메뉴 건너뛰기




Volumn 13, Issue 6, 2012, Pages 869-879

A Centronuclear Myopathy - Dynamin 2 Mutation Impairs Autophagy in Mice

Author keywords

Autophagosome maturation; Dynamin 2; Knock in mouse model; Neonatal autophagy

Indexed keywords

DYNAMIN II; GLYCOGEN;

EID: 84860915944     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2012.01348.x     Document Type: Article
Times cited : (49)

References (40)
  • 1
    • 50249103834 scopus 로고    scopus 로고
    • The cell biology of autophagy in metazoans: a developing story
    • Melendez A, Neufeld TP. The cell biology of autophagy in metazoans: a developing story. Development 2008;135:2347-2360.
    • (2008) Development , vol.135 , pp. 2347-2360
    • Melendez, A.1    Neufeld, T.P.2
  • 2
    • 48249111779 scopus 로고    scopus 로고
    • The role of autophagy in neonatal tissues: just a response to amino acid starvation?
    • Schiaffino S, Mammucari C, Sandri M. The role of autophagy in neonatal tissues: just a response to amino acid starvation?. Autophagy 2008;4:727-730.
    • (2008) Autophagy , vol.4 , pp. 727-730
    • Schiaffino, S.1    Mammucari, C.2    Sandri, M.3
  • 3
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie Z, Klionsky DJ. Autophagosome formation: core machinery and adaptations. Nat Cell Biol 2007;9:1102-1109.
    • (2007) Nat Cell Biol , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 4
    • 33750974189 scopus 로고    scopus 로고
    • Endoplasmic reticulum and Golgi complex: contributions to, and turnover by, autophagy
    • Mijaljica D, Prescott M, Devenish RJ. Endoplasmic reticulum and Golgi complex: contributions to, and turnover by, autophagy. Traffic 2006;7:1590-1595.
    • (2006) Traffic , vol.7 , pp. 1590-1595
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 5
    • 77954197767 scopus 로고    scopus 로고
    • Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae
    • van der Vaart A, Griffith J, Reggiori F. Exit from the Golgi is required for the expansion of the autophagosomal phagophore in yeast Saccharomyces cerevisiae. Mol Biol Cell 2010;21:2270-2284.
    • (2010) Mol Biol Cell , vol.21 , pp. 2270-2284
    • van der Vaart, A.1    Griffith, J.2    Reggiori, F.3
  • 7
    • 77955131007 scopus 로고    scopus 로고
    • Plasma membrane contributes to the formation of pre-autophagosomal structures
    • Ravikumar B, Moreau K, Jahreiss L, Puri C, Rubinsztein DC. Plasma membrane contributes to the formation of pre-autophagosomal structures. Nat Cell Biol 2010;12:747-757.
    • (2010) Nat Cell Biol , vol.12 , pp. 747-757
    • Ravikumar, B.1    Moreau, K.2    Jahreiss, L.3    Puri, C.4    Rubinsztein, D.C.5
  • 8
    • 26844531363 scopus 로고    scopus 로고
    • Maturation of autophagic vacuoles in mammalian cells
    • Eskelinen EL. Maturation of autophagic vacuoles in mammalian cells. Autophagy 2005;1:1-10.
    • (2005) Autophagy , vol.1 , pp. 1-10
    • Eskelinen, E.L.1
  • 9
    • 33846010776 scopus 로고    scopus 로고
    • Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes
    • Fass E, Shvets E, Degani I, Hirschberg K, Elazar Z. Microtubules support production of starvation-induced autophagosomes but not their targeting and fusion with lysosomes. J Biol Chem 2006;281:36303-36316.
    • (2006) J Biol Chem , vol.281 , pp. 36303-36316
    • Fass, E.1    Shvets, E.2    Degani, I.3    Hirschberg, K.4    Elazar, Z.5
  • 10
    • 33645120442 scopus 로고    scopus 로고
    • Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes
    • Kochl R, Hu XW, Chan EY, Tooze SA. Microtubules facilitate autophagosome formation and fusion of autophagosomes with endosomes. Traffic 2006;7:129-145.
    • (2006) Traffic , vol.7 , pp. 129-145
    • Kochl, R.1    Hu, X.W.2    Chan, E.Y.3    Tooze, S.A.4
  • 15
    • 0030668143 scopus 로고    scopus 로고
    • Ubiquitously expressed dynamin-II has a higher intrinsic GTPase activity and a greater propensity for self-assembly than neuronal dynamin-I
    • Warnock DE, Baba T, Schmid SL. Ubiquitously expressed dynamin-II has a higher intrinsic GTPase activity and a greater propensity for self-assembly than neuronal dynamin-I. Mol Biol Cell 1997;8:2553-2562.
    • (1997) Mol Biol Cell , vol.8 , pp. 2553-2562
    • Warnock, D.E.1    Baba, T.2    Schmid, S.L.3
  • 17
    • 0036153898 scopus 로고    scopus 로고
    • Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles
    • van Dam EM, Stoorvogel W. Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles. Mol Biol Cell 2002;13:169-182.
    • (2002) Mol Biol Cell , vol.13 , pp. 169-182
    • van Dam, E.M.1    Stoorvogel, W.2
  • 18
    • 0033995518 scopus 로고    scopus 로고
    • Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor
    • Nicoziani P, Vilhardt F, Llorente A, Hilout L, Courtoy PJ, Sandvig K, van Deurs B. Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor. Mol Biol Cell 2000;11:481-495.
    • (2000) Mol Biol Cell , vol.11 , pp. 481-495
    • Nicoziani, P.1    Vilhardt, F.2    Llorente, A.3    Hilout, L.4    Courtoy, P.J.5    Sandvig, K.6    van Deurs, B.7
  • 19
    • 0032559342 scopus 로고    scopus 로고
    • Role of dynamin in the formation of transport vesicles from the trans-Golgi network
    • Jones SM, Howell KE, Henley JR, Cao H, McNiven MA. Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science 1998;279:573-577.
    • (1998) Science , vol.279 , pp. 573-577
    • Jones, S.M.1    Howell, K.E.2    Henley, J.R.3    Cao, H.4    McNiven, M.A.5
  • 21
    • 77954906120 scopus 로고    scopus 로고
    • Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers
    • Wang L, Barylko B, Byers C, Ross JA, Jameson DM, Albanesi JP. Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers. J Biol Chem 2010;285:22753-22757.
    • (2010) J Biol Chem , vol.285 , pp. 22753-22757
    • Wang, L.1    Barylko, B.2    Byers, C.3    Ross, J.A.4    Jameson, D.M.5    Albanesi, J.P.6
  • 26
    • 77955708390 scopus 로고    scopus 로고
    • Overview of macroautophagy regulation in mammalian cells
    • Mehrpour M, Esclatine A, Beau I, Codogno P. Overview of macroautophagy regulation in mammalian cells. Cell Res 2010;20:748-762.
    • (2010) Cell Res , vol.20 , pp. 748-762
    • Mehrpour, M.1    Esclatine, A.2    Beau, I.3    Codogno, P.4
  • 27
    • 0026672734 scopus 로고
    • Second messengers regulate endosomal acidification in Swiss 3T3 fibroblasts
    • Zen K, Biwersi J, Periasamy N, Verkman AS. Second messengers regulate endosomal acidification in Swiss 3T3 fibroblasts. J Cell Biol 1992;119:99-110.
    • (1992) J Cell Biol , vol.119 , pp. 99-110
    • Zen, K.1    Biwersi, J.2    Periasamy, N.3    Verkman, A.S.4
  • 28
    • 0019906301 scopus 로고
    • Intralysosomal accumulation of polyanions. II. Polyanion internalization and its influence on lysosomal pH and membrane fluidity
    • Kielian MC, Cohn ZA. Intralysosomal accumulation of polyanions. II. Polyanion internalization and its influence on lysosomal pH and membrane fluidity. J Cell Biol 1982;93:875-882.
    • (1982) J Cell Biol , vol.93 , pp. 875-882
    • Kielian, M.C.1    Cohn, Z.A.2
  • 30
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends C, Sowa ME, Gygi SP, Harper JW. Network organization of the human autophagy system. Nature 2010;466:68-76.
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 31
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation
    • Polson HE, de Lartigue J, Rigden DJ, Reedijk M, Urbe S, Clague MJ, Tooze SA. Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation. Autophagy 2010;6:506-522.
    • (2010) Autophagy , vol.6 , pp. 506-522
    • Polson, H.E.1    de Lartigue, J.2    Rigden, D.J.3    Reedijk, M.4    Urbe, S.5    Clague, M.J.6    Tooze, S.A.7
  • 32
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk VI, Menzies FM, Rubinsztein DC. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett 2010;584:1393-1398.
    • (2010) FEBS Lett , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 33
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk VI, Mansilla A, Menzies FM, Rubinsztein DC. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 2009;33:517-527.
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 36
    • 77954164144 scopus 로고    scopus 로고
    • Zebrafish MTMR14 is required for excitation-contraction coupling, developmental motor function and the regulation of autophagy
    • Dowling JJ, Low SE, Busta AS, Feldman EL. Zebrafish MTMR14 is required for excitation-contraction coupling, developmental motor function and the regulation of autophagy. Hum Mol Genet 2010;19:2668-2681.
    • (2010) Hum Mol Genet , vol.19 , pp. 2668-2681
    • Dowling, J.J.1    Low, S.E.2    Busta, A.S.3    Feldman, E.L.4
  • 37
    • 34249912645 scopus 로고    scopus 로고
    • Regulation of ubiquitin-proteasome system, caspase enzyme activities, and extracellular proteinases in rat soleus muscle in response to unloading
    • Berthon P, Duguez S, Favier FB, Amirouche A, Feasson L, Vico L, Denis C, Freyssenet D. Regulation of ubiquitin-proteasome system, caspase enzyme activities, and extracellular proteinases in rat soleus muscle in response to unloading. Pflugers Arch 2007;454:625-633.
    • (2007) Pflugers Arch , vol.454 , pp. 625-633
    • Berthon, P.1    Duguez, S.2    Favier, F.B.3    Amirouche, A.4    Feasson, L.5    Vico, L.6    Denis, C.7    Freyssenet, D.8
  • 38
    • 0038339517 scopus 로고    scopus 로고
    • Myogenic and nonmyogenic cells differentially express proteinases, Hsc/Hsp70, and BAG-1 during skeletal muscle regeneration
    • Duguez S, Bihan MC, Gouttefangeas D, Feasson L, Freyssenet D. Myogenic and nonmyogenic cells differentially express proteinases, Hsc/Hsp70, and BAG-1 during skeletal muscle regeneration. Am J Physiol Endocrinol Metab 2003;285:E206-E215.
    • (2003) Am J Physiol Endocrinol Metab , vol.285
    • Duguez, S.1    Bihan, M.C.2    Gouttefangeas, D.3    Feasson, L.4    Freyssenet, D.5
  • 40
    • 0021895138 scopus 로고
    • A new generation of Ca2+ indicators with greatly improved fluorescence properties
    • Grynkiewicz G, Poenie M, Tsien RY. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J Biol Chem 1985;260:3440-3450.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.