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Volumn 6, Issue 1, 2011, Pages

The cytoskeletal protein Ndel1 regulates Dynamin 2 GTPase activity

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; DYNAMIN II; GLUTAMATE RECEPTOR 1; GUANOSINE TRIPHOSPHATASE; PROTEIN NDEL1; UNCLASSIFIED DRUG; AMPA RECEPTOR; CARRIER PROTEIN; GLUTAMATE RECEPTOR IONOTROPIC, AMPA 1; NDEL1 PROTEIN, HUMAN;

EID: 79551557180     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0014583     Document Type: Article
Times cited : (5)

References (61)
  • 1
    • 3242706075 scopus 로고    scopus 로고
    • A NUDEL-dependent mechanism of neurofilament assembly regulates the integrity of CNS neurons
    • Nguyen MD, Shu T, Sanada K, Lariviere RC, Tseng HC, et al. (2004) A NUDEL-dependent mechanism of neurofilament assembly regulates the integrity of CNS neurons. Nat Cell Biol 6: 595-608.
    • (2004) Nat Cell Biol , vol.6 , pp. 595-608
    • Nguyen, M.D.1    Shu, T.2    Sanada, K.3    Lariviere, R.C.4    Tseng, H.C.5
  • 2
    • 0034520636 scopus 로고    scopus 로고
    • NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein
    • Niethammer M, Smith DS, Ayala R, Peng J, Ko J, et al. (2000) NUDEL is a novel Cdk5 substrate that associates with LIS1 and cytoplasmic dynein. Neuron 28: 697-711.
    • (2000) Neuron , vol.28 , pp. 697-711
    • Niethammer, M.1    Smith, D.S.2    Ayala, R.3    Peng, J.4    Ko, J.5
  • 3
    • 0034520597 scopus 로고    scopus 로고
    • A LIS1/ NUDEL/cytoplasmic dynein heavy chain complex in the developing and adult nervous system
    • Sasaki S, Shionoya A, Ishida M, Gambello MJ, Yingling J, et al. (2000) A LIS1/ NUDEL/cytoplasmic dynein heavy chain complex in the developing and adult nervous system. Neuron 28: 681-696.
    • (2000) Neuron , vol.28 , pp. 681-696
    • Sasaki, S.1    Shionoya, A.2    Ishida, M.3    Gambello, M.J.4    Yingling, J.5
  • 4
    • 45549102674 scopus 로고    scopus 로고
    • Ndel1 controls the dynein-mediated transport of vimentin during neurite outgrowth
    • Shim SY, Samuels BA, Wang J, Neumayer G, Belzil C, et al. (2008) Ndel1 controls the dynein-mediated transport of vimentin during neurite outgrowth. J Biol Chem 283: 12232-12240.
    • (2008) J Biol Chem , vol.283 , pp. 12232-12240
    • Shim, S.Y.1    Samuels, B.A.2    Wang, J.3    Neumayer, G.4    Belzil, C.5
  • 5
    • 75649100553 scopus 로고    scopus 로고
    • Ndel1 palmitoylation: A new mean to regulate cytoplasmic dynein activity
    • Shmueli A, Segal M, Sapir T, Tsutsumi R, Noritake J, et al. (2010) Ndel1 palmitoylation: a new mean to regulate cytoplasmic dynein activity. EMBO J 29: 107-119.
    • (2010) EMBO J , vol.29 , pp. 107-119
    • Shmueli, A.1    Segal, M.2    Sapir, T.3    Tsutsumi, R.4    Noritake, J.5
  • 6
    • 0033769717 scopus 로고    scopus 로고
    • Regulation of cytoplasmic dynein behaviour and microtubule organization by mammalian Lis1
    • Smith DS, Niethammer M, Ayala R, Zhou Y, Gambello MJ, et al. (2000) Regulation of cytoplasmic dynein behaviour and microtubule organization by mammalian Lis1. Nat Cell Biol 2: 767-775.
    • (2000) Nat Cell Biol , vol.2 , pp. 767-775
    • Smith, D.S.1    Niethammer, M.2    Ayala, R.3    Zhou, Y.4    Gambello, M.J.5
  • 7
    • 53549119395 scopus 로고    scopus 로고
    • LIS1 and NDEL1 coordinate the plus-end-directed transport of cytoplasmic dynein
    • Yamada M, Toba S, Yoshida Y, Haratani K, Mori D, et al. (2008) LIS1 and NDEL1 coordinate the plus-end-directed transport of cytoplasmic dynein. EMBO J 27: 2471-2483.
    • (2008) EMBO J , vol.27 , pp. 2471-2483
    • Yamada, M.1    Toba, S.2    Yoshida, Y.3    Haratani, K.4    Mori, D.5
  • 8
    • 27744560966 scopus 로고    scopus 로고
    • Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting protein, is essential for mitotic cell division and neuronal migration
    • Toyo-Oka K, Sasaki S, Yano Y, Mori D, Kobayashi T, et al. (2005) Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting protein, is essential for mitotic cell division and neuronal migration. Hum Mol Genet 14: 3113-3128.
    • (2005) Hum Mol Genet , vol.14 , pp. 3113-3128
    • Toyo-Oka, K.1    Sasaki, S.2    Yano, Y.3    Mori, D.4    Kobayashi, T.5
  • 9
    • 34347369839 scopus 로고    scopus 로고
    • Nudel modulates kinetochore association and function of cytoplasmic dynein in M phase
    • Liang Y, Yu W, Li Y, Yu L, Zhang Q, et al. (2007) Nudel modulates kinetochore association and function of cytoplasmic dynein in M phase. Mol Biol Cell 18: 2656-2666.
    • (2007) Mol Biol Cell , vol.18 , pp. 2656-2666
    • Liang, Y.1    Yu, W.2    Li, Y.3    Yu, L.4    Zhang, Q.5
  • 10
    • 28544453286 scopus 로고    scopus 로고
    • A schizophrenia-associated mutation of DISC1 perturbs cerebral cortex development
    • Kamiya A, Kubo K, Tomoda T, Takaki M, Youn R, et al. (2005) A schizophrenia-associated mutation of DISC1 perturbs cerebral cortex development. Nat Cell Biol 7: 1167-1178.
    • (2005) Nat Cell Biol , vol.7 , pp. 1167-1178
    • Kamiya, A.1    Kubo, K.2    Tomoda, T.3    Takaki, M.4    Youn, R.5
  • 11
    • 23844559241 scopus 로고    scopus 로고
    • Complete loss of Ndel1 results in neuronal migration defects and early embryonic lethality
    • Sasaki S, Mori D, Toyo-oka K, Chen A, Garrett-Beal L, et al. (2005) Complete loss of Ndel1 results in neuronal migration defects and early embryonic lethality. Mol Cell Biol 25: 7812-7827.
    • (2005) Mol Cell Biol , vol.25 , pp. 7812-7827
    • Sasaki, S.1    Mori, D.2    Toyo-oka, K.3    Chen, A.4    Garrett-Beal, L.5
  • 12
    • 5144228139 scopus 로고    scopus 로고
    • Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning
    • Shu T, Ayala R, Nguyen MD, Xie Z, Gleeson JG, et al. (2004) Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to regulate cortical neuronal positioning. Neuron 44: 263-277.
    • (2004) Neuron , vol.44 , pp. 263-277
    • Shu, T.1    Ayala, R.2    Nguyen, M.D.3    Xie, Z.4    Gleeson, J.G.5
  • 13
    • 33846040831 scopus 로고    scopus 로고
    • Trekking across the brain: The journey of neuronal migration
    • Ayala R, Shu T, Tsai LH (2007) Trekking across the brain: the journey of neuronal migration. Cell 128: 29-43.
    • (2007) Cell , vol.128 , pp. 29-43
    • Ayala, R.1    Shu, T.2    Tsai, L.H.3
  • 14
    • 0141646441 scopus 로고    scopus 로고
    • Disregulated RhoGTPases and actin cytoskeleton contribute to the migration defect in Lis1-deficient neurons
    • Kholmanskikh SS, Dobrin JS, Wynshaw-Boris A, Letourneau PC, Ross ME (2003) Disregulated RhoGTPases and actin cytoskeleton contribute to the migration defect in Lis1-deficient neurons. J Neurosci 23: 8673-8681.
    • (2003) J Neurosci , vol.23 , pp. 8673-8681
    • Kholmanskikh, S.S.1    Dobrin, J.S.2    Wynshaw-Boris, A.3    Letourneau, P.C.4    Ross, M.E.5
  • 16
    • 66249131630 scopus 로고    scopus 로고
    • Nudel and FAK as antagonizing strength modulators of nascent adhesions through paxillin
    • Shan Y, Yu L, Li Y, Pan Y, Zhang Q, et al. (2009) Nudel and FAK as antagonizing strength modulators of nascent adhesions through paxillin. PLoS Biol 7: e1000116.
    • (2009) PLoS Biol , vol.7
    • Shan, Y.1    Yu, L.2    Li, Y.3    Pan, Y.4    Zhang, Q.5
  • 17
    • 42049119895 scopus 로고    scopus 로고
    • Nudel binds Cdc42GAP to modulate Cdc42 activity at the leading edge of migrating cells
    • Shen Y, Li N, Wu S, Zhou Y, Shan Y, et al. (2008) Nudel binds Cdc42GAP to modulate Cdc42 activity at the leading edge of migrating cells. Dev Cell 14: 342-353.
    • (2008) Dev Cell , vol.14 , pp. 342-353
    • Shen, Y.1    Li, N.2    Wu, S.3    Zhou, Y.4    Shan, Y.5
  • 18
    • 0037766786 scopus 로고    scopus 로고
    • DISC1 (Disrupted-In- Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: Regulation and loss of interaction with mutation
    • Morris JA, Kandpal G, Ma L, Austin CP (2003) DISC1 (Disrupted-In- Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. Hum Mol Genet 12: 1591-1608.
    • (2003) Hum Mol Genet , vol.12 , pp. 1591-1608
    • Morris, J.A.1    Kandpal, G.2    Ma, L.3    Austin, C.P.4
  • 19
    • 0037422609 scopus 로고    scopus 로고
    • Disruptedin- Schizophrenia-1 (DISC-1): Mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth
    • Ozeki Y, Tomoda T, Kleiderlein J, Kamiya A, Bord L, et al. (2003) Disruptedin- Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth. Proc Natl Acad Sci U S A 100: 289-294.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 289-294
    • Ozeki, Y.1    Tomoda, T.2    Kleiderlein, J.3    Kamiya, A.4    Bord, L.5
  • 20
    • 73849148044 scopus 로고    scopus 로고
    • Functional interplay between LIS1, NDE1 and NDEL1 in dynein-dependent organelle positioning
    • Lam C, Vergnolle MA, Thorpe L, Woodman PG, Allan VJ (2010) Functional interplay between LIS1, NDE1 and NDEL1 in dynein-dependent organelle positioning. J Cell Sci 123: 202-212.
    • (2010) J Cell Sci , vol.123 , pp. 202-212
    • Lam, C.1    Vergnolle, M.A.2    Thorpe, L.3    Woodman, P.G.4    Allan, V.J.5
  • 21
    • 1242285142 scopus 로고    scopus 로고
    • Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein
    • Liang Y, Yu W, Li Y, Yang Z, Yan X, et al. (2004) Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein. J Cell Biol 164: 557-566.
    • (2004) J Cell Biol , vol.164 , pp. 557-566
    • Liang, Y.1    Yu, W.2    Li, Y.3    Yang, Z.4    Yan, X.5
  • 22
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw JE (2000) Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol 16: 483-519.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 23
    • 67449124363 scopus 로고    scopus 로고
    • Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant
    • Tanabe K, Takei K (2009) Dynamic instability of microtubules requires dynamin 2 and is impaired in a Charcot-Marie-Tooth mutant. J Cell Biol 185: 939-948.
    • (2009) J Cell Biol , vol.185 , pp. 939-948
    • Tanabe, K.1    Takei, K.2
  • 24
    • 0035826257 scopus 로고    scopus 로고
    • GTPase activity of dynamin and resulting conformation change are essential for endocytosis
    • Marks B, Stowell MH, Vallis Y, Mills IG, Gibson A, et al. (2001) GTPase activity of dynamin and resulting conformation change are essential for endocytosis. Nature 410: 231-235.
    • (2001) Nature , vol.410 , pp. 231-235
    • Marks, B.1    Stowell, M.H.2    Vallis, Y.3    Mills, I.G.4    Gibson, A.5
  • 25
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A, Uyhazi K, Frost A, De Camilli P (2006) GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 441: 528-531.
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 26
    • 4344586301 scopus 로고    scopus 로고
    • Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin
    • Danino D, Moon KH, Hinshaw JE (2004) Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin. J Struct Biol 147: 259-267.
    • (2004) J Struct Biol , vol.147 , pp. 259-267
    • Danino, D.1    Moon, K.H.2    Hinshaw, J.E.3
  • 28
    • 0032563156 scopus 로고    scopus 로고
    • Dynamin: A molecular motor with pinchase action
    • McNiven MA (1998) Dynamin: a molecular motor with pinchase action. Cell 94: 151-154.
    • (1998) Cell , vol.94 , pp. 151-154
    • McNiven, M.A.1
  • 29
    • 0028137796 scopus 로고
    • Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues
    • Cook TA, Urrutia R, McNiven MA (1994) Identification of dynamin 2, an isoform ubiquitously expressed in rat tissues. Proc Natl Acad Sci U S A 91: 644-648.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 644-648
    • Cook, T.A.1    Urrutia, R.2    McNiven, M.A.3
  • 30
    • 0028805690 scopus 로고
    • Dynamin and endocytosis
    • Liu JP, Robinson PJ (1995) Dynamin and endocytosis. Endocr Rev 16: 590-607.
    • (1995) Endocr Rev , vol.16 , pp. 590-607
    • Liu, J.P.1    Robinson, P.J.2
  • 32
    • 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 (1998) Role of dynamin in the formation of transport vesicles from the trans-Golgi network. Science 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
  • 33
    • 0037371802 scopus 로고    scopus 로고
    • Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis
    • Cao H, Orth JD, Chen J, Weller SG, Heuser JE, et al. (2003) Cortactin is a component of clathrin-coated pits and participates in receptor-mediated endocytosis. Mol Cell Biol 23: 2162-2170.
    • (2003) Mol Cell Biol , vol.23 , pp. 2162-2170
    • Cao, H.1    Orth, J.D.2    Chen, J.3    Weller, S.G.4    Heuser, J.E.5
  • 34
    • 18344381438 scopus 로고    scopus 로고
    • Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport
    • Cao H, Weller S, Orth JD, Chen J, Huang B, et al. (2005) Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport. Nat Cell Biol 7: 483-492.
    • (2005) Nat Cell Biol , vol.7 , pp. 483-492
    • Cao, H.1    Weller, S.2    Orth, J.D.3    Chen, J.4    Huang, B.5
  • 35
    • 33744508200 scopus 로고    scopus 로고
    • Dynamin as a mover and pincher during cell migration and invasion
    • Kruchten AE, McNiven MA (2006) Dynamin as a mover and pincher during cell migration and invasion. J Cell Sci 119: 1683-1690.
    • (2006) J Cell Sci , vol.119 , pp. 1683-1690
    • Kruchten, A.E.1    McNiven, M.A.2
  • 36
    • 0037343053 scopus 로고    scopus 로고
    • A dynamin-cortactin- Arp2/3 complex mediates actin reorganization in growth factor-stimulated cells
    • Krueger EW, Orth JD, Cao H, McNiven MA (2003) A dynamin-cortactin- Arp2/3 complex mediates actin reorganization in growth factor-stimulated cells. Mol Biol Cell 14: 1085-1096.
    • (2003) Mol Biol Cell , vol.14 , pp. 1085-1096
    • Krueger, E.W.1    Orth, J.D.2    Cao, H.3    McNiven, M.A.4
  • 37
    • 0034597062 scopus 로고    scopus 로고
    • Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape
    • McNiven MA, Kim L, Krueger EW, Orth JD, Cao H, et al. (2000) Regulated interactions between dynamin and the actin-binding protein cortactin modulate cell shape. J Cell Biol 151: 187-198.
    • (2000) J Cell Biol , vol.151 , pp. 187-198
    • McNiven, M.A.1    Kim, L.2    Krueger, E.W.3    Orth, J.D.4    Cao, H.5
  • 38
    • 0037039414 scopus 로고    scopus 로고
    • The large GTPase dynamin regulates actin comet formation and movement in living cells
    • Orth JD, Krueger EW, Cao H, McNiven MA (2002) The large GTPase dynamin regulates actin comet formation and movement in living cells. Proc Natl Acad Sci U S A 99: 167-172.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 167-172
    • Orth, J.D.1    Krueger, E.W.2    Cao, H.3    McNiven, M.A.4
  • 39
    • 0037223126 scopus 로고    scopus 로고
    • Dynamin at the actin-membrane interface
    • Orth JD, McNiven MA (2003) Dynamin at the actin-membrane interface. Curr Opin Cell Biol 15: 31-39.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 31-39
    • Orth, J.D.1    McNiven, M.A.2
  • 40
  • 42
    • 33744997144 scopus 로고    scopus 로고
    • Filling the GAP for dynamin
    • Hinshaw JE (2006) Filling the GAP for dynamin. Nat Cell Biol 8: 432-433.
    • (2006) Nat Cell Biol , vol.8 , pp. 432-433
    • Hinshaw, J.E.1
  • 43
    • 0029787352 scopus 로고    scopus 로고
    • Dynamin self-assembly stimulates its GTPase activity
    • Warnock DE, Hinshaw JE, Schmid SL (1996) Dynamin self-assembly stimulates its GTPase activity. J Biol Chem 271: 22310-22314.
    • (1996) J Biol Chem , vol.271 , pp. 22310-22314
    • Warnock, D.E.1    Hinshaw, J.E.2    Schmid, S.L.3
  • 44
    • 33745007067 scopus 로고    scopus 로고
    • The phox homology domain of phospholipase D activates dynamin GTPase activity and accelerates EGFR endocytosis
    • Lee CS, Kim IS, Park JB, Lee MN, Lee HY, et al. (2006) The phox homology domain of phospholipase D activates dynamin GTPase activity and accelerates EGFR endocytosis. Nat Cell Biol 8: 477-484.
    • (2006) Nat Cell Biol , vol.8 , pp. 477-484
    • Lee, C.S.1    Kim, I.S.2    Park, J.B.3    Lee, M.N.4    Lee, H.Y.5
  • 46
    • 0033695663 scopus 로고    scopus 로고
    • Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization
    • Lin JW, Ju W, Foster K, Lee SH, Ahmadian G, et al. (2000) Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization. Nat Neurosci 3: 1282-1290.
    • (2000) Nat Neurosci , vol.3 , pp. 1282-1290
    • Lin, J.W.1    Ju, W.2    Foster, K.3    Lee, S.H.4    Ahmadian, G.5
  • 47
    • 0034094514 scopus 로고    scopus 로고
    • Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin
    • Cao H, Thompson HM, Krueger EW, McNiven MA (2000) Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin. J Cell Sci 113(Pt 11): 1993-2002.
    • (2000) J Cell Sci , vol.113 , Issue.PART 11 , pp. 1993-2002
    • Cao, H.1    Thompson, H.M.2    Krueger, E.W.3    McNiven, M.A.4
  • 48
    • 0033535593 scopus 로고    scopus 로고
    • Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
    • Sever S, Muhlberg AB, Schmid SL (1999) Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature 398: 481-486.
    • (1999) Nature , vol.398 , pp. 481-486
    • Sever, S.1    Muhlberg, A.B.2    Schmid, S.L.3
  • 49
    • 2342640469 scopus 로고    scopus 로고
    • A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity
    • Ligon LA, Tokito M, Finklestein JM, Grossman FE, Holzbaur EL (2004) A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity. J Biol Chem 279: 19201-19208.
    • (2004) J Biol Chem , vol.279 , pp. 19201-19208
    • Ligon, L.A.1    Tokito, M.2    Finklestein, J.M.3    Grossman, F.E.4    Holzbaur, E.L.5
  • 50
    • 33846149648 scopus 로고    scopus 로고
    • DISC1 regulates the transport of the NUDEL/LIS1/14-3-3epsilon complex through kinesin-1
    • Taya S, Shinoda T, Tsuboi D, Asaki J, Nagai K, et al. (2007) DISC1 regulates the transport of the NUDEL/LIS1/14-3-3epsilon complex through kinesin-1. J Neurosci 27: 15-26.
    • (2007) J Neurosci , vol.27 , pp. 15-26
    • Taya, S.1    Shinoda, T.2    Tsuboi, D.3    Asaki, J.4    Nagai, K.5
  • 51
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen M, Sun Y, Drubin DG (2003) A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115: 475-487.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 53
    • 0037128930 scopus 로고    scopus 로고
    • Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function
    • Tai CY, Dujardin DL, Faulkner NE, Vallee RB (2002) Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function. J Cell Biol 156: 959-968.
    • (2002) J Cell Biol , vol.156 , pp. 959-968
    • Tai, C.Y.1    Dujardin, D.L.2    Faulkner, N.E.3    Vallee, R.B.4
  • 54
    • 0031720535 scopus 로고    scopus 로고
    • Differential distribution of dynamin isoforms in mammalian cells
    • Cao H, Garcia F, McNiven MA (1998) Differential distribution of dynamin isoforms in mammalian cells. Mol Biol Cell 9: 2595-2609.
    • (1998) Mol Biol Cell , vol.9 , pp. 2595-2609
    • Cao, H.1    Garcia, F.2    McNiven, M.A.3
  • 55
    • 33846601355 scopus 로고    scopus 로고
    • Charcot- Marie-Tooth disease type 2E, a disorder of the cytoskeleton
    • Fabrizi GM, Cavallaro T, Angiari C, Cabrini I, Taioli F, et al. (2007) Charcot- Marie-Tooth disease type 2E, a disorder of the cytoskeleton. Brain 130: 394-403.
    • (2007) Brain , vol.130 , pp. 394-403
    • Fabrizi, G.M.1    Cavallaro, T.2    Angiari, C.3    Cabrini, I.4    Taioli, F.5
  • 56
    • 34547597494 scopus 로고    scopus 로고
    • Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth disease
    • Fabrizi GM, Ferrarini M, Cavallaro T, Cabrini I, Cerini R, et al. (2007) Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth disease. Neurology 69: 291-295.
    • (2007) Neurology , vol.69 , pp. 291-295
    • Fabrizi, G.M.1    Ferrarini, M.2    Cavallaro, T.3    Cabrini, I.4    Cerini, R.5
  • 57
    • 0033911099 scopus 로고    scopus 로고
    • A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene
    • Mersiyanova IV, Perepelov AV, Polyakov AV, Sitnikov VF, Dadali EL, et al. (2000) A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene. Am J Hum Genet 67: 37-46.
    • (2000) Am J Hum Genet , vol.67 , pp. 37-46
    • Mersiyanova, I.V.1    Perepelov, A.V.2    Polyakov, A.V.3    Sitnikov, V.F.4    Dadali, E.L.5
  • 58
    • 20144366550 scopus 로고    scopus 로고
    • Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease
    • Zuchner S, Noureddine M, Kennerson M, Verhoeven K, Claeys K, et al. (2005) Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease. Nat Genet 37: 289-294.
    • (2005) Nat Genet , vol.37 , pp. 289-294
    • Zuchner, S.1    Noureddine, M.2    Kennerson, M.3    Verhoeven, K.4    Claeys, K.5
  • 59
    • 0242529972 scopus 로고    scopus 로고
    • Effects of elevated cytoplasmic calcium and protein kinase C on endoplasmic reticulum structure and function in HEK293 cells
    • Ribeiro CM, McKay RR, Hosoki E, Bird GS, Putney JW Jr. (2000) Effects of elevated cytoplasmic calcium and protein kinase C on endoplasmic reticulum structure and function in HEK293 cells. Cell Calcium 27: 175-185.
    • (2000) Cell Calcium , vol.27 , pp. 175-185
    • Ribeiro, C.M.1    McKay, R.R.2    Hosoki, E.3    Bird, G.S.4    Putney Jr., J.W.5
  • 60
    • 0030964828 scopus 로고    scopus 로고
    • Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors
    • Roderick HL, Campbell AK, Llewellyn DH (1997) Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors. FEBS Lett 405: 181-185.
    • (1997) FEBS Lett , vol.405 , pp. 181-185
    • Roderick, H.L.1    Campbell, A.K.2    Llewellyn, D.H.3
  • 61
    • 0027022489 scopus 로고
    • Cell-free formation of immature secretory granules and constitutive secretory vesicles from trans-Golgi network
    • Tooze SA, Huttner WB (1992) Cell-free formation of immature secretory granules and constitutive secretory vesicles from trans-Golgi network. Methods Enzymol 219: 81-93.
    • (1992) Methods Enzymol , vol.219 , pp. 81-93
    • Tooze, S.A.1    Huttner, W.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.