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Volumn 23, Issue 22, 2014, Pages 5961-5975

Golgi fragmentation in pmn mice is due to a defective ARF1/TBCE cross-talk that coordinates COPI vesicle formation and tubulin polymerization

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; ALPHA TUBULIN; BETA TUBULIN; COAT PROTEIN COMPLEX I; PROTEIN; TUBULIN BINDING COFACTOR E PROTEIN; UNCLASSIFIED DRUG; CHAPERONE; TBCE PROTEIN, MOUSE; TUBULIN;

EID: 84911382750     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddu320     Document Type: Article
Times cited : (35)

References (61)
  • 1
    • 0842324801 scopus 로고    scopus 로고
    • The mechanisms of vesicle budding and fusion
    • Bonifacino, J.S. and Glick, B.S. (2004) The mechanisms of vesicle budding and fusion. Cell, 116, 153-166.
    • (2004) Cell , vol.116 , pp. 153-166
    • Bonifacino, J.S.1    Glick, B.S.2
  • 4
    • 0029890685 scopus 로고    scopus 로고
    • The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu,Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease
    • Mourelatos, Z., Gonatas, N.K., Stieber, A., Gurney, M.E. and Dal Canto, M.C. (1996) The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu,Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease. Proc. Natl. Acad. Sci. U.S.A., 93, 5472-5477.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5472-5477
    • Mourelatos, Z.1    Gonatas, N.K.2    Stieber, A.3    Gurney, M.E.4    Dal Canto, M.C.5
  • 5
    • 0022412716 scopus 로고
    • Microtubules and the organization of the Golgi complex
    • Thyberg, J. and Moskalewski, S. (1985) Microtubules and the organization of the Golgi complex. Exp. Cell Res., 159, 1-16.
    • (1985) Exp. Cell Res. , vol.159 , pp. 1-16
    • Thyberg, J.1    Moskalewski, S.2
  • 6
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole, N.B., Sciaky, N., Marotta, A., Song, J. and Lippincott-Schwartz, J. (1996) Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol. Biol. Cell, 7, 631-650.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 7
    • 0023019044 scopus 로고
    • Amicrotubule-binding protein associated with membranes of the Golgi apparatus
    • Allan, V.J. and Kreis, T.E. (1986)Amicrotubule-binding protein associated with membranes of the Golgi apparatus. J. Cell Biol., 103, 2229-2239.
    • (1986) J. Cell Biol. , vol.103 , pp. 2229-2239
    • Allan, V.J.1    Kreis, T.E.2
  • 8
    • 7244239105 scopus 로고    scopus 로고
    • Dysregulation of stathmin, a microtubuledestabilizing protein, and up-regulation of Hsp25, Hsp27, and the antioxidant peroxiredoxin 6 in a mouse model of familial amyotrophic lateral sclerosis
    • Strey, C.W., Spellman, D., Stieber, A., Gonatas, J.O., Wang, X., Lambris, J.D. and Gonatas, N.K. (2004) Dysregulation of stathmin, a microtubuledestabilizing protein, and up-regulation of Hsp25, Hsp27, and the antioxidant peroxiredoxin 6 in a mouse model of familial amyotrophic lateral sclerosis. Am. J. Pathol., 165, 1701-1718.
    • (2004) Am. J. Pathol. , vol.165 , pp. 1701-1718
    • Strey, C.W.1    Spellman, D.2    Stieber, A.3    Gonatas, J.O.4    Wang, X.5    Lambris, J.D.6    Gonatas, N.K.7
  • 9
    • 29444443348 scopus 로고    scopus 로고
    • Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis
    • Urushitani, M., Sik, A., Sakurai, T., Nukina, N., Takahashi, R. and Julien, J.P. (2006) Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis. Nat. Neurosci., 9, 108-118.
    • (2006) Nat. Neurosci. , vol.9 , pp. 108-118
    • Urushitani, M.1    Sik, A.2    Sakurai, T.3    Nukina, N.4    Takahashi, R.5    Julien, J.P.6
  • 11
    • 1642528556 scopus 로고    scopus 로고
    • Disruption of the structure of the Golgi apparatus and the function of the secretory pathway by mutants G93A and G85R of Cu, Zn superoxide dismutase (SOD1) of familial amyotrophic lateral sclerosis
    • Stieber, A., Gonatas, J.O., Moore, J.S., Bantly, A., Yim, H.S., Yim, M.B. and Gonatas, N.K. (2004) Disruption of the structure of the Golgi apparatus and the function of the secretory pathway by mutants G93A and G85R of Cu, Zn superoxide dismutase (SOD1) of familial amyotrophic lateral sclerosis. J. Neurol. Sci., 219, 45-53.
    • (2004) J. Neurol. Sci. , vol.219 , pp. 45-53
    • Stieber, A.1    Gonatas, J.O.2    Moore, J.S.3    Bantly, A.4    Yim, H.S.5    Yim, M.B.6    Gonatas, N.K.7
  • 15
    • 0037175395 scopus 로고    scopus 로고
    • Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease
    • Bömmel, H., Xie, G., Rossoll, W., Wiese, S., Jablonka, S., Boehm, T. and Sendtner, M. (2002) Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease. J. Cell Biol., 159, 563-569.
    • (2002) J. Cell Biol. , vol.159 , pp. 563-569
    • Bömmel, H.1    Xie, G.2    Rossoll, W.3    Wiese, S.4    Jablonka, S.5    Boehm, T.6    Sendtner, M.7
  • 17
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    • Tian, G., Lewis, S.A., Feierbach, B., Stearns, T., Rommelaere, H., Ampe, C. and Cowan, N.J. (1997) Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. J. Cell Biol., 138, 821-832.
    • (1997) J. Cell Biol. , vol.138 , pp. 821-832
    • Tian, G.1    Lewis, S.A.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5    Ampe, C.6    Cowan, N.J.7
  • 18
    • 34548081175 scopus 로고    scopus 로고
    • Progressive motor neuronopathy: a critical role of the tubulin chaperone TBCE in axonal tubulin routing from the Golgi apparatus
    • Schaefer, M.K., Schmalbruch, H., Buhler, E., Lopez, C., Martin, N., Guenet, J.L. and Haase, G. (2007) Progressive motor neuronopathy: a critical role of the tubulin chaperone TBCE in axonal tubulin routing from the Golgi apparatus. J. Neurosci., 27, 8779-8789.
    • (2007) J. Neurosci. , vol.27 , pp. 8779-8789
    • Schaefer, M.K.1    Schmalbruch, H.2    Buhler, E.3    Lopez, C.4    Martin, N.5    Guenet, J.L.6    Haase, G.7
  • 20
    • 0030953519 scopus 로고    scopus 로고
    • Gene therapy of murine motor neuron disease using adenoviral vectors for neurotrophic factors
    • Haase, G., Kennel, P., Pettmann, B., Vigne, E., Akli, S., Revah, F., Schmalbruch, H. and Kahn, A. (1997) Gene therapy of murine motor neuron disease using adenoviral vectors for neurotrophic factors. Nat. Med., 3, 429-436.
    • (1997) Nat. Med. , vol.3 , pp. 429-436
    • Haase, G.1    Kennel, P.2    Pettmann, B.3    Vigne, E.4    Akli, S.5    Revah, F.6    Schmalbruch, H.7    Kahn, A.8
  • 21
    • 34547591790 scopus 로고    scopus 로고
    • Active ADP-ribosylation factor-1 (ARF1) is required for mitotic Golgi fragmentation
    • Xiang, Y., Seemann, J., Bisel, B., Punthambaker, S. and Wang, Y. (2007) Active ADP-ribosylation factor-1 (ARF1) is required for mitotic Golgi fragmentation. J. Biol. Chem., 282, 21829-21837.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21829-21837
    • Xiang, Y.1    Seemann, J.2    Bisel, B.3    Punthambaker, S.4    Wang, Y.5
  • 22
    • 51349135435 scopus 로고    scopus 로고
    • Coat-tether interaction in Golgi organization
    • Guo, Y., Punj, V., Sengupta, D. and Linstedt, A.D. (2008) Coat-tether interaction in Golgi organization. Mol. Biol. Cell, 19, 2830-2843.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2830-2843
    • Guo, Y.1    Punj, V.2    Sengupta, D.3    Linstedt, A.D.4
  • 23
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura, N., Lowe, M., Levine, T.P., Rabouille, C. and Warren, G. (1997) The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell, 89, 445-455.
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 24
    • 65349155174 scopus 로고    scopus 로고
    • Early endosomes and endosomal coatomer are required for autophagy
    • Razi, M., Chan, E.Y. and Tooze, S.A. (2009) Early endosomes and endosomal coatomer are required for autophagy. J. Cell Biol., 185, 305-321.
    • (2009) J. Cell Biol. , vol.185 , pp. 305-321
    • Razi, M.1    Chan, E.Y.2    Tooze, S.A.3
  • 25
    • 11244273061 scopus 로고    scopus 로고
    • Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment
    • Xu, D. and Hay, J.C. (2004) Reconstitution of COPII vesicle fusion to generate a pre-Golgi intermediate compartment. J. Cell. Biol., 167, 997-1003.
    • (2004) J. Cell. Biol. , vol.167 , pp. 997-1003
    • Xu, D.1    Hay, J.C.2
  • 26
    • 0037113095 scopus 로고    scopus 로고
    • Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC)
    • Horstmann, H., Ng, C.P., Tang, B.L. and Hong, W. (2002) Ultrastructural characterization of endoplasmic reticulum-Golgi transport containers (EGTC). J. Cell. Sci., 115, 4263-4273.
    • (2002) J. Cell. Sci. , vol.115 , pp. 4263-4273
    • Horstmann, H.1    Ng, C.P.2    Tang, B.L.3    Hong, W.4
  • 27
    • 47249163819 scopus 로고    scopus 로고
    • Depletion of beta-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1
    • Styers, M.L., O'Connor, A.K., Grabski, R., Cormet-Boyaka, E. and Sztul, E. (2008) Depletion of beta-COP reveals a role for COP-I in compartmentalization of secretory compartments and in biosynthetic transport of caveolin-1. Am. J. Physiol. Cell. Physiol., 294, C1485-C1498.
    • (2008) Am. J. Physiol. Cell. Physiol. , vol.294 , pp. C1485-C1498
    • Styers, M.L.1    O'Connor, A.K.2    Grabski, R.3    Cormet-Boyaka, E.4    Sztul, E.5
  • 28
    • 33845991859 scopus 로고    scopus 로고
    • SNAREstatus regulates tether recruitment and function in homotypic COPII vesicle fusion
    • Bentley, M., Liang, Y., Mullen, K., Xu, D., Sztul, E. and Hay, J.C. (2006) SNAREstatus regulates tether recruitment and function in homotypic COPII vesicle fusion. J. Biol. Chem., 281, 38825-38833.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38825-38833
    • Bentley, M.1    Liang, Y.2    Mullen, K.3    Xu, D.4    Sztul, E.5    Hay, J.C.6
  • 29
    • 15844394630 scopus 로고    scopus 로고
    • GS28, a 28-kilodalton GolgiSNAREthat participates in ER-Golgi transport
    • Subramaniam, V.N., Peter, F., Philp, R., Wong, S.H. and Hong, W. (1996) GS28, a 28-kilodalton GolgiSNAREthat participates in ER-Golgi transport. Science, 272, 1161-1163.
    • (1996) Science , vol.272 , pp. 1161-1163
    • Subramaniam, V.N.1    Peter, F.2    Philp, R.3    Wong, S.H.4    Hong, W.5
  • 30
    • 1842297531 scopus 로고    scopus 로고
    • GS15, a 15-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) homologous to rbet1
    • Xu, Y., Wong, S.H., Zhang, T., Subramaniam, V.N. and Hong, W. (1997) GS15, a 15-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) homologous to rbet1. J. Biol. Chem., 272, 20162-20166.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20162-20166
    • Xu, Y.1    Wong, S.H.2    Zhang, T.3    Subramaniam, V.N.4    Hong, W.5
  • 31
    • 0031808667 scopus 로고    scopus 로고
    • Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p
    • Ballensiefen, W., Ossipov, D. and Schmitt, H.D. (1998) Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p. J. Cell. Sci., 111, 1507-1520.
    • (1998) J. Cell. Sci. , vol.111 , pp. 1507-1520
    • Ballensiefen, W.1    Ossipov, D.2    Schmitt, H.D.3
  • 32
    • 0037193471 scopus 로고    scopus 로고
    • ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • Rein, U., Andag, U., Duden, R., Schmitt, H.D. and Spang, A. (2002) ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. J. Cell Biol., 157, 395-404.
    • (2002) J. Cell Biol. , vol.157 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 33
    • 0032989978 scopus 로고    scopus 로고
    • Therapeutic benefit of ciliary neurotrophic factor in progressive motor neuronopathy depends on the route of delivery
    • Haase, G., Pettmann, B., Bordet, T., Villa, P., Vigne, E., Schmalbruch, H. and Kahn, A. (1999) Therapeutic benefit of ciliary neurotrophic factor in progressive motor neuronopathy depends on the route of delivery. Ann. Neurol., 45, 296-304.
    • (1999) Ann. Neurol. , vol.45 , pp. 296-304
    • Haase, G.1    Pettmann, B.2    Bordet, T.3    Villa, P.4    Vigne, E.5    Schmalbruch, H.6    Kahn, A.7
  • 36
    • 69949178740 scopus 로고    scopus 로고
    • Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells
    • Miller, P.M., Folkmann, A.W., Maia, A.R., Efimova, N., Efimov, A. and Kaverina, I. (2009) Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells. Nat. Cell Biol., 11, 1069-1080.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1069-1080
    • Miller, P.M.1    Folkmann, A.W.2    Maia, A.R.3    Efimova, N.4    Efimov, A.5    Kaverina, I.6
  • 37
    • 0025094169 scopus 로고
    • Spatial and temporal colocalization of the Golgi apparatus and microtubules rich in detyrosinated tubulin
    • Skoufias, D.A., Burgess, T.L. and Wilson, L. (1990) Spatial and temporal colocalization of the Golgi apparatus and microtubules rich in detyrosinated tubulin. J. Cell Biol., 111, 1929-1937.
    • (1990) J. Cell Biol. , vol.111 , pp. 1929-1937
    • Skoufias, D.A.1    Burgess, T.L.2    Wilson, L.3
  • 39
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes beta-actin folding
    • Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H. and Cowan, N.J. (1992) A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell, 69, 1043-1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 40
    • 0033588020 scopus 로고    scopus 로고
    • Tubulin folding cofactors as GTPase-activating proteins GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer.
    • Tian, G., Bhamidipati, A., Cowan, N.J. and Lewis, S.A. (1999) Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer. J. Biol. Chem., 274, 24054-24058.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24054-24058
    • Tian, G.1    Bhamidipati, A.2    Cowan, N.J.3    Lewis, S.A.4
  • 41
    • 41649093538 scopus 로고    scopus 로고
    • A pachygyria-causing alpha-tubulin mutation results in inefficient cycling withCCTand a deficient interaction withTBCB.Mol
    • Tian, G., Kong, X.P., Jaglin, X.H., Chelly, J., Keays, D. and Cowan, N.J. (2008) A pachygyria-causing alpha-tubulin mutation results in inefficient cycling withCCTand a deficient interaction withTBCB.Mol. Biol. Cell., 19, 1152-1161.
    • (2008) Biol. Cell. , vol.19 , pp. 1152-1161
    • Tian, G.1    Kong, X.P.2    Jaglin, X.H.3    Chelly, J.4    Keays, D.5    Cowan, N.J.6
  • 42
    • 0034729382 scopus 로고    scopus 로고
    • ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin
    • Bhamidipati, A., Lewis, S.A. and Cowan, N.J. (2000) ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. J. Cell Biol., 149, 1087-1096.
    • (2000) J. Cell Biol. , vol.149 , pp. 1087-1096
    • Bhamidipati, A.1    Lewis, S.A.2    Cowan, N.J.3
  • 43
    • 12344277564 scopus 로고    scopus 로고
    • Coupling of ER exit to microtubules through direct interaction of COPII with dynactin
    • Watson, P., Forster, R., Palmer, K.J., Pepperkok, R. and Stephens, D.J. (2005) Coupling of ER exit to microtubules through direct interaction of COPII with dynactin. Nat. Cell Biol., 7, 48-55.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 48-55
    • Watson, P.1    Forster, R.2    Palmer, K.J.3    Pepperkok, R.4    Stephens, D.J.5
  • 44
    • 3042548289 scopus 로고    scopus 로고
    • Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network
    • Carreno, S., Engqvist-Goldstein, A.E., Zhang, C.X., McDonald, K.L. and Drubin, D.G. (2004) Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network. J. Cell Biol., 165, 781-788.
    • (2004) J. Cell Biol. , vol.165 , pp. 781-788
    • Carreno, S.1    Engqvist-Goldstein, A.E.2    Zhang, C.X.3    McDonald, K.L.4    Drubin, D.G.5
  • 45
    • 77950520993 scopus 로고    scopus 로고
    • Protein complexes containing CYFIP/Sra/PIR121 coordinate Arf1 and Rac1 signalling during clathrin-AP-1-coated carrier biogenesis at the TGN
    • Anitei, M., Stange, C., Parshina, I., Baust, T., Schenck, A., Raposo, G., Kirchhausen, T. and Hoflack, B. (2010) Protein complexes containing CYFIP/Sra/PIR121 coordinate Arf1 and Rac1 signalling during clathrin-AP-1-coated carrier biogenesis at the TGN. Nat. Cell Biol., 12, 330-340.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 330-340
    • Anitei, M.1    Stange, C.2    Parshina, I.3    Baust, T.4    Schenck, A.5    Raposo, G.6    Kirchhausen, T.7    Hoflack, B.8
  • 47
    • 0001417555 scopus 로고    scopus 로고
    • GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28
    • Sagiv, Y., Legesse-Miller, A., Porat, A. and Elazar, Z. (2000) GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28. EMBO J., 19, 1494-1504.
    • (2000) EMBO J. , vol.19 , pp. 1494-1504
    • Sagiv, Y.1    Legesse-Miller, A.2    Porat, A.3    Elazar, Z.4
  • 48
    • 80051788343 scopus 로고    scopus 로고
    • OSBP-related protein 7 interacts with GATE-16 and negatively regulates GS28 protein stability
    • Zhong, W., Zhou, Y., Li, S., Zhou, T., Ma, H., Wei, K., Li, H., Olkkonen, V.M. and Yan, D. (2011) OSBP-related protein 7 interacts with GATE-16 and negatively regulates GS28 protein stability. Exp. Cell Res., 317, 2353-2363.
    • (2011) Exp. Cell Res. , vol.317 , pp. 2353-2363
    • Zhong, W.1    Zhou, Y.2    Li, S.3    Zhou, T.4    Ma, H.5    Wei, K.6    Li, H.7    Olkkonen, V.M.8    Yan, D.9
  • 50
    • 77953234920 scopus 로고    scopus 로고
    • Mutation in archain 1, a subunit ofCOPIcoatomer complex, causes diluted coat color and Purkinje cell degeneration
    • Xu, X., Kedlaya, R., Higuchi, H., Ikeda, S., Justice, M.J., Setaluri, V. and Ikeda, A. (2010) Mutation in archain 1, a subunit ofCOPIcoatomer complex, causes diluted coat color and Purkinje cell degeneration. PLoS Genet., 6, e1000956.
    • (2010) PLoS Genet. , vol.6 , pp. e1000956
    • Xu, X.1    Kedlaya, R.2    Higuchi, H.3    Ikeda, S.4    Justice, M.J.5    Setaluri, V.6    Ikeda, A.7
  • 51
    • 0028829638 scopus 로고
    • The mouse mutation muscle deficient (mdf) is characterized by a progressive motoneuron disease
    • Blot, S., Poirier, C. and Dreyfus, P.A. (1995) The mouse mutation muscle deficient (mdf) is characterized by a progressive motoneuron disease. J. Neuropathol. Exp. Neurol., 54, 812-825.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 812-825
    • Blot, S.1    Poirier, C.2    Dreyfus, P.A.3
  • 53
    • 84870014632 scopus 로고    scopus 로고
    • An early onset progressive motor neuron disorder in Scyl1-deficient mice is associated with mislocalization of TDP-43
    • Pelletier, S., Gingras, S., Howell, S., Vogel, P. and Ihle, J.N. (2012) An early onset progressive motor neuron disorder in Scyl1-deficient mice is associated with mislocalization of TDP-43. J. Neurosci, 32, 16560-16573.
    • (2012) J. Neurosci , vol.32 , pp. 16560-16573
    • Pelletier, S.1    Gingras, S.2    Howell, S.3    Vogel, P.4    Ihle, J.N.5
  • 54
    • 0030690116 scopus 로고    scopus 로고
    • Inhibition of axonal growth by brefeldin A in hippocampal neurons in culture
    • Jareb, M. and Banker, G. (1997) Inhibition of axonal growth by brefeldin A in hippocampal neurons in culture. J. Neurosci., 17, 8955-8963.
    • (1997) J. Neurosci. , vol.17 , pp. 8955-8963
    • Jareb, M.1    Banker, G.2
  • 56
    • 84871267501 scopus 로고    scopus 로고
    • The spinal muscular atrophy disease protein SMN is linked to the Golgi network
    • Ting, C.H., Wen, H.L., Liu, H.C., Hsieh-Li, H.M., Li, H. and Lin-Chao, S. (2012) The spinal muscular atrophy disease protein SMN is linked to the Golgi network. PLoS One, 7, e51826.
    • (2012) PLoS One , vol.7
    • Ting, C.H.1    Wen, H.L.2    Liu, H.C.3    Hsieh-Li, H.M.4    Li, H.5    Lin-Chao, S.6
  • 57
    • 84884709045 scopus 로고    scopus 로고
    • Dilysine motifs in exon 2b of SMN protein mediate binding to the COPI vesicle protein alpha-COP and neurite outgrowth in a cell culture model of spinal muscular atrophy
    • Custer, S.K., Todd, A.G., Singh, N.N. and Androphy, E.J. (2013) Dilysine motifs in exon 2b of SMN protein mediate binding to the COPI vesicle protein alpha-COP and neurite outgrowth in a cell culture model of spinal muscular atrophy. Hum. Mol. Genet., 22, 4043-4052.
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 4043-4052
    • Custer, S.K.1    Todd, A.G.2    Singh, N.N.3    Androphy, E.J.4
  • 58
    • 35348913641 scopus 로고    scopus 로고
    • Copb1-facilitated axonal transport and translation of kappa opioid-receptor mRNA
    • Bi, J., Tsai, N.P., Lu, H.Y., Loh, H.H. and Wei, L.N. (2007) Copb1-facilitated axonal transport and translation of kappa opioid-receptor mRNA. Proc. Natl. Acad. Sci. U.S.A., 104, 13810-13815.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 13810-13815
    • Bi, J.1    Tsai, N.P.2    Lu, H.Y.3    Loh, H.H.4    Wei, L.N.5
  • 59
    • 84873034506 scopus 로고    scopus 로고
    • COPI transport complexes bind to specific RNAs in neuronal cells
    • Todd, A.G., Lin, H., Ebert, A.D., Liu, Y. and Androphy, E.J. (2013) COPI transport complexes bind to specific RNAs in neuronal cells. Hum. Mol. Genet., 22, 729-736.
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 729-736
    • Todd, A.G.1    Lin, H.2    Ebert, A.D.3    Liu, Y.4    Androphy, E.J.5
  • 60
    • 33344462702 scopus 로고    scopus 로고
    • Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF
    • Pun, S., Santos, A.F., Saxena, S., Xu, L. and Caroni, P. (2006) Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF. Nat. Neurosci., 9, 408-419.
    • (2006) Nat. Neurosci. , vol.9 , pp. 408-419
    • Pun, S.1    Santos, A.F.2    Saxena, S.3    Xu, L.4    Caroni, P.5
  • 61
    • 80053958802 scopus 로고    scopus 로고
    • SMN requirement for synaptic vesicle, active zone and microtubule postnatal organization in motor nerve terminals
    • Torres-Benito, L., Neher, M.F., Cano, R., Ruiz, R. and Tabares, L. (2011) SMN requirement for synaptic vesicle, active zone and microtubule postnatal organization in motor nerve terminals. PLoS One, 6, e26164.
    • (2011) PLoS One , vol.6
    • Torres-Benito, L.1    Neher, M.F.2    Cano, R.3    Ruiz, R.4    Tabares, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.