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Volumn 148, Issue 2, 2007, Pages 413-420

One-trial in vitro conditioning regulates an association between the β-thymosin repeat protein Csp24 and actin

Author keywords

actin binding; beta thymosin repeat protein; excitability; phosphorylation; protein kinase C

Indexed keywords

A TYPE POTASSIUM CHANNEL; ACTIN; ANTIBODY; G ACTIN; PHOSPHOPROTEIN; PHOSPHOPROTEIN 24; POTASSIUM CHANNEL; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR; RECOMBINANT PROTEIN; THYMOSIN; UNCLASSIFIED DRUG;

EID: 34548409620     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuroscience.2007.06.023     Document Type: Article
Times cited : (7)

References (54)
  • 1
    • 4444285120 scopus 로고    scopus 로고
    • Roles of fascin in cell adhesion and motility
    • Adams J.C. Roles of fascin in cell adhesion and motility. Curr Opin Cell Biol 16 (2004) 590-596
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 590-596
    • Adams, J.C.1
  • 3
    • 33644835262 scopus 로고    scopus 로고
    • The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins
    • Aguda A.H., Xue B., Irobi E., Preat T., and Robinson R.C. The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins. Structure 14 (2006) 469-476
    • (2006) Structure , vol.14 , pp. 469-476
    • Aguda, A.H.1    Xue, B.2    Irobi, E.3    Preat, T.4    Robinson, R.C.5
  • 4
    • 0034664732 scopus 로고    scopus 로고
    • Ciboulot regulates actin assembly during Drosophila brain metamorphosis
    • Boquet I., Boujemaa R., Carlier M.F., and Preat T. 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
  • 5
    • 0041589208 scopus 로고    scopus 로고
    • Depolymerization of actin filaments by profilin. Effects of profilin on capping protein function
    • Bubb M.R., Yarmola E.G., Gibson B.G., and Southwick F.S. Depolymerization of actin filaments by profilin. Effects of profilin on capping protein function. J Biol Chem 278 (2003) 24629-24635
    • (2003) J Biol Chem , vol.278 , pp. 24629-24635
    • Bubb, M.R.1    Yarmola, E.G.2    Gibson, B.G.3    Southwick, F.S.4
  • 6
    • 0029956147 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton in the regulation of the cystic fibrosis transmembrane conductance regulator
    • Cantiello H.F. Role of the actin cytoskeleton in the regulation of the cystic fibrosis transmembrane conductance regulator. Exp Physiol 81 (1996) 505-514
    • (1996) Exp Physiol , vol.81 , pp. 505-514
    • Cantiello, H.F.1
  • 8
    • 2542616090 scopus 로고    scopus 로고
    • Pavlovian conditioning of Hermissenda: current cellular, molecular, and circuit perspectives
    • Crow T. Pavlovian conditioning of Hermissenda: current cellular, molecular, and circuit perspectives. Learn Mem 11 (2004) 229-238
    • (2004) Learn Mem , vol.11 , pp. 229-238
    • Crow, T.1
  • 9
    • 0026042942 scopus 로고
    • Light paired with serotonin in vivo produces both short- and long-term enhancement of generator potentials of identified B-photoreceptors in Hermissenda
    • Crow T., and Forrester J. Light paired with serotonin in vivo produces both short- and long-term enhancement of generator potentials of identified B-photoreceptors in Hermissenda. J Neurosci 11 (1991) 608-617
    • (1991) J Neurosci , vol.11 , pp. 608-617
    • Crow, T.1    Forrester, J.2
  • 10
    • 0038672193 scopus 로고    scopus 로고
    • Inhibition of conditioned stimulus pathway phosphoprotein 24 expression blocks the development of intermediate-term memory in Hermissenda
    • Crow T., Redell J.B., Tian L.M., Xue-Bian J., and Dash P.K. 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.4    Dash, P.K.5
  • 11
    • 0031424374 scopus 로고    scopus 로고
    • Time-dependent changes in excitability after one-trial conditioning of Hermissenda
    • Crow T., and Siddiqi V. 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
  • 12
    • 0029965953 scopus 로고    scopus 로고
    • Time-dependent increase in protein phosphorylation following one-trial enhancement in Hermissenda
    • Crow T., Siddiqi V., Zhu Q., and Neary J.T. Time-dependent increase 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
  • 13
    • 0034656695 scopus 로고    scopus 로고
    • Identification of a 24 kDa phosphoprotein associated with an intermediate stage of memory in Hermissenda
    • Crow T., and Xue-Bian J.J. Identification of a 24 kDa phosphoprotein associated with an intermediate stage of memory in Hermissenda. J Neurosci 20 (2000) RC74
    • (2000) J Neurosci , vol.20
    • Crow, T.1    Xue-Bian, J.J.2
  • 14
    • 0037115048 scopus 로고    scopus 로고
    • One-trial in vitro conditioning regulates a cytoskeletal-related protein (CSP24) in the conditioned stimulus pathway of Hermissenda
    • Crow T., and Xue-Bian J.J. 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
  • 15
    • 4544358285 scopus 로고    scopus 로고
    • Rho/ROCK and Cdk5 effects on phosphorylation of a beta-thymosin repeat protein in Hermissenda
    • Crow T., Xue-Bian J.J., Dash P.K., and Tian L.M. Rho/ROCK and Cdk5 effects on phosphorylation of a beta-thymosin repeat protein in Hermissenda. Biochem Biophys Res Commun 323 (2004) 395-401
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 395-401
    • Crow, T.1    Xue-Bian, J.J.2    Dash, P.K.3    Tian, L.M.4
  • 16
    • 0032802329 scopus 로고    scopus 로고
    • Protein synthesis-dependent and mRNA synthesis-independent intermediate phase of memory in Hermissenda
    • Crow T., Xue-Bian J.J., and Siddiqi V. 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
  • 17
    • 0032080250 scopus 로고    scopus 로고
    • Phosphorylation of mitogen-activated protein kinase by one-trial and multi-trial classical conditioning
    • Crow T., Xue-Bian J.J., Siddiqi V., Kang Y., and Neary J.T. Phosphorylation of mitogen-activated protein kinase by one-trial and multi-trial classical conditioning. J Neurosci 18 (1998) 3480-3487
    • (1998) J Neurosci , vol.18 , pp. 3480-3487
    • Crow, T.1    Xue-Bian, J.J.2    Siddiqi, V.3    Kang, Y.4    Neary, J.T.5
  • 18
    • 0023051136 scopus 로고
    • Protein kinase C activation induces conductance changes in Hermissenda photoreceptors like those seen in associative learning
    • Farley J., and Auerbach S. Protein kinase C activation induces conductance changes in Hermissenda photoreceptors like those seen in associative learning. Nature 319 (1986) 220-223
    • (1986) Nature , vol.319 , pp. 220-223
    • Farley, J.1    Auerbach, S.2
  • 19
    • 0032078861 scopus 로고    scopus 로고
    • Rapid actin-based plasticity in dendritic spines
    • Fischer M., Kaech S., Knutti D., and Matus A. Rapid actin-based plasticity in dendritic spines. Neuron 20 (1998) 847-854
    • (1998) Neuron , vol.20 , pp. 847-854
    • Fischer, M.1    Kaech, S.2    Knutti, D.3    Matus, A.4
  • 20
    • 0038662761 scopus 로고    scopus 로고
    • Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo
    • Fukazawa Y., Saitoh Y., Ozawa F., Ohta Y., Mizuno K., and Inokuchi K. Hippocampal LTP is accompanied by enhanced F-actin content within the dendritic spine that is essential for late LTP maintenance in vivo. Neuron 38 (2003) 447-460
    • (2003) Neuron , vol.38 , pp. 447-460
    • Fukazawa, Y.1    Saitoh, Y.2    Ozawa, F.3    Ohta, Y.4    Mizuno, K.5    Inokuchi, K.6
  • 23
    • 0037064067 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin
    • Hattan D., Nesti E., Cachero T.G., and Morielli A.D. Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin. J Biol Chem 277 (2002) 38596-38606
    • (2002) J Biol Chem , vol.277 , pp. 38596-38606
    • Hattan, D.1    Nesti, E.2    Cachero, T.G.3    Morielli, A.D.4
  • 24
    • 0037177848 scopus 로고    scopus 로고
    • Control of actin dynamics by proteins made of beta-thymosin repeats: the actobindin family
    • Hertzog M., Yarmola E.G., Didry D., Bubb M.R., and Carlier M.F. Control of actin dynamics by proteins made of beta-thymosin repeats: the actobindin family. J Biol Chem 277 (2002) 14786-14792
    • (2002) J Biol Chem , vol.277 , pp. 14786-14792
    • Hertzog, M.1    Yarmola, E.G.2    Didry, D.3    Bubb, M.R.4    Carlier, M.F.5
  • 27
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama T., and Mihashi K. Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem 114 (1981) 33-38
    • (1981) Eur J Biochem , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 28
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • Larsson C. Protein kinase C and the regulation of the actin cytoskeleton. Cell Signal 18 (2006) 276-284
    • (2006) Cell Signal , vol.18 , pp. 276-284
    • Larsson, C.1
  • 30
    • 12744271503 scopus 로고    scopus 로고
    • Cortactin phosphorylation as a switch for actin cytoskeletal network and cell dynamics control
    • Lua B.L., and Low B.C. Cortactin phosphorylation as a switch for actin cytoskeletal network and cell dynamics control. FEBS Lett 579 (2005) 577-585
    • (2005) FEBS Lett , vol.579 , pp. 577-585
    • Lua, B.L.1    Low, B.C.2
  • 31
    • 0034640199 scopus 로고    scopus 로고
    • Alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells
    • Maruoka N.D., Steele D.F., Au B.P., Dan P., Zhang X., Moore E.D., and Fedida D. Alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. FEBS Lett 473 (2000) 188-194
    • (2000) FEBS Lett , vol.473 , pp. 188-194
    • Maruoka, N.D.1    Steele, D.F.2    Au, B.P.3    Dan, P.4    Zhang, X.5    Moore, E.D.6    Fedida, D.7
  • 32
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • Matsuzaki M., Honkura N., Ellis-Davies G.C., and Kasai H. Structural basis of long-term potentiation in single dendritic spines. Nature 429 (2004) 761-766
    • (2004) Nature , vol.429 , pp. 761-766
    • Matsuzaki, M.1    Honkura, N.2    Ellis-Davies, G.C.3    Kasai, H.4
  • 33
    • 0025452909 scopus 로고
    • Regulation of short-term associative memory by calcium-dependent protein kinase
    • Matzel L.D., Lederhendler I.I., and Alkon D.L. Regulation of short-term associative memory by calcium-dependent protein kinase. J Neurosci 10 (1990) 2300-2307
    • (1990) J Neurosci , vol.10 , pp. 2300-2307
    • Matzel, L.D.1    Lederhendler, I.I.2    Alkon, D.L.3
  • 34
    • 0036828324 scopus 로고    scopus 로고
    • Signaling mechanisms that regulate actin-based motility processes in the nervous system
    • Meyer G., and Feldman E.L. Signaling mechanisms that regulate actin-based motility processes in the nervous system. J Neurochem 83 (2002) 490-503
    • (2002) J Neurochem , vol.83 , pp. 490-503
    • Meyer, G.1    Feldman, E.L.2
  • 36
    • 21244432905 scopus 로고    scopus 로고
    • Cytoskeletal regulation of calcium-permeable cation channels in the human syncytiotrophoblast: role of gelsolin
    • Montalbetti N., Li Q., Timpanaro G.A., Gonzalez-Perrett S., Dai X.Q., Chen X.Z., and Cantiello H.F. Cytoskeletal regulation of calcium-permeable cation channels in the human syncytiotrophoblast: role of gelsolin. J Physiol 566 (2005) 309-325
    • (2005) J Physiol , vol.566 , pp. 309-325
    • Montalbetti, N.1    Li, Q.2    Timpanaro, G.A.3    Gonzalez-Perrett, S.4    Dai, X.Q.5    Chen, X.Z.6    Cantiello, H.F.7
  • 37
    • 33748912660 scopus 로고    scopus 로고
    • Kv2.1 potassium channels are retained within dynamic cell surface microdomains that are defined by a perimeter fence
    • O'Connell K.M., Rolig A.S., Whitesell J.D., and Tamkun M.M. Kv2.1 potassium channels are retained within dynamic cell surface microdomains that are defined by a perimeter fence. J Neurosci 26 (2006) 9609-9618
    • (2006) J Neurosci , vol.26 , pp. 9609-9618
    • O'Connell, K.M.1    Rolig, A.S.2    Whitesell, J.D.3    Tamkun, M.M.4
  • 38
    • 3042710591 scopus 로고    scopus 로고
    • Regulation of cytoskeletal dynamics by actin-monomer-binding proteins
    • Paavilainen V.O., Bertling E., Falck S., and Lappalainen P. Regulation of cytoskeletal dynamics by actin-monomer-binding proteins. Trends Cell Biol 14 (2004) 386-394
    • (2004) Trends Cell Biol , vol.14 , pp. 386-394
    • Paavilainen, V.O.1    Bertling, E.2    Falck, S.3    Lappalainen, P.4
  • 39
    • 9644303000 scopus 로고    scopus 로고
    • Phosphorylation of actin-binding protein (ABP-280; filamin) by tyrosine kinase p56lck modulates actin filament cross-linking
    • Pal S.C., and Goldmann W.H. Phosphorylation of actin-binding protein (ABP-280; filamin) by tyrosine kinase p56lck modulates actin filament cross-linking. Cell Biol Int 28 (2004) 935-941
    • (2004) Cell Biol Int , vol.28 , pp. 935-941
    • Pal, S.C.1    Goldmann, W.H.2
  • 40
    • 0034548877 scopus 로고    scopus 로고
    • Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin
    • Petrecca K., Miller D.M., and Shrier A. Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin. J Neurosci 20 (2000) 8736-8744
    • (2000) J Neurosci , vol.20 , pp. 8736-8744
    • Petrecca, K.1    Miller, D.M.2    Shrier, A.3
  • 41
    • 3543083870 scopus 로고    scopus 로고
    • The co-workers of actin filaments: from cell structures to signals
    • Revenu C., Athman R., Robine S., and Louvard D. The co-workers of actin filaments: from cell structures to signals. Nat Rev Mol Cell Biol 5 (2004) 635-646
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 635-646
    • Revenu, C.1    Athman, R.2    Robine, S.3    Louvard, D.4
  • 42
    • 0142211278 scopus 로고    scopus 로고
    • Direct interaction between the actin-binding protein filamin-A and the inwardly rectifying potassium channel, Kir2.1
    • Sampson L.J., Leyland M.L., and Dart C. Direct interaction between the actin-binding protein filamin-A and the inwardly rectifying potassium channel, Kir2.1. J Biol Chem 278 (2003) 41988-41997
    • (2003) J Biol Chem , vol.278 , pp. 41988-41997
    • Sampson, L.J.1    Leyland, M.L.2    Dart, C.3
  • 43
    • 0029080144 scopus 로고
    • Increasing intracellular concentrations of thymosin beta 4 in PtK2 cells: effects on stress fibers, cytokinesis, and cell spreading
    • Sanger J.M., Golla R., Safer D., Choi J.K., Yu K.R., Sanger J.W., and Nachmias V.T. Increasing intracellular concentrations of thymosin beta 4 in PtK2 cells: effects on stress fibers, cytokinesis, and cell spreading. Cell Motil Cytoskeleton 31 (1995) 307-322
    • (1995) Cell Motil Cytoskeleton , vol.31 , pp. 307-322
    • Sanger, J.M.1    Golla, R.2    Safer, D.3    Choi, J.K.4    Yu, K.R.5    Sanger, J.W.6    Nachmias, V.T.7
  • 44
    • 32544455943 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II-mediated actin reorganization
    • 2+/calmodulin-dependent protein kinase II-mediated actin reorganization. J Neurosci 26 (2006) 1813-1822
    • (2006) J Neurosci , vol.26 , pp. 1813-1822
    • Shi, Y.1    Ethell, I.M.2
  • 45
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., and Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246 (1971) 4866-4871
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 46
    • 0036176244 scopus 로고    scopus 로고
    • Rapid turnover of actin in dendritic spines and its regulation by activity
    • Star E.N., Kwiatkowski D.J., and Murthy V.N. Rapid turnover of actin in dendritic spines and its regulation by activity. Nat Neurosci 5 (2002) 239-246
    • (2002) Nat Neurosci , vol.5 , pp. 239-246
    • Star, E.N.1    Kwiatkowski, D.J.2    Murthy, V.N.3
  • 48
  • 50
    • 0029870891 scopus 로고    scopus 로고
    • beta-Thymosins are not simple actin monomer buffering proteins. Insights from overexpression studies
    • Sun H.Q., Kwiatkowska K., and Yin H.L. beta-Thymosins are not simple actin monomer buffering proteins. Insights from overexpression studies. 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
  • 51
    • 15444365811 scopus 로고    scopus 로고
    • MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions
    • Tapp H., Al Naggar I.M., Yarmola E.G., Harrison A., Shaw G., Edison A.S., and Bubb M.R. MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions. J Biol Chem 280 (2005) 9946-9956
    • (2005) J Biol Chem , vol.280 , pp. 9946-9956
    • Tapp, H.1    Al Naggar, I.M.2    Yarmola, E.G.3    Harrison, A.4    Shaw, G.5    Edison, A.S.6    Bubb, M.R.7
  • 52
    • 4644284610 scopus 로고    scopus 로고
    • Tetrathymosinbeta is required for actin dynamics in Caenorhabditis elegans and acts via functionally different actin-binding repeats
    • Van Troys M., Ono K., Dewitte D., Jonckheere V., De Ruyck N., Vandekerckhove J., Ono S., and Ampe C. Tetrathymosinbeta is required for actin dynamics in Caenorhabditis elegans and acts via functionally different actin-binding repeats. Mol Biol Cell 15 (2004) 4735-4748
    • (2004) Mol Biol Cell , vol.15 , pp. 4735-4748
    • Van Troys, M.1    Ono, K.2    Dewitte, D.3    Jonckheere, V.4    De Ruyck, N.5    Vandekerckhove, J.6    Ono, S.7    Ampe, C.8
  • 53
    • 18644374367 scopus 로고    scopus 로고
    • + current produced by one-trial in vitro conditioning of Hermissenda
    • + current produced by one-trial in vitro conditioning of Hermissenda. J Neurosci 25 (2005) 4793-4800
    • (2005) J Neurosci , vol.25 , pp. 4793-4800
    • Yamoah, E.N.1    Levic, S.2    Redell, J.B.3    Crow, T.4
  • 54
    • 0034623126 scopus 로고    scopus 로고
    • Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A
    • Yarmola E.G., Somasundaram T., Boring T.A., Spector I., and Bubb M.R. Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J Biol Chem 275 (2000) 28120-28127
    • (2000) J Biol Chem , vol.275 , pp. 28120-28127
    • Yarmola, E.G.1    Somasundaram, T.2    Boring, T.A.3    Spector, I.4    Bubb, M.R.5


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