메뉴 건너뛰기




Volumn 287, Issue 26, 2012, Pages 22341-22353

Specific serine-proline phosphorylation and glycogen synthase kinase 3β-directed subcellular targeting of stathmin 3/sclip in neurons

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOGEN SYNTHASE KINASE-3; NEURITES; NEURONAL DIFFERENTIATION; STATHMIN; SUB-CELLULAR; SUBCELLULAR TARGETING;

EID: 84862705619     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.344044     Document Type: Article
Times cited : (11)

References (72)
  • 1
    • 0025745372 scopus 로고
    • Stathmin. A relay phosphoprotein for multiple signal transduction?
    • Sobel, A. (1991) Stathmin. A relay phosphoprotein for multiple signal transduction? Trends Biochem. Sci. 16, 301-305
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 301-305
    • Sobel, A.1
  • 3
    • 0024509921 scopus 로고
    • Intracellular substrates for extracellular signaling. Characterization of a ubiquitous, neuron-enriched phosphoprotein (stathmin)
    • Sobel, A., Boutterin, M. C., Beretta, L., Chneiweiss, H., Doye, V., and Peyro-Saint-Paul, H. (1989) Intracellular substrates for extracellular signaling. Characterization of a ubiquitous, neuron-enriched phosphoprotein (stathmin). J. Biol. Chem. 264, 3765-3772
    • (1989) J. Biol. Chem. , vol.264 , pp. 3765-3772
    • Sobel, A.1    Boutterin, M.C.2    Beretta, L.3    Chneiweiss, H.4    Doye, V.5    Peyro-Saint-Paul, H.6
  • 4
    • 0027169646 scopus 로고
    • Stathmin gene family. Phylogenetic conservation and developmental regulation in Xenopus
    • Maucuer, A., Moreau, J., Méchali, M., and Sobel, A. (1993) Stathmin gene family. Phylogenetic conservation and developmental regulation in Xenopus. J. Biol. Chem. 268, 16420-16429
    • (1993) J. Biol. Chem. , vol.268 , pp. 16420-16429
    • Maucuer, A.1    Moreau, J.2    Méchali, M.3    Sobel, A.4
  • 5
    • 0031745284 scopus 로고    scopus 로고
    • SCLIP. A novel SCG10-like protein of the stathmin family expressed in the nervous system
    • Ozon, S., Byk, T., and Sobel, A. (1998) SCLIP. A novel SCG10-like protein of the stathmin family expressed in the nervous system. J. Neurochem. 70, 2386-2396
    • (1998) J. Neurochem. , vol.70 , pp. 2386-2396
    • Ozon, S.1    Byk, T.2    Sobel, A.3
  • 6
    • 0030768533 scopus 로고    scopus 로고
    • The stathmin family, molecular and biological characterization of novel mammalian proteins expressed in the nervous system
    • Ozon, S., Maucuer, A., and Sobel, A. (1997) The stathmin family, molecular and biological characterization of novel mammalian proteins expressed in the nervous system. Eur. J. Biochem. 248, 794-806
    • (1997) Eur. J. Biochem. , vol.248 , pp. 794-806
    • Ozon, S.1    Maucuer, A.2    Sobel, A.3
  • 7
    • 0027292675 scopus 로고
    • Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2
    • Beretta, L., Dobránsky, T., and Sobel, A. (1993) Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2. J. Biol. Chem. 268, 20076-20084
    • (1993) J. Biol. Chem. , vol.268 , pp. 20076-20084
    • Beretta, L.1    Dobránsky, T.2    Sobel, A.3
  • 8
    • 0035910554 scopus 로고    scopus 로고
    • Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16
    • Daub, H., Gevaert, K., Vandekerckhove, J., Sobel, A., and Hall, A. (2001) Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16. J. Biol. Chem. 276, 1677-1680
    • (2001) J. Biol. Chem. , vol.276 , pp. 1677-1680
    • Daub, H.1    Gevaert, K.2    Vandekerckhove, J.3    Sobel, A.4    Hall, A.5
  • 10
    • 0032145275 scopus 로고    scopus 로고
    • Serine 16 of stathmin as a cytosolic target for Ca2/calmodulin-dependent kinase II after CD2 triggering of human T lymphocytes
    • le Gouvello, S., Manceau, V., and Sobel, A. (1998) Serine 16 of stathmin as a cytosolic target for Ca2/calmodulin-dependent kinase II after CD2 triggering of human T lymphocytes. J. Immunol. 161, 1113-1122
    • (1998) J. Immunol. , vol.161 , pp. 1113-1122
    • Le Gouvello, S.1    Manceau, V.2    Sobel, A.3
  • 12
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont, L. D., and Mitchison, T. J. (1996) Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 84, 623-631
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 13
    • 0035844234 scopus 로고    scopus 로고
    • Stathmin family proteins display specific molecular and tubulin binding properties
    • Charbaut, E., Curmi, P. A., Ozon, S., Lachkar, S., Redeker, V., and Sobel, A. (2001) Stathmin family proteins display specific molecular and tubulin binding properties. J. Biol. Chem. 276, 16146-16154
    • (2001) J. Biol. Chem. , vol.276 , pp. 16146-16154
    • Charbaut, E.1    Curmi, P.A.2    Ozon, S.3    Lachkar, S.4    Redeker, V.5    Sobel, A.6
  • 16
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli, R. B., Gigant, B., Curmi, P. A., Jourdain, I., Lachkar, S., Sobel, A., and Knossow, M. (2004) Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428, 198-202
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6    Knossow, M.7
  • 17
    • 33744915563 scopus 로고    scopus 로고
    • Control of intrinsically disordered stathmin by multisite phosphorylation
    • Honnappa, S., Jahnke, W., Seelig, J., and Steinmetz, M. O. (2006) Control of intrinsically disordered stathmin by multisite phosphorylation. J. Biol. Chem. 281, 16078-16083
    • (2006) J. Biol. Chem. , vol.281 , pp. 16078-16083
    • Honnappa, S.1    Jahnke, W.2    Seelig, J.3    Steinmetz, M.O.4
  • 19
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin. A tubulin-sequestering protein that forms a ternary T2S complex with two tubulin molecules
    • Jourdain, L., Curmi, P., Sobel, A., Pantaloni, D., and Carlier, M. F. (1997) Stathmin. A tubulin-sequestering protein that forms a ternary T2S complex with two tubulin molecules. Biochemistry 36, 10817-10821
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.F.5
  • 20
    • 72149120574 scopus 로고    scopus 로고
    • The microtubule network and neuronal morphogenesis. Dynamic and coordinated orchestration through multiple players
    • Poulain, F. E., and Sobel, A. (2010) The microtubule network and neuronal morphogenesis. Dynamic and coordinated orchestration through multiple players. Mol. Cell Neurosci. 43, 15-32
    • (2010) Mol. Cell Neurosci. , vol.43 , pp. 15-32
    • Poulain, F.E.1    Sobel, A.2
  • 21
    • 21044448079 scopus 로고    scopus 로고
    • Two separate motifs cooperate to target stathmin-related proteins to the Golgi complex
    • Charbaut, E., Chauvin, S., Enslen, H., Zamaroczy, S., and Sobel, A. (2005) Two separate motifs cooperate to target stathmin-related proteins to the Golgi complex. J. Cell Sci. 118, 2313-2323
    • (2005) J. Cell Sci. , vol.118 , pp. 2313-2323
    • Charbaut, E.1    Chauvin, S.2    Enslen, H.3    Zamaroczy, S.4    Sobel, A.5
  • 22
    • 53349177067 scopus 로고    scopus 로고
    • Palmitoylation of stathmin family proteins domain A controls Golgi versus mitochondrial subcellular targeting
    • Chauvin, S., Poulain, F. E., Ozon, S., and Sobel, A. (2008) Palmitoylation of stathmin family proteins domain A controls Golgi versus mitochondrial subcellular targeting. Biol. Cell 100, 577-589
    • (2008) Biol. Cell , vol.100 , pp. 577-589
    • Chauvin, S.1    Poulain, F.E.2    Ozon, S.3    Sobel, A.4
  • 24
    • 79957597365 scopus 로고    scopus 로고
    • Subcellular Golgi localization of stathmin family proteins is promoted by a specific set ofDHHCpalmitoyl transferases
    • Levy, A. D., Devignot, V., Fukata, Y., Fukata, M., Sobel, A., and Chauvin, S. (2011) Subcellular Golgi localization of stathmin family proteins is promoted by a specific set ofDHHCpalmitoyl transferases. Mol. Biol. Cell 22, 1930-1942
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1930-1942
    • Levy, A.D.1    Devignot, V.2    Fukata, Y.3    Fukata, M.4    Sobel, A.5    Chauvin, S.6
  • 25
    • 0036605565 scopus 로고    scopus 로고
    • Regulation and subcellular localization of the microtubule-destabilizing stathmin family phosphoproteins in cortical neurons
    • Gavet, O., El Messari, S., Ozon, S., and Sobel, A. (2002) Regulation and subcellular localization of the microtubule-destabilizing stathmin family phosphoproteins in cortical neurons. J. Neurosci. Res. 68, 535-550
    • (2002) J. Neurosci. Res. , vol.68 , pp. 535-550
    • Gavet, O.1    El Messari, S.2    Ozon, S.3    Sobel, A.4
  • 26
    • 33846528695 scopus 로고    scopus 로고
    • The "SCG10-LIke Protein" SCLIP is a novel regulator of axonal branching in hippocampal neurons, unlike SCG10
    • Poulain, F. E., and Sobel, A. (2007) The "SCG10-LIke Protein" SCLIP is a novel regulator of axonal branching in hippocampal neurons, unlike SCG10. Mol. Cell. Neurosci. 34, 137-146
    • (2007) Mol. Cell. Neurosci. , vol.34 , pp. 137-146
    • Poulain, F.E.1    Sobel, A.2
  • 28
    • 33748577718 scopus 로고    scopus 로고
    • The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18
    • Watabe-Uchida, M., John, K. A., Janas, J. A., Newey, S. E., and Van Aelst, L. (2006) The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18. Neuron 51, 727-739
    • (2006) Neuron , vol.51 , pp. 727-739
    • Watabe-Uchida, M.1    John, K.A.2    Janas, J.A.3    Newey, S.E.4    Van Aelst, L.5
  • 29
    • 34249062484 scopus 로고    scopus 로고
    • The microtubule destabilizer stathmin mediates the development of dendritic arbors in neuronal cells
    • Ohkawa, N., Fujitani, K., Tokunaga, E., Furuya, S., and Inokuchi, K. (2007) The microtubule destabilizer stathmin mediates the development of dendritic arbors in neuronal cells. J. Cell Sci. 120, 1447-1456
    • (2007) J. Cell Sci. , vol.120 , pp. 1447-1456
    • Ohkawa, N.1    Fujitani, K.2    Tokunaga, E.3    Furuya, S.4    Inokuchi, K.5
  • 30
    • 0346750741 scopus 로고    scopus 로고
    • Role of the microtubule destabilizing proteins SCG10 and stathmin in neuronal growth
    • Grenningloh, G., Soehrman, S., Bondallaz, P., Ruchti, E., and Cadas, H. (2004) Role of the microtubule destabilizing proteins SCG10 and stathmin in neuronal growth. J. Neurobiol. 58, 60-69
    • (2004) J. Neurobiol. , vol.58 , pp. 60-69
    • Grenningloh, G.1    Soehrman, S.2    Bondallaz, P.3    Ruchti, E.4    Cadas, H.5
  • 31
    • 0033151999 scopus 로고    scopus 로고
    • Differential, regional, and cellular expression of the stathmin family transcripts in the adult rat brain
    • Ozon, S., El Mestikawy, S., and Sobel, A. (1999) Differential, regional, and cellular expression of the stathmin family transcripts in the adult rat brain. J. Neurosci. Res. 56, 553-564
    • (1999) J. Neurosci. Res. , vol.56 , pp. 553-564
    • Ozon, S.1    El Mestikawy, S.2    Sobel, A.3
  • 32
    • 0028340726 scopus 로고
    • Differential localization of SCG10 and p19/stathmin messenger RNAs in adult rat brain indicates distinct roles for these growth-associated proteins
    • Himi, T., Okazaki, T., Wang, H., McNeill, T. H., and Mori, N. (1994) Differential localization of SCG10 and p19/stathmin messenger RNAs in adult rat brain indicates distinct roles for these growth-associated proteins. Neuroscience 60, 907-926
    • (1994) Neuroscience , vol.60 , pp. 907-926
    • Himi, T.1    Okazaki, T.2    Wang, H.3    McNeill, T.H.4    Mori, N.5
  • 33
    • 0034629506 scopus 로고    scopus 로고
    • Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry
    • Redeker, V., Lachkar, S., Siavoshian, S., Charbaut, E., Rossier, J., Sobel, A., and Curmi, P. A. (2000) Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry. J. Biol. Chem. 275, 6841-6849
    • (2000) J. Biol. Chem. , vol.275 , pp. 6841-6849
    • Redeker, V.1    Lachkar, S.2    Siavoshian, S.3    Charbaut, E.4    Rossier, J.5    Sobel, A.6    Curmi, P.A.7
  • 34
    • 0032478782 scopus 로고    scopus 로고
    • Identification of in vitro phosphorylation sites in the growth cone protein SCG10. Effect of phosphorylation site mutants on microtubule- destabilizing activity
    • Antonsson, B., Kassel, D. B., Di Paolo, G., Lutjens, R., Riederer, B. M., and Grenningloh, G. (1998) Identification of in vitro phosphorylation sites in the growth cone protein SCG10. Effect of phosphorylation site mutants on microtubule-destabilizing activity. J. Biol. Chem. 273, 8439-8446
    • (1998) J. Biol. Chem. , vol.273 , pp. 8439-8446
    • Antonsson, B.1    Kassel, D.B.2    Di Paolo, G.3    Lutjens, R.4    Riederer, B.M.5    Grenningloh, G.6
  • 35
    • 11844260672 scopus 로고    scopus 로고
    • Both the establishment and the maintenance of neuronal polarity require active mechanisms. Critical roles of GSK-3β and its upstream regulators
    • Jiang, H., Guo, W., Liang, X., and Rao, Y. (2005) Both the establishment and the maintenance of neuronal polarity require active mechanisms. Critical roles of GSK-3β and its upstream regulators. Cell 120, 123-135
    • (2005) Cell , vol.120 , pp. 123-135
    • Jiang, H.1    Guo, W.2    Liang, X.3    Rao, Y.4
  • 36
  • 37
    • 34047093866 scopus 로고    scopus 로고
    • GSK-3α and GSK-3β are necessary for axon formation
    • Garrido, J. J., Simón, D., Varea, O., and Wandosell, F. (2007) GSK-3α and GSK-3β are necessary for axon formation. FEBS Lett. 581, 1579-1586
    • (2007) FEBS Lett. , vol.581 , pp. 1579-1586
    • Garrido, J.J.1    Simón, D.2    Varea, O.3    Wandosell, F.4
  • 38
    • 8744251609 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3β and the regulation of axon growth
    • Goold, R. G., and Gordon-Weeks, P. R. (2004) Glycogen synthase kinase 3β and the regulation of axon growth. Biochem. Soc. Trans. 32, 809-811
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 809-811
    • Goold, R.G.1    Gordon-Weeks, P.R.2
  • 39
    • 84856716198 scopus 로고    scopus 로고
    • Role of GSK-3 signaling in neuronal morphogenesis
    • article 48
    • Kim, Y. T., Hur, E. M., Snider, W. D., and Zhou, F. Q. (2011) Role of GSK-3 signaling in neuronal morphogenesis. Front. Mol. Neurosci. 4, article 48, 1-11
    • (2011) Front. Mol. Neurosci. , vol.4 , pp. 1-11
    • Kim, Y.T.1    Hur, E.M.2    Snider, W.D.3    Zhou, F.Q.4
  • 40
    • 0031745447 scopus 로고    scopus 로고
    • The stathmin phosphoprotein family. Intracellular localization and effects on the microtubule network
    • Gavet, O., Ozon, S., Manceau, V., Lawler, S., Curmi, P., and Sobel, A. (1998) The stathmin phosphoprotein family. Intracellular localization and effects on the microtubule network. J. Cell Sci. 111, 3333-3346
    • (1998) J. Cell Sci. , vol.111 , pp. 3333-3346
    • Gavet, O.1    Ozon, S.2    Manceau, V.3    Lawler, S.4    Curmi, P.5    Sobel, A.6
  • 41
    • 0002329664 scopus 로고    scopus 로고
    • Banker G., and K. Goslin, K., eds MIT Press, Cambridge, MA
    • Goslin, K., Assmussen, H., and Banker, G. (1998) in Culturing Nerve Cells (Banker G., and K. Goslin, K., eds) pp. 339-370, MIT Press, Cambridge, MA
    • (1998) Culturing Nerve Cells , pp. 339-370
    • Goslin, K.1    Assmussen, H.2    Banker, G.3
  • 42
    • 0025215226 scopus 로고
    • Developmental tissue expression and phylogenetic conservation of stathmin, a phosphoprotein associated with cell regulations
    • Koppel, J., Boutterin, M. C., Doye, V., Peyro-Saint-Paul, H., and Sobel, A. (1990) Developmental tissue expression and phylogenetic conservation of stathmin, a phosphoprotein associated with cell regulations. J. Biol. Chem. 265, 3703-3707
    • (1990) J. Biol. Chem. , vol.265 , pp. 3703-3707
    • Koppel, J.1    Boutterin, M.C.2    Doye, V.3    Peyro-Saint-Paul, H.4    Sobel, A.5
  • 43
    • 0347380122 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 and neuronal migration in the neocortex
    • Gupta, A., and Tsai, L. H. (2003) Cyclin-dependent kinase 5 and neuronal migration in the neocortex. Neurosignals 12, 173-179
    • (2003) Neurosignals , vol.12 , pp. 173-179
    • Gupta, A.1    Tsai, L.H.2
  • 44
    • 0031855511 scopus 로고    scopus 로고
    • Role of MAP kinase in neurons
    • Fukunaga, K., and Miyamoto, E. (1998) Role of MAP kinase in neurons. Mol. Neurobiol. 16, 79-95
    • (1998) Mol. Neurobiol. , vol.16 , pp. 79-95
    • Fukunaga, K.1    Miyamoto, E.2
  • 47
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti, C. G., Sullivan, C. A., and Banker, G. A. (1988) The establishment of polarity by hippocampal neurons in culture. J. Neurosci. 8, 1454-1468
    • (1988) J. Neurosci. , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 48
    • 0141953237 scopus 로고    scopus 로고
    • Cytoskeletal dynamics and transport in growth cone motility and axon guidance
    • Dent, E. W., and Gertler, F. B. (2003) Cytoskeletal dynamics and transport in growth cone motility and axon guidance. Neuron 40, 209-227
    • (2003) Neuron , vol.40 , pp. 209-227
    • Dent, E.W.1    Gertler, F.B.2
  • 50
    • 33748599842 scopus 로고    scopus 로고
    • Organometallic compounds with biological activity. A very selective and highly potent cellular inhibitor for glycogen synthase kinase 3
    • Atilla-Gokcumen, G. E., Williams, D. S., Bregman, H., Pagano, N., and Meggers, E. (2006) Organometallic compounds with biological activity. A very selective and highly potent cellular inhibitor for glycogen synthase kinase 3. Chembiochem. 7, 1443-1450
    • (2006) Chembiochem. , vol.7 , pp. 1443-1450
    • Atilla-Gokcumen, G.E.1    Williams, D.S.2    Bregman, H.3    Pagano, N.4    Meggers, E.5
  • 51
    • 80052682729 scopus 로고    scopus 로고
    • Functional implications of glycogen synthase kinase-3-mediated Tau phosphorylation
    • Hanger, D. P., and Noble, W. (2011) Functional implications of glycogen synthase kinase-3-mediated Tau phosphorylation. Int. J. Alzheimers Dis. 2011, 352805
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 352805
    • Hanger, D.P.1    Noble, W.2
  • 52
    • 9244249219 scopus 로고    scopus 로고
    • APC and GSK-3β are involved in mPar3 targeting to the nascent axon and establishment of neuronal polarity
    • Shi, S. H., Cheng, T., Jan, L. Y., and Jan, Y. N. (2004) APC and GSK-3β are involved in mPar3 targeting to the nascent axon and establishment of neuronal polarity. Curr. Biol. 14, 2025-2032
    • (2004) Curr. Biol. , vol.14 , pp. 2025-2032
    • Shi, S.H.1    Cheng, T.2    Jan, L.Y.3    Jan, Y.N.4
  • 54
    • 0030750560 scopus 로고    scopus 로고
    • Control of microtubule dynamics by oncoprotein 18. Dissection of the regulatory role of multisite phosphorylation during mitosis
    • Larsson, N., Marklund, U., Gradin, H. M., Brattsand, G., and Gullberg, M. (1997) Control of microtubule dynamics by oncoprotein 18. Dissection of the regulatory role of multisite phosphorylation during mitosis. Mol. Cell. Biol. 17, 5530-5539
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5530-5539
    • Larsson, N.1    Marklund, U.2    Gradin, H.M.3    Brattsand, G.4    Gullberg, M.5
  • 55
    • 0028023846 scopus 로고
    • Assembly and bundling of marginal band microtubule protein. Role of Tau
    • Sanchez, I., and Cohen, W. D. (1994) Assembly and bundling of marginal band microtubule protein. Role of Tau. Cell Motil. Cytoskeleton 29, 57-71
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 57-71
    • Sanchez, I.1    Cohen, W.D.2
  • 56
    • 70350417339 scopus 로고    scopus 로고
    • Cytoskeletal dynamics in growth-cone steering
    • Geraldo, S., and Gordon-Weeks, P. R. (2009) Cytoskeletal dynamics in growth-cone steering. J. Cell Sci. 122, 3595-3604
    • (2009) J. Cell Sci. , vol.122 , pp. 3595-3604
    • Geraldo, S.1    Gordon-Weeks, P.R.2
  • 57
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation. The therapeutic challenge for neurodegenerative disease
    • Hanger, D. P., Anderton, B. H., and Noble, W. (2009) Tau phosphorylation. The therapeutic challenge for neurodegenerative disease. Trends Mol. Med. 15, 112-119
    • (2009) Trends Mol. Med. , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 59
    • 69349101851 scopus 로고    scopus 로고
    • Nonprimed and DYRK1A-primed GSK-3β phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons
    • Scales, T. M., Lin, S., Kraus, M., Goold, R. G., and Gordon-Weeks, P. R. (2009) Nonprimed and DYRK1A-primed GSK-3β phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons. J. Cell Sci. 122, 2424-2435
    • (2009) J. Cell Sci. , vol.122 , pp. 2424-2435
    • Scales, T.M.1    Lin, S.2    Kraus, M.3    Goold, R.G.4    Gordon-Weeks, P.R.5
  • 61
    • 1442300147 scopus 로고    scopus 로고
    • L1/laminin modulation of growth cone response to EphB triggers growth pauses and regulates the microtubule destabilizing protein SCG10
    • Suh, L. H., Oster, S. F., Soehrman, S. S., Grenningloh, G., and Sretavan, D. W. (2004) L1/laminin modulation of growth cone response to EphB triggers growth pauses and regulates the microtubule destabilizing protein SCG10. J. Neurosci. 24, 1976-1986
    • (2004) J. Neurosci. , vol.24 , pp. 1976-1986
    • Suh, L.H.1    Oster, S.F.2    Soehrman, S.S.3    Grenningloh, G.4    Sretavan, D.W.5
  • 63
    • 60549098791 scopus 로고    scopus 로고
    • Membrane transport of WAVE2 and lamellipodia formation require Pak1 that mediates phosphorylation and recruitment of stathmin/Op18 to Pak1-WAVE2-kinesin complex
    • Takahashi, K., and Suzuki, K. (2009) Membrane transport of WAVE2 and lamellipodia formation require Pak1 that mediates phosphorylation and recruitment of stathmin/Op18 to Pak1-WAVE2-kinesin complex. Cell Signal 21, 695-703
    • (2009) Cell Signal , vol.21 , pp. 695-703
    • Takahashi, K.1    Suzuki, K.2
  • 64
    • 71349086233 scopus 로고    scopus 로고
    • Directional control of WAVE2 membrane targeting by EB1 and phosphatidylinositol 3,4,5-triphosphate
    • Takahashi, K., Tanaka, T., and Suzuki, K. (2010) Directional control of WAVE2 membrane targeting by EB1 and phosphatidylinositol 3,4,5-triphosphate. Cell Signal. 22, 510-518
    • (2010) Cell Signal. , vol.22 , pp. 510-518
    • Takahashi, K.1    Tanaka, T.2    Suzuki, K.3
  • 65
    • 0346750747 scopus 로고    scopus 로고
    • Actin and microtubules in neurite initiation. Are MAPs the missing link?
    • Dehmelt, L., and Halpain, S. (2004) Actin and microtubules in neurite initiation. Are MAPs the missing link? J. Neurobiol. 58, 18-33
    • (2004) J. Neurobiol. , vol.58 , pp. 18-33
    • Dehmelt, L.1    Halpain, S.2
  • 66
    • 0042882289 scopus 로고    scopus 로고
    • Drosophila pod-1 cross-links both actin and microtubules and controls the targeting of axons
    • Rothenberg, M. E., Rogers, S. L., Vale, R. D., Jan, L. Y., and Jan, Y. N. (2003) Drosophila pod-1 cross-links both actin and microtubules and controls the targeting of axons. Neuron 39, 779-791
    • (2003) Neuron , vol.39 , pp. 779-791
    • Rothenberg, M.E.1    Rogers, S.L.2    Vale, R.D.3    Jan, L.Y.4    Jan, Y.N.5
  • 67
    • 34247481813 scopus 로고    scopus 로고
    • Spinophilin facilitates dephosphorylation of doublecortin by PP1 to mediate microtubule bundling at the axonal wrist
    • Bielas, S. L., Serneo, F. F., Chechlacz, M., Deerinck, T. J., Perkins, G. A., Allen, P. B., Ellisman, M. H., and Gleeson, J. G. (2007) Spinophilin facilitates dephosphorylation of doublecortin by PP1 to mediate microtubule bundling at the axonal wrist. Cell 129, 579-591
    • (2007) Cell , vol.129 , pp. 579-591
    • Bielas, S.L.1    Serneo, F.F.2    Chechlacz, M.3    Deerinck, T.J.4    Perkins, G.A.5    Allen, P.B.6    Ellisman, M.H.7    Gleeson, J.G.8
  • 68
    • 0034602161 scopus 로고    scopus 로고
    • Patient mutations in doublecortin define a repeated tubulin-binding domain
    • Taylor, K. R., Holzer, A. K., Bazan, J. F., Walsh, C. A., and Gleeson, J. G. (2000) Patient mutations in doublecortin define a repeated tubulin-binding domain. J. Biol. Chem. 275, 34442-34450
    • (2000) J. Biol. Chem. , vol.275 , pp. 34442-34450
    • Taylor, K.R.1    Holzer, A.K.2    Bazan, J.F.3    Walsh, C.A.4    Gleeson, J.G.5
  • 70
    • 0032979181 scopus 로고    scopus 로고
    • Stathmin interaction with HSC70 family proteins
    • Manceau, V., Gavet, O., Curmi, P., and Sobel, A. (1999) Stathmin interaction with HSC70 family proteins. Electrophoresis 20, 409-417
    • (1999) Electrophoresis , vol.20 , pp. 409-417
    • Manceau, V.1    Gavet, O.2    Curmi, P.3    Sobel, A.4
  • 71
    • 0033860681 scopus 로고    scopus 로고
    • Common mechanisms underlying growth cone guidance and axon branching
    • Kalil, K., Szebenyi, G., and Dent, E. W. (2000) Common mechanisms underlying growth cone guidance and axon branching. J. Neurobiol. 44, 145-158
    • (2000) J. Neurobiol. , vol.44 , pp. 145-158
    • Kalil, K.1    Szebenyi, G.2    Dent, E.W.3
  • 72
    • 0032189429 scopus 로고    scopus 로고
    • Interstitial branches develop from active regions of the axon demarcated by the primary growth cone during pausing behaviors
    • Szebenyi, G., Callaway, J. L., Dent, E. W., and Kalil, K. (1998) Interstitial branches develop from active regions of the axon demarcated by the primary growth cone during pausing behaviors. J. Neurosci. 18, 7930-7940
    • (1998) J. Neurosci. , vol.18 , pp. 7930-7940
    • Szebenyi, G.1    Callaway, J.L.2    Dent, E.W.3    Kalil, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.