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Volumn 323, Issue 2, 2004, Pages 395-401

Rho/ROCK and Cdk5 effects on phosphorylation of a β-thymosin repeat protein in Hermissenda

Author keywords

Csp24; Cyclin dependent kinase; Cytoskeleton; Hermissenda; Rho GTPase; Rho associated kinase

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; BETA THYMOSIN REPEAT PROTEIN; BUTYROLACTONE; CYCLIN DEPENDENT KINASE 5; GUANOSINE TRIPHOSPHATASE; ISOPROTEIN; LYSOPHOSPHATIDIC ACID; PHOSPHATE; PROTEIN CSP24; PROTEIN INHIBITOR; RHO FACTOR; THYMOSIN; UNCLASSIFIED DRUG;

EID: 4544358285     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.103     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 0027052542 scopus 로고
    • Actin matrix of dendritic spines, synaptic plasticity, and long-term potentiation
    • E. Fifkova, and M. Morales Actin matrix of dendritic spines, synaptic plasticity, and long-term potentiation Int. Rev. Cytol. 139 1992 267 307
    • (1992) Int. Rev. Cytol. , vol.139 , pp. 267-307
    • Fifkova, E.1    Morales, M.2
  • 2
    • 0034177303 scopus 로고    scopus 로고
    • Actin and the agile spine: How and why do dendritic spines dance?
    • S. Halpain Actin and the agile spine: how and why do dendritic spines dance? Trends Neurosci. 23 2000 141 146
    • (2000) Trends Neurosci. , vol.23 , pp. 141-146
    • Halpain, S.1
  • 3
    • 0034721711 scopus 로고    scopus 로고
    • Actin-based plasticity in dendritic spines
    • A. Matus Actin-based plasticity in dendritic spines Science 290 2000 754 758
    • (2000) Science , vol.290 , pp. 754-758
    • Matus, A.1
  • 4
    • 0037068824 scopus 로고    scopus 로고
    • Spine motility: Phenomenology, mechanisms, and function
    • T. Bonhoeffer, and R. Yuste Spine motility: phenomenology, mechanisms, and function Neuron 35 2002 1019 1027
    • (2002) Neuron , vol.35 , pp. 1019-1027
    • Bonhoeffer, T.1    Yuste, R.2
  • 6
    • 0032609718 scopus 로고    scopus 로고
    • Rho family proteins and regulation of the actin cytoskeleton
    • A.J. Ridley Rho family proteins and regulation of the actin cytoskeleton Prog. Mol. Subcell. Biol. 22 1999 1 22
    • (1999) Prog. Mol. Subcell. Biol. , vol.22 , pp. 1-22
    • Ridley, A.J.1
  • 7
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • A.J. Ridley Rho family proteins: coordinating cell responses Trends Cell Biol. 12 2001 471 477
    • (2001) Trends Cell Biol. , vol.12 , pp. 471-477
    • Ridley, A.J.1
  • 8
    • 4544257423 scopus 로고    scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • A.J. Ridley, H.F. Paterson, C.L. Johnson, D. Diekmann, and A. Hall The small GTP-binding protein rac regulates growth factor-induced membrane ruffling Cell 116 2004 167 179
    • (2004) Cell , vol.116 , pp. 167-179
    • Ridley, A.J.1    Paterson, H.F.2    Johnson, C.L.3    Diekmann, D.4    Hall, A.5
  • 9
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • A.J. Ridley, and A. Hall The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors Cell 70 1992 389 399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 10
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • C.D. Nobes, and A. Hall Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia Cell 81 1995 53 62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 14
    • 0034574572 scopus 로고    scopus 로고
    • Rho GTPases in neuronal morphogenesis
    • L. Luo Rho GTPases in neuronal morphogenesis Nat. Rev. Neurosci. 1 2000 173 180
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 173-180
    • Luo, L.1
  • 15
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • L. Luo Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity Annu. Rev. Cell. Dev. Biol. 18 2002 601 635
    • (2002) Annu. Rev. Cell. Dev. Biol. , vol.18 , pp. 601-635
    • Luo, L.1
  • 16
    • 0028829750 scopus 로고
    • The Rho’s progress: A potential role during neuritogenesis for the Rho family of GTPases
    • D.J. Mackay, C.D. Nobes, and A. Hall The Rho’s progress: a potential role during neuritogenesis for the Rho family of GTPases Trends Neurosci. 18 1995 496 501
    • (1995) Trends Neurosci. , vol.18 , pp. 496-501
    • MacKay, D.J.1    Nobes, C.D.2    Hall, A.3
  • 17
    • 0029166671 scopus 로고
    • Rho, rac, and cdc42 GTPases regulators of actin structures, cell adhesion and motility
    • C.D. Nobes, and A. Hall Rho, rac, and cdc42 GTPases regulators of actin structures, cell adhesion and motility Biochem. Soc. Trans. 3 1995 456 459
    • (1995) Biochem. Soc. Trans. , vol.3 , pp. 456-459
    • Nobes, C.D.1    Hall, A.2
  • 18
    • 0030982564 scopus 로고    scopus 로고
    • Regulation of dendritic growth and remodeling by Rho, Rac and Cdc42
    • R. Threadgill, K. Bobb, and A. Ghosh Regulation of dendritic growth and remodeling by Rho, Rac and Cdc42 Neuron 19 1997 625 634
    • (1997) Neuron , vol.19 , pp. 625-634
    • Threadgill, R.1    Bobb, K.2    Ghosh, A.3
  • 20
    • 0345735940 scopus 로고    scopus 로고
    • Rho-dependent contractile responses in the neuronal growth cone are independent of classical peripheral retrograde actin flow
    • X.-F. Zhang, A.W. Schaefer, D.T. Burnette, V.T. Schoonderwoert, and P. Forscher Rho-dependent contractile responses in the neuronal growth cone are independent of classical peripheral retrograde actin flow Neuron 40 2003 931 944
    • (2003) Neuron , vol.40 , pp. 931-944
    • Zhang, X.-F.1    Schaefer, A.W.2    Burnette, D.T.3    Schoonderwoert, V.T.4    Forscher, P.5
  • 21
    • 0034656695 scopus 로고    scopus 로고
    • Identification of a 24 kDa phosphoprotein associated with an intermediate stage of memory in Hermissenda
    • T. Crow, and J.J. Xue-Bian Identification of a 24 kDa phosphoprotein associated with an intermediate stage of memory in Hermissenda J. Neurosci. 20 2000 RC74 1â€"5
    • (2000) J. Neurosci. , vol.20
    • Crow, T.1    Xue-Bian, J.J.2
  • 22
    • 0037115048 scopus 로고    scopus 로고
    • One-trial in vitro conditioning regulates a cytoskeletal-related protein (Csp24) in the conditioned stimulus pathway of Hermissenda
    • T. Crow, and J.J. Xue-Bian One-trial in vitro conditioning regulates a cytoskeletal-related protein (Csp24) in the conditioned stimulus pathway of Hermissenda J. Neurosci. 22 2002 10514 10518
    • (2002) J. Neurosci. , vol.22 , pp. 10514-10518
    • Crow, T.1    Xue-Bian, J.J.2
  • 23
    • 0038672193 scopus 로고    scopus 로고
    • Inhibition of conditioned stimulus pathway phosphoprotein 24 expression blocks the development of intermediate-term memory in Hermissenda
    • T. Crow, J.B. Redell, L.-M. Tian, J.J. Xue-Bian, and P.K. Dash Inhibition of conditioned stimulus pathway phosphoprotein 24 expression blocks the development of intermediate-term memory in Hermissenda J. Neurosci. 23 2003 3415 3422
    • (2003) J. Neurosci. , vol.23 , pp. 3415-3422
    • Crow, T.1    Redell, J.B.2    Tian, L.-M.3    Xue-Bian, J.J.4    Dash, P.K.5
  • 24
    • 0034664732 scopus 로고    scopus 로고
    • Ciboulot regulates actin assembly during Drosophila brain metamorphosis
    • I. Boquet, R. Boujemaa, M.-F. Carlier, and T. Preat Ciboulot regulates actin assembly during Drosophila brain metamorphosis Cell 102 2000 797 808
    • (2000) Cell , vol.102 , pp. 797-808
    • Boquet, I.1    Boujemaa, R.2    Carlier, M.-F.3    Preat, T.4
  • 25
  • 26
    • 0032802329 scopus 로고    scopus 로고
    • Protein synthesis-dependent and mRNA synthesis-independent intermediate phase of memory in Hermissenda
    • T. Crow, J.J. Xue-Bian, and V. Siddiqi Protein synthesis-dependent and mRNA synthesis-independent intermediate phase of memory in Hermissenda J. Neurophysiol. 82 1999 495 500
    • (1999) J. Neurophysiol. , vol.82 , pp. 495-500
    • Crow, T.1    Xue-Bian, J.J.2    Siddiqi, V.3
  • 27
    • 0027550516 scopus 로고
    • Small actin-binding proteins: The β-thymosin family
    • V.T. Nachmias Small actin-binding proteins: the β-thymosin family Curr. Opin. Cell. Biol. 5 1993 56 62
    • (1993) Curr. Opin. Cell. Biol. , vol.5 , pp. 56-62
    • Nachmias, V.T.1
  • 28
    • 0030930280 scopus 로고    scopus 로고
    • β-Thymosins from marine invertebrates: Primary structure and interaction with actin
    • D. Safer, and P.K. Chowrashi β-Thymosins from marine invertebrates: primary structure and interaction with actin Cell Motil. Cytoskel. 38 1997 163 171
    • (1997) Cell Motil. Cytoskel. , vol.38 , pp. 163-171
    • Safer, D.1    Chowrashi, P.K.2
  • 29
    • 0031179053 scopus 로고    scopus 로고
    • A novel β-thymosin from the Sea Urchin: Extending the phylogenetic distribution of β-thymosins from mammals to echinoderms
    • S. Stoeva, S. Hörger, and W. Voelter A novel β-thymosin from the Sea Urchin: extending the phylogenetic distribution of β-thymosins from mammals to echinoderms J. Peptide Sci. 3 1997 282 290
    • (1997) J. Peptide Sci. , vol.3 , pp. 282-290
    • Stoeva, S.1    Hörger, S.2    Voelter, W.3
  • 33
    • 0029965953 scopus 로고    scopus 로고
    • Time-dependent increases in protein phosphorylation following one-trial enhancement in Hermissenda
    • T. Crow, V. Siddiqi, Q. Zhu, and J.T. Neary Time-dependent increases in protein phosphorylation following one-trial enhancement in Hermissenda J. Neurochem. 66 1996 1736 1741
    • (1996) J. Neurochem. , vol.66 , pp. 1736-1741
    • Crow, T.1    Siddiqi, V.2    Zhu, Q.3    Neary, J.T.4
  • 34
    • 0029870891 scopus 로고    scopus 로고
    • β-Thymosins are not simple actin monomer buffering proteins
    • H.-Q. Sun, K. Kwiatkowska, and H.L. Yin β-Thymosins are not simple actin monomer buffering proteins J. Biol. Chem. 271 1996 9223 9230
    • (1996) J. Biol. Chem. , vol.271 , pp. 9223-9230
    • Sun, H.-Q.1    Kwiatkowska, K.2    Yin, H.L.3
  • 35
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • A. Hall Rho GTPases and the actin cytoskeleton Science 279 1998 509 514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 36
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • M. Raftopoulou, and A. Hall Cell migration: Rho GTPases lead the way Dev. Biol. 265 2004 23 32
    • (2004) Dev. Biol. , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 38
    • 0037079063 scopus 로고    scopus 로고
    • Fear memory formation involves p190 RhoGAP and ROCK proteins through a GRB2-mediated complex
    • R. Lamprecht, C.R. Farb, and J.E. LeDoux Fear memory formation involves p190 RhoGAP and ROCK proteins through a GRB2-mediated complex Neuron 36 2002 727 738
    • (2002) Neuron , vol.36 , pp. 727-738
    • Lamprecht, R.1    Farb, C.R.2    Ledoux, J.E.3
  • 39
    • 0032500583 scopus 로고    scopus 로고
    • Molecular analysis of the interactions between protein kinase C-Îμ and filamentous actin
    • R. Prekeris, R.M. Hernandez, M.W. Mayhew, M.K. White, and D.M. Terrian Molecular analysis of the interactions between protein kinase C-Îμ and filamentous actin J. Biol. Chem. 273 1998 26790 26798
    • (1998) J. Biol. Chem. , vol.273 , pp. 26790-26798
    • Prekeris, R.1    Hernandez, R.M.2    Mayhew, M.W.3    White, M.K.4    Terrian, D.M.5
  • 42
    • 0347285297 scopus 로고    scopus 로고
    • The molecular mystery of neuronal migration: FAK and Cdk5
    • M. Nikolic The molecular mystery of neuronal migration: FAK and Cdk5 Trends Cell Biol. 14 2004 1 4
    • (2004) Trends Cell Biol. , vol.14 , pp. 1-4
    • Nikolic, M.1
  • 44
    • 0029966469 scopus 로고    scopus 로고
    • The Cdk5/p35 kinase is essential for neurite outgrowth during neuronal differentiation
    • M. Nikolic, H. Duidek, Y.T. Kwon, Y.F.M. Ramos, and L.-H. Tsai The Cdk5/p35 kinase is essential for neurite outgrowth during neuronal differentiation Genes Dev. 7 1996 818 825
    • (1996) Genes Dev. , vol.7 , pp. 818-825
    • Nikolic, M.1    Duidek, H.2    Kwon, Y.T.3    Ramos, Y.F.M.4    Tsai, L.-H.5
  • 45
    • 0032504964 scopus 로고    scopus 로고
    • The p35/Cdk5 kinase is a neuron-specific Rac effector that inhibits Pak1 activity
    • M. Nikolic, M.M. Chou, W. Lu, B.J. Mayer, and L.H. Tsai The p35/Cdk5 kinase is a neuron-specific Rac effector that inhibits Pak1 activity Nature 395 1998 194 198
    • (1998) Nature , vol.395 , pp. 194-198
    • Nikolic, M.1    Chou, M.M.2    Lu, W.3    Mayer, B.J.4    Tsai, L.H.5
  • 46
    • 0023038690 scopus 로고    scopus 로고
    • Light-paired with serotonin mimics the effects of conditioning on phototactic behavior in Hermissenda
    • T. Crow, and J. Forrester Light-paired with serotonin mimics the effects of conditioning on phototactic behavior in Hermissenda Proc. Natl. Acad. Sci. USA 83 1996 7975 7978
    • (1996) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7975-7978
    • Crow, T.1    Forrester, J.2
  • 47
    • 0027261024 scopus 로고    scopus 로고
    • Differential modulation of voltage-dependent currents in Hermissenda type B photoreceptors by serotonin
    • J. Acosta-Urquidi, and T. Crow Differential modulation of voltage-dependent currents in Hermissenda type B photoreceptors by serotonin J. Neurophysiol. 70 1999 541 598
    • (1999) J. Neurophysiol. , vol.70 , pp. 541-598
    • Acosta-Urquidi, J.1    Crow, T.2
  • 49
    • 0030013316 scopus 로고    scopus 로고
    • 2+ currents in Hermissenda photoreceptors by 5-HT and GABA
    • 2+ currents in Hermissenda photoreceptors by 5-HT and GABA J. Neurosci. 16 1996 4799 4809
    • (1996) J. Neurosci. , vol.16 , pp. 4799-4809
    • Yamoah, E.N.1    Crow, T.2
  • 50
    • 0031424374 scopus 로고    scopus 로고
    • Time-dependent changes in excitability after one-trial conditioning of Hermissenda
    • T. Crow, and V. Siddiqi Time-dependent changes in excitability after one-trial conditioning of Hermissenda J. Neurophysiol. 78 1997 3460 3464
    • (1997) J. Neurophysiol. , vol.78 , pp. 3460-3464
    • Crow, T.1    Siddiqi, V.2


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