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Volumn 124, Issue 7, 2011, Pages 1032-1042

Phosphorylation of kinesin light chain 1 at serine 460 modulates binding and trafficking of calsyntenin-1

Author keywords

Alzheimer's disease; Axonal transport; Calsyntenin 1; ERK; Kinesin light chain 1; MAPK

Indexed keywords

ADENOSINE DERIVATIVE; ASPARTIC ACID; C JUN N TERMINAL KINASE INTERACTIN PROTEIN 1; CALSYNTENIN 1; COLLAPSIN RESPONSE MEDIATOR PROTEIN 2; HUNTINGTIN; HUNTINGTIN ASSOCIATED PROTEIN 1 ISOFORM A; KINASE D INTERACTING SUBSTRATE OF 220 KDA; KINESIN 1; KINESIN LIGHT CHAIN 1; MITOGEN ACTIVATED PROTEIN KINASE; SERINE 460; SERINE DERIVATIVE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 79953141458     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.075168     Document Type: Article
Times cited : (51)

References (56)
  • 3
    • 1542782550 scopus 로고    scopus 로고
    • Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism
    • Araki, Y., Tomita, S., Yamaguchi, H., Miyagi, N., Sumioka, A., Kirino, Y. and Suzuki, T. (2003). Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism. J. Biol. Chem. 278, 49448-49458.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49448-49458
    • Araki, Y.1    Tomita, S.2    Yamaguchi, H.3    Miyagi, N.4    Sumioka, A.5    Kirino, Y.6    Suzuki, T.7
  • 4
    • 33947607769 scopus 로고    scopus 로고
    • The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport
    • Araki, Y., Kawano, T., Taru, H., Saito, Y., Wada, S., Miyamoto, K., Kobayashi, H., Ishikawa, H. O., Ohsugi, Y., Yamamoto, T. et al. (2007). The novel cargo Alcadein induces vesicle association of kinesin-1 motor components and activates axonal transport. EMBO J. 26, 1475-1486.
    • (2007) EMBO J , vol.26 , pp. 1475-1486
    • Araki, Y.1    Kawano, T.2    Taru, H.3    Saito, Y.4    Wada, S.5    Miyamoto, K.6    Kobayashi, H.7    Ishikawa, H.O.8    Ohsugi, Y.9    Yamamoto, T.10
  • 5
    • 33749853607 scopus 로고    scopus 로고
    • A probabilitybased approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil, S. A., Villen, J., Gerber, S. A., Rush, J. and Gygi, S. P. (2006). A probabilitybased approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. 24, 1285-1292.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 7
    • 33846087314 scopus 로고    scopus 로고
    • Kidins220/ARMS is transported by a kinesin-1-based mechanism likely to be involved in neuronal differentiation
    • Bracale, A., Cesca, F., Neubrand, V. E., Newsome, T. P., Way, M. and Schiavo, G. (2007). Kidins220/ARMS is transported by a kinesin-1-based mechanism likely to be involved in neuronal differentiation. Mol. Biol. Cell 18, 142-152.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 142-152
    • Bracale, A.1    Cesca, F.2    Neubrand, V.E.3    Newsome, T.P.4    Way, M.5    Schiavo, G.6
  • 8
    • 44449124267 scopus 로고    scopus 로고
    • Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis
    • Cantin, G. T., Yi, W., Lu, B., Park, S. K., Xu, T., Lee, J. D. and Yates, J. R., 3rd (2008). Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J. Proteome Res. 7, 1346-1351.
    • (2008) J. Proteome Res. , vol.7 , pp. 1346-1351
    • Cantin, G.T.1    Yi, W.2    Lu, B.3    Park, S.K.4    Xu, T.5    Lee, J.D.6    Yates 3rd., J.R.7
  • 10
    • 34147192803 scopus 로고    scopus 로고
    • Visualization and quantification of mitochondrial dynamics in living animal cells
    • De Vos, K. J. and Sheetz, M. P. (2007). Visualization and quantification of mitochondrial dynamics in living animal cells. Methods Cell Biol. 80, 627-682.
    • (2007) Methods Cell Biol , vol.80 , pp. 627-682
    • De Vos, K.J.1    Sheetz, M.P.2
  • 11
    • 0034641135 scopus 로고    scopus 로고
    • Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria
    • De Vos, K., Severin, F., Van Herreweghe, F., Vancompernolle, K., Goossens, V., Hyman, A. and Grooten, J. (2000). Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria. J. Cell Biol. 149, 1207-1214.
    • (2000) J. Cell Biol. , vol.149 , pp. 1207-1214
    • De Vos, K.1    Severin, F.2    Van Herreweghe, F.3    Vancompernolle, K.4    Goossens, V.5    Hyman, A.6    Grooten, J.7
  • 16
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelieres, F. P., King, S. J., Humbert, S. and Saudou, F. (2007). Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583.
    • (2007) J. Neurosci. , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6    Saudou, F.7
  • 17
    • 74949142875 scopus 로고    scopus 로고
    • Collapsin response mediator protein 4a (CRMP4a) is upregulated in motoneurons of mutant SOD1 mice and can trigger motoneuron axonal degeneration and cell death
    • Duplan, L., Bernard, N., Casseron, W., Dudley, K., Thouvenot, E., Honnorat, J., Rogemond, V., De Bovis, B., Aebischer, P., Marin, P. et al. (2010). Collapsin response mediator protein 4a (CRMP4a) is upregulated in motoneurons of mutant SOD1 mice and can trigger motoneuron axonal degeneration and cell death. J. Neurosci. 30, 785-796.
    • (2010) J. Neurosci. , vol.30 , pp. 785-796
    • Duplan, L.1    Bernard, N.2    Casseron, W.3    Dudley, K.4    Thouvenot, E.5    Honnorat, J.6    Rogemond, V.7    De Bovis, B.8    Aebischer, P.9    Marin, P.10
  • 18
    • 0027425443 scopus 로고
    • The Drosophila kinesin light chain. Primary structure and interaction with kinesin heavy chain
    • Gauger, A. K. and Goldstein, L. S. (1993). The Drosophila kinesin light chain. Primary structure and interaction with kinesin heavy chain. J. Biol. Chem. 268, 13657-13666.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13657-13666
    • Gauger, A.K.1    Goldstein, L.S.2
  • 19
    • 37749000849 scopus 로고    scopus 로고
    • Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release
    • Guillaud, L., Wong, R. and Hirokawa, N. (2007). Disruption of KIF17-Mint1 interaction by CaMKII-dependent phosphorylation: a molecular model of kinesin-cargo release. Nat. Cell Biol. 10, 19-29.
    • (2007) Nat. Cell Biol. , vol.10 , pp. 19-29
    • Guillaud, L.1    Wong, R.2    Hirokawa, N.3
  • 20
    • 41849140047 scopus 로고    scopus 로고
    • Cooperative versus independent transport of different cargoes by Kinesin-1
    • Hammond, J. W., Griffin, K., Jih, G. T., Stuckey, J. and Verhey, K. J. (2008). Cooperative versus independent transport of different cargoes by Kinesin-1. Traffic 9, 725-741.
    • (2008) Traffic , vol.9 , pp. 725-741
    • Hammond, J.W.1    Griffin, K.2    Jih, G.T.3    Stuckey, J.4    Verhey, K.J.5
  • 22
    • 50349090965 scopus 로고    scopus 로고
    • Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics
    • Hirokawa, N. and Noda, Y. (2008). Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics. Physiol. Rev. 88, 1089-1118.
    • (2008) Physiol. Rev. , vol.88 , pp. 1089-1118
    • Hirokawa, N.1    Noda, Y.2
  • 23
    • 0027263661 scopus 로고
    • Phosphorylation of neuronal kinesin heavy and light chains in vivo
    • Hollenbeck, P. J. (1993). Phosphorylation of neuronal kinesin heavy and light chains in vivo. J. Neurochem. 60, 2265-2275.
    • (1993) J. Neurochem. , vol.60 , pp. 2265-2275
    • Hollenbeck, P.J.1
  • 25
    • 27744476574 scopus 로고    scopus 로고
    • The high and middle molecular weight neurofilament subunits regulate the association of neurofilaments with kinesin: Inhibition by phosphorylation of the high molecular weight subunit
    • Jung, C., Lee, S., Ortiz, D., Zhu, Q., Julien, J. P. and Shea, T. B. (2005). The high and middle molecular weight neurofilament subunits regulate the association of neurofilaments with kinesin: Inhibition by phosphorylation of the high molecular weight subunit. Brain Res. Mol. Brain Res. 141, 151-155.
    • (2005) Brain Res. Mol. Brain Res. , vol.141 , pp. 151-155
    • Jung, C.1    Lee, S.2    Ortiz, D.3    Zhu, Q.4    Julien, J.P.5    Shea, T.B.6
  • 26
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • Kamal, A., Stokin, G. B., Yang, Z. H., Xia, C. H. and Goldstein, L. S. B. (2000). Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron 28, 449-459.
    • (2000) Neuron , vol.28 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.H.3    Xia, C.H.4    Goldstein, L.S.B.5
  • 27
    • 20744459425 scopus 로고    scopus 로고
    • Tubulin and CRMP-2 complex is transported via Kinesin-1
    • Kimura, T., Watanabe, H., Iwamatsu, A. and Kaibuchi, K. (2005). Tubulin and CRMP-2 complex is transported via Kinesin-1. J. Neurochem. 93, 1371-1382.
    • (2005) J. Neurochem. , vol.93 , pp. 1371-1382
    • Kimura, T.1    Watanabe, H.2    Iwamatsu, A.3    Kaibuchi, K.4
  • 30
    • 10344227214 scopus 로고    scopus 로고
    • The neuronal adaptor protein X11beta reduces Abeta levels and amyloid plaque formation in the brains of transgenic mice
    • Lee, J. H., Lau, K. F., Perkinton, M. S., Standen, C. L., Rogelj, B., Falinska, A., McLoughlin, D. M. and Miller, C. C. (2004). The neuronal adaptor protein X11beta reduces Abeta levels and amyloid plaque formation in the brains of transgenic mice. J. Biol. Chem. 279, 49099-49104.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49099-49104
    • Lee, J.H.1    Lau, K.F.2    Perkinton, M.S.3    Standen, C.L.4    Rogelj, B.5    Falinska, A.6    McLoughlin, D.M.7    Miller, C.C.8
  • 31
    • 0028939893 scopus 로고
    • Phosphorylation of kinesin in vivo correlates with organelle association and neurite outgrowth
    • Lee, K. D. and Hollenbeck, P. J. (1995). Phosphorylation of kinesin in vivo correlates with organelle association and neurite outgrowth. J. Biol. Chem. 270, 5600-5605.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5600-5605
    • Lee, K.D.1    Hollenbeck, P.J.2
  • 32
    • 2142765951 scopus 로고    scopus 로고
    • A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization
    • Li, Q., Lau, A., Morris, T. J., Guo, L., Fordyce, C. B. and Stanley, E. F. (2004). A syntaxin 1, Galpha(o), and N-type calcium channel complex at a presynaptic nerve terminal: analysis by quantitative immunocolocalization. J. Neurosci. 24, 4070-4081.
    • (2004) J. Neurosci. , vol.24 , pp. 4070-4081
    • Li, Q.1    Lau, A.2    Morris, T.J.3    Guo, L.4    Fordyce, C.B.5    Stanley, E.F.6
  • 33
    • 0030884680 scopus 로고    scopus 로고
    • Phosphotransferases associated with the regulation of kinesin motor activity
    • Lindesmith, L., McIlvain, J. M., Jr, Argon, Y. and Sheetz, M. P. (1997). Phosphotransferases associated with the regulation of kinesin motor activity. J. Biol. Chem. 272, 22929-22933.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22929-22933
    • Lindesmith, L.1    McIlvain Jr., J.M.2    Argon, Y.3    Sheetz, M.P.4
  • 35
    • 0027164170 scopus 로고
    • Calmodulin binding to and cAMP-dependent phosphorylation of kinesin light chains modulate kinesin ATPase activity
    • Matthies, H. J., Miller, R. J. and Palfrey, H. C. (1993). Calmodulin binding to and cAMP-dependent phosphorylation of kinesin light chains modulate kinesin ATPase activity. J. Biol. Chem. 268, 11176-11187.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11176-11187
    • Matthies, H.J.1    Miller, R.J.2    Palfrey, H.C.3
  • 36
    • 33645642673 scopus 로고    scopus 로고
    • Interaction of huntingtinassociated protein-1 with kinesin light chain: Implications in intracellular trafficking in neurons
    • McGuire, J. R., Rong, J., Li, S. H. and Li, X. J. (2005). Interaction of huntingtinassociated protein-1 with kinesin light chain: Implications in intracellular trafficking in neurons. J. Biol. Chem. 281, 3552-3559.
    • (2005) J. Biol. Chem. , vol.281 , pp. 3552-3559
    • McGuire, J.R.1    Rong, J.2    Li, S.H.3    Li, X.J.4
  • 38
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesinbased motility
    • Morfini, G., Szebenyi, G., Elluru, R., Ratner, N. and Brady, S. T. (2002). Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesinbased motility. EMBO J. 21, 281-293.
    • (2002) EMBO J , vol.21 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 40
    • 0028363485 scopus 로고
    • Cloning and localization of a conventional kinesin motor expressed exclusively in neurons
    • Niclas, J., Navone, F., Hom-Booher, N. and Vale, R. D. (1994). Cloning and localization of a conventional kinesin motor expressed exclusively in neurons. Neuron 12, 1059-1072.
    • (1994) Neuron , vol.12 , pp. 1059-1072
    • Niclas, J.1    Navone, F.2    Hom-Booher, N.3    Vale, R.D.4
  • 41
    • 36348971109 scopus 로고    scopus 로고
    • HAP1 can sequester a subset of TBP in cytoplasmic inclusions via specific interaction with the conserved TBP(CORE)
    • Prigge, J. R. and Schmidt, E. E. (2007). HAP1 can sequester a subset of TBP in cytoplasmic inclusions via specific interaction with the conserved TBP(CORE). BMC Mol. Biol. 8, 76.
    • (2007) BMC Mol. Biol. , vol.8 , pp. 76
    • Prigge, J.R.1    Schmidt, E.E.2
  • 42
    • 0032546953 scopus 로고    scopus 로고
    • Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins
    • Rahman, A., Friedman, D. S. and Goldstein, L. S. (1998). Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins. J. Biol. Chem. 273, 15395-15403.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15395-15403
    • Rahman, A.1    Friedman, D.S.2    Goldstein, L.S.3
  • 44
    • 0027057337 scopus 로고
    • The phosphorylation of kinesin regulates its binding to synaptic vesicles
    • Sato-Yoshitake, R., Yorifuji, H., Inagaki, M. and Hirokawa, N. (1992). The phosphorylation of kinesin regulates its binding to synaptic vesicles. J. Biol. Chem. 267, 23930-23936.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23930-23936
    • Sato-Yoshitake, R.1    Yorifuji, H.2    Inagaki, M.3    Hirokawa, N.4
  • 45
    • 33845663953 scopus 로고    scopus 로고
    • Unloading kinesin transported cargoes from the tubulin track via the inflammatory c-Jun Nterminal kinase pathway
    • Stagi, M., Gorlovoy, P., Larionov, S., Takahashi, K. and Neumann, H. (2006). Unloading kinesin transported cargoes from the tubulin track via the inflammatory c-Jun Nterminal kinase pathway. FASEB J. 20, 2573-2575.
    • (2006) FASEB J , vol.20 , pp. 2573-2575
    • Stagi, M.1    Gorlovoy, P.2    Larionov, S.3    Takahashi, K.4    Neumann, H.5
  • 47
    • 0033591331 scopus 로고    scopus 로고
    • Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity
    • Stock, M. F., Guerrero, J., Cobb, B., Eggers, C. T., Huang, T. G., Li, X. and Hackney, D. D. (1999). Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity. J. Biol. Chem. 274, 14617-14623.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14617-14623
    • Stock, M.F.1    Guerrero, J.2    Cobb, B.3    Eggers, C.T.4    Huang, T.G.5    Li, X.6    Hackney, D.D.7
  • 53
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's disease
    • Walsh, D. M. and Selkoe, D. J. (2004). Deciphering the molecular basis of memory failure in Alzheimer's disease. Neuron 44, 181-193.
    • (2004) Neuron , vol.44 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 54
    • 0032508714 scopus 로고    scopus 로고
    • A mammalian scaffold complex that selectively mediates MAP kinase activation
    • Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J. and Davis, R. J. (1998). A mammalian scaffold complex that selectively mediates MAP kinase activation. Science 281, 1671-1674.
    • (1998) Science , vol.281 , pp. 1671-1674
    • Whitmarsh, A.J.1    Cavanagh, J.2    Tournier, C.3    Yasuda, J.4    Davis, R.J.5
  • 55
    • 33751572018 scopus 로고    scopus 로고
    • Cargo selection by specific kinesin light chain 1 isoforms
    • Wozniak, M. J. and Allan, V. J. (2006). Cargo selection by specific kinesin light chain 1 isoforms. EMBO J. 25, 5457-5468.
    • (2006) EMBO J , vol.25 , pp. 5457-5468
    • Wozniak, M.J.1    Allan, V.J.2
  • 56
    • 60749102885 scopus 로고    scopus 로고
    • Neurofilament subunit (NFL) head domain phosphorylation regulates axonal transport of neurofilaments
    • Yates, D. M., Manser, C., De Vos, K. J., Shaw, C. E., McLoughlin, D. M. and Miller, C. C. (2009). Neurofilament subunit (NFL) head domain phosphorylation regulates axonal transport of neurofilaments. Eur. J. Cell Biol. 88, 193-202.
    • (2009) Eur. J. Cell Biol. , vol.88 , pp. 193-202
    • Yates, D.M.1    Manser, C.2    De Vos, K.J.3    Shaw, C.E.4    McLoughlin, D.M.5    Miller, C.C.6


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