endoplasmic Reticulum. J. Biol. Chem. 283, 18892-18904.
    • (2008) J. Biol. Chem. , vol.283 , pp. 18892-18904
    • Shibata, Y.1    Voss, C.2    Rist, J.M.3    Hu, J.4    Rapoport, T.A.5    Prinz, W.A.6    Voeltz, G.K.7
  • 41
    • 0033636778 scopus 로고    scopus 로고
    • Junctophilins: A Novel Family Of Junctional Membrane Complex Proteins
    • Takeshima, H., Komazaki, S., Nishi, M., Iino, M. And Kangawa, K. (2000). Junctophilins: A Novel Family Of Junctional Membrane Complex Proteins. Mol. Cell 6, 11-22.
    • (2000) Mol. Cell , vol.6 , pp. 11-22
    • Takeshima, H.1    Komazaki, S.2    Nishi, M.3    Iino, M.4    Kangawa, K.5
  • 43
    • 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., Rezgui, S. S., Brocard, J., Chapel, A., Lacampagne, A., Lunardi, J., Dewaard, M. And Marty, I. (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    Rezgui, S.S.3    Brocard, J.4    Chapel, A.5    Lacampagne, A.6    Lunardi, J.7    Dewaard, M.8    Marty, I.9
  • 44
    • 33646409613 scopus 로고    scopus 로고
    • Morphogenesis Of The Endoplasmic Reticulum: Beyond Active Membrane Expansion
    • Vedrenne, C. And Hauri, H. P. (2006). Morphogenesis Of The Endoplasmic Reticulum: Beyond Active Membrane Expansion. Traffic 7, 639-646.
    • (2006) Traffic , vol.7 , pp. 639-646
    • Vedrenne, C.1    Hauri, H.P.2
  • 45
    • 58149110941 scopus 로고    scopus 로고
    • Altered Stored Calcium Release In Skeletal Myotubes Deficient Of Triadin And Junctin
    • Wang, Y., Li, X., Duan, H., Fulton, T. R., Eu, J. P. And Meissner, G. (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    Meissner, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.