메뉴 건너뛰기




Volumn 66, Issue 3, 1996, Pages 1214-1221

Phosphorylation of neurofilament proteins in isolated goldfish mauthner axoplasm

Author keywords

Kinase; Neurofilament; Phosphorylation

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE;

EID: 0030022295     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66031214.x     Document Type: Article
Times cited : (5)

References (50)
  • 1
    • 0025329230 scopus 로고
    • Effect of temperature on long term survival of anucleate giant axons in crayfish and goldfish
    • Blundon J. A., Sheller R. A., Moehlenbruck J. W., and Bittner G. D (1990) Effect of temperature on long term survival of anucleate giant axons in crayfish and goldfish. J. Comp. Neurol. 297, 1-14.
    • (1990) J. Comp. Neurol. , vol.297 , pp. 1-14
    • Blundon, J.A.1    Sheller, R.A.2    Moehlenbruck, J.W.3    Bittner, G.D.4
  • 2
    • 0024365695 scopus 로고
    • Properties of several protein kinases that copurify with rat spinal cord neurofilaments
    • Caputo C. B., Sygowski L. A., Brunner W. F., Scott C. W., and Salama A. I. (1989) Properties of several protein kinases that copurify with rat spinal cord neurofilaments. Biochim. Biophys. Acta 1012, 299-307.
    • (1989) Biochim. Biophys. Acta , vol.1012 , pp. 299-307
    • Caputo, C.B.1    Sygowski, L.A.2    Brunner, W.F.3    Scott, C.W.4    Salama, A.I.5
  • 3
    • 0021867264 scopus 로고
    • The structure, biochemical properties, and immunogenicity of neurofilament peripheral regions are determined by phosphorylation state
    • Carden M. J., Schiaepfer W. W., and Lee V. M.-Y. (1985) The structure, biochemical properties, and immunogenicity of neurofilament peripheral regions are determined by phosphorylation state. J. Biol. Chem. 200, 9805-9817.
    • (1985) J. Biol. Chem. , vol.200 , pp. 9805-9817
    • Carden, M.J.1    Schiaepfer, W.W.2    Lee, V.M.-Y.3
  • 4
    • 0025248571 scopus 로고
    • Inhibition of forskolin-induced outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependem protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PCI2D pheochromocytoma cells
    • Chijiwa T., Mishima A., Hagiwara M., Sano M., Hayashi K., Inoue T., Naito K , Toshioka T., and Hidaka H. (1990) Inhibition of forskolin-induced outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependem protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PCI2D pheochromocytoma cells. J. Biol. Chem. 265, 5267-5272.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5267-5272
    • Chijiwa, T.1    Mishima, A.2    Hagiwara, M.3    Sano, M.4    Hayashi, K.5    Inoue, T.6    Naito, K.7    Toshioka, T.8    Hidaka, H.9
  • 5
    • 0345301057 scopus 로고
    • Biochemistry of neurofilaments
    • Marotta C. A., ed, University of Minnesota Press, Minneapolis
    • Chiu F.-C., Goldman J. E., and Norton W. T. (1983) Biochemistry of neurofilaments, in Neurofilaments (Marotta C. A., ed), pp. 27-56. University of Minnesota Press, Minneapolis.
    • (1983) Neurofilaments , pp. 27-56
    • Chiu, F.-C.1    Goldman, J.E.2    Norton, W.T.3
  • 6
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelmating Schwann cells
    • de Waegh S. M., Lee V. M.-Y., and Brady S. T. (1992) Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelmating Schwann cells. Cell 68, 451-463.
    • (1992) Cell , vol.68 , pp. 451-463
    • De Waegh, S.M.1    Lee, V.M.-Y.2    Brady, S.T.3
  • 7
    • 0025029764 scopus 로고
    • Characterization of neurofilament-associated protein kinase activities from bovine spinal cord
    • Dosemeci A., Floyd C. C., and Pant H. C. (1990) Characterization of neurofilament-associated protein kinase activities from bovine spinal cord. Cell. Mol. Neurobiol. 10, 369-382.
    • (1990) Cell. Mol. Neurobiol. , vol.10 , pp. 369-382
    • Dosemeci, A.1    Floyd, C.C.2    Pant, H.C.3
  • 9
    • 0026334107 scopus 로고
    • Cellular and molecular biology of neuronal intermediate filaments
    • Fliegner K. H. and Liem R. K. (1991) Cellular and molecular biology of neuronal intermediate filaments. Int. Rev. Cytol. 131, 109-167.
    • (1991) Int. Rev. Cytol. , vol.131 , pp. 109-167
    • Fliegner, K.H.1    Liem, R.K.2
  • 10
    • 0025906420 scopus 로고
    • Principal neurofilament-associated protein kinase in squid axoplasm is related to casein kinase I
    • Floyd C. C., Giant P., Gallant P. E., and Pant H. C. (1991) Principal neurofilament-associated protein kinase in squid axoplasm is related to casein kinase I. J. Biol. Chem. 266, 4987-4994.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4987-4994
    • Floyd, C.C.1    Giant, P.2    Gallant, P.E.3    Pant, H.C.4
  • 11
    • 0022503140 scopus 로고
    • Calcium-activated proteolysis of neurofilament proteins in the squid giant axon
    • Gallant P. E., Pant H. C., Pruss R. M., and Gainer H. (1986) Calcium-activated proteolysis of neurofilament proteins in the squid giant axon. J. Neurochem. 46, 1573-1581.
    • (1986) J. Neurochem. , vol.46 , pp. 1573-1581
    • Gallant, P.E.1    Pant, H.C.2    Pruss, R.M.3    Gainer, H.4
  • 14
    • 0027193392 scopus 로고
    • Phosphorylation modulates calpain-mediated proteolysis and calmodulin binding of the 200-kDa and 160-kDa neurofilament proteins
    • Greenwood J. A., Troncoso J. C., Costello A. C., and Johnson G. V. W. (1993) Phosphorylation modulates calpain-mediated proteolysis and calmodulin binding of the 200-kDa and 160-kDa neurofilament proteins. J. Neurochem. 61, 191-199.
    • (1993) J. Neurochem. , vol.61 , pp. 191-199
    • Greenwood, J.A.1    Troncoso, J.C.2    Costello, A.C.3    Johnson, G.V.W.4
  • 16
    • 0025729415 scopus 로고
    • Microtubule destabilization and neurofilament phosphorylation precede dendritic sprouting after axotomy of lamprey central neurons
    • Hall G. F., Lee V. M.-Y., and Kosik K. S. (1991) Microtubule destabilization and neurofilament phosphorylation precede dendritic sprouting after axotomy of lamprey central neurons. Proc. Natl. Acad. Sci. USA 88, 5016-5020.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5016-5020
    • Hall, G.F.1    Lee, V.M.-Y.2    Kosik, K.S.3
  • 17
    • 0026452774 scopus 로고
    • Neuronal cdc2-like kinase: A cdc2-related protein kinase with predominantly neuronal expression
    • Hellmich M. R., Pant H. C., Wada E., and Battey J. F. (1992) Neuronal cdc2-like kinase: a cdc2-related protein kinase with predominantly neuronal expression. Proc. Natl. Acad. Sci USA 89, 10867-10871.
    • (1992) Proc. Natl. Acad. Sci USA , vol.89 , pp. 10867-10871
    • Hellmich, M.R.1    Pant, H.C.2    Wada, E.3    Battey, J.F.4
  • 19
    • 0021751197 scopus 로고
    • Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C
    • Hidaka H., Inagaki M., Kawamoto S., and Sasaki Y. (1984) Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C. Biochemistry 23, 5036-5041.
    • (1984) Biochemistry , vol.23 , pp. 5036-5041
    • Hidaka, H.1    Inagaki, M.2    Kawamoto, S.3    Sasaki, Y.4
  • 20
    • 0025836712 scopus 로고
    • Phosphorylation of neurofilament H subunit at the tail domain by cdc2 kinase dissociates the association to microtubules
    • Hisanaga S., Kusubata M., Okumura E., and Kishimoto T. (1991) Phosphorylation of neurofilament H subunit at the tail domain by cdc2 kinase dissociates the association to microtubules. J. Biol. Chem. 266, 21798-21803.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21798-21803
    • Hisanaga, S.1    Kusubata, M.2    Okumura, E.3    Kishimoto, T.4
  • 21
    • 0019782192 scopus 로고
    • A comparison of in vitro-and in vivo-phosphorylated neurofilament peptides
    • Julien J.-P. and Mushynski W. E. (1981) A comparison of in vitro-and in vivo-phosphorylated neurofilament peptides. J. Neurochem. 37, 1579-1585.
    • (1981) J. Neurochem. , vol.37 , pp. 1579-1585
    • Julien, J.-P.1    Mushynski, W.E.2
  • 22
    • 0020469579 scopus 로고
    • Multiple phosphorylation sites in mammalian neurofilament polypeptides
    • Julien J. P. and Mushynski W. E. (1982) Multiple phosphorylation sites in mammalian neurofilament polypeptides. J. Biol. Chem. 257, 10467-10470.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10467-10470
    • Julien, J.P.1    Mushynski, W.E.2
  • 23
    • 0021718634 scopus 로고
    • 1-(5-Isoquinolinesulfonyl)-2-methylpiperazine (H-7) is a selective inhibitor of protein kinase C in rabbit platelets
    • Kawamoto S. and Hidaka H. (1984) 1-(5-Isoquinolinesulfonyl)-2-methylpiperazine (H-7) is a selective inhibitor of protein kinase C in rabbit platelets. Biochem. Biophys. Res. Commun. 125, 258-264.
    • (1984) Biochem. Biophys. Res. Commun. , vol.125 , pp. 258-264
    • Kawamoto, S.1    Hidaka, H.2
  • 24
    • 0000937265 scopus 로고
    • Evaluation of local synthesis of axonal proteins in the goldfish Mauthner cell axon and axons of the dorsal and ventral roots of the rat in vitro
    • Koenig E. (1991) Evaluation of local synthesis of axonal proteins in the goldfish Mauthner cell axon and axons of the dorsal and ventral roots of the rat in vitro. Mol. Cell. Neurosci. 2, 384-394.
    • (1991) Mol. Cell. Neurosci. , vol.2 , pp. 384-394
    • Koenig, E.1
  • 25
    • 0022512277 scopus 로고
    • Structural similarities and differences between neurofilament proteins from five different species as revealed using monoclonal antibodies
    • Lee V. M.-Y., Carden M. J., and Schlaepfer W. W. (1986) Structural similarities and differences between neurofilament proteins from five different species as revealed using monoclonal antibodies. J. Neurosci. 6, 2179-2186.
    • (1986) J. Neurosci. , vol.6 , pp. 2179-2186
    • Lee, V.M.-Y.1    Carden, M.J.2    Schlaepfer, W.W.3
  • 27
    • 0027152211 scopus 로고
    • Bovine neurofilament-enriched preparations contain kinase activity similar to casein kinase I-neurofilament phosphorylation by casein kinase I (CKI)
    • Link W. T., Dosemeci A., Floyd C. C., and Pant H. C. (1993) Bovine neurofilament-enriched preparations contain kinase activity similar to casein kinase I-neurofilament phosphorylation by casein kinase I (CKI). Neurosci. Lett. 151, 89-93.
    • (1993) Neurosci. Lett. , vol.151 , pp. 89-93
    • Link, W.T.1    Dosemeci, A.2    Floyd, C.C.3    Pant, H.C.4
  • 28
    • 0026529403 scopus 로고
    • Phosphorylation-dependent neurofilament epitopes are reduced at the node of Ranvier
    • Mata M., Kupina N., and Fink D. J. (1992) Phosphorylation-dependent neurofilament epitopes are reduced at the node of Ranvier. J. Neurocytol. 21, 199-210.
    • (1992) J. Neurocytol. , vol.21 , pp. 199-210
    • Mata, M.1    Kupina, N.2    Fink, D.J.3
  • 29
    • 0017331761 scopus 로고
    • A colorimetric method for the determination of submicrogram quantities of protein
    • McKnight G. S. (1977) A colorimetric method for the determination of submicrogram quantities of protein. Anal. Biochem. 78, 86-92.
    • (1977) Anal. Biochem. , vol.78 , pp. 86-92
    • McKnight, G.S.1
  • 31
    • 0028053427 scopus 로고
    • Long-term survival followed by degradation of neurofilament proteins in severed goldfish Mauthner axons
    • Moehlenbruck J. W., Cummings J. A., and Bittner G. D. (1994) Long-term survival followed by degradation of neurofilament proteins in severed goldfish Mauthner axons. J. Neurobiol. 25, 1637-1651.
    • (1994) J. Neurobiol. , vol.25 , pp. 1637-1651
    • Moehlenbruck, J.W.1    Cummings, J.A.2    Bittner, G.D.3
  • 32
    • 0022909139 scopus 로고
    • Differential turnover of phosphate groups on neurofilament subunits in mammalian neurons in vivo
    • Nixon R. A. and Lewis S. E. (1986) Differential turnover of phosphate groups on neurofilament subunits in mammalian neurons in vivo. J. Biol. Chem. 261, 16298-16301.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16298-16301
    • Nixon, R.A.1    Lewis, S.E.2
  • 33
    • 0025943790 scopus 로고
    • Neurofilament phosphorylation. a new look at regulation and function
    • Nixon R. A. and Sihag R. K. (1991) Neurofilament phosphorylation. a new look at regulation and function. Trends Neurosci. 14, 501-506.
    • (1991) Trends Neurosci. , vol.14 , pp. 501-506
    • Nixon, R.A.1    Sihag, R.K.2
  • 34
    • 0019985828 scopus 로고
    • Posttranslational modification of a neurofilament protein during axoplasmic transport: Implications for regional specialization of CNS axons
    • Nixon R. A., Brown B. A., and Marotta C. A. (1982) Posttranslational modification of a neurofilament protein during axoplasmic transport: implications for regional specialization of CNS axons. J. Cell Biol. 94, 150-158.
    • (1982) J. Cell Biol. , vol.94 , pp. 150-158
    • Nixon, R.A.1    Brown, B.A.2    Marotta, C.A.3
  • 35
    • 0027931132 scopus 로고
    • Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: Influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber
    • Nixon R. A., Paskevich P. A., Sihag R. K., and Thayer C. Y. (1994) Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber. J. Cell Biol. 126, 1031-1046.
    • (1994) J. Cell Biol. , vol.126 , pp. 1031-1046
    • Nixon, R.A.1    Paskevich, P.A.2    Sihag, R.K.3    Thayer, C.Y.4
  • 36
    • 0024237394 scopus 로고
    • Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain
    • Pant H. C. (1988) Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain. Biochem. J. 256, 665-668.
    • (1988) Biochem. J. , vol.256 , pp. 665-668
    • Pant, H.C.1
  • 37
    • 0017841021 scopus 로고
    • Neurofilament protein is phosphorylated in the squid giant axon
    • Pant H. C., Shecket G., Gainer H., and Lasek R. J. (1978) Neurofilament protein is phosphorylated in the squid giant axon. J. Cell Biol. 78, R23-R27.
    • (1978) J. Cell Biol. , vol.78
    • Pant, H.C.1    Shecket, G.2    Gainer, H.3    Lasek, R.J.4
  • 38
    • 0023025498 scopus 로고
    • Characterization of a cyclic nucleotide- and calcium-independent neurofilament protein kinase activity in axoplasm from the squid giant axon
    • Pant H. C., Gallant P. E., and Gainer H. (1986) Characterization of a cyclic nucleotide- and calcium-independent neurofilament protein kinase activity in axoplasm from the squid giant axon. J. Biol. Chem. 261, 2968-2977.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2968-2977
    • Pant, H.C.1    Gallant, P.E.2    Gainer, H.3
  • 39
    • 0023912946 scopus 로고
    • Neurofilaments are spaced randomly in the radial dimensions of axons
    • Price R., Paggi P., Lasek R., and Katz M. (1988) Neurofilaments are spaced randomly in the radial dimensions of axons. J. Neurocytol. 17, 55-62.
    • (1988) J. Neurocytol. , vol.17 , pp. 55-62
    • Price, R.1    Paggi, P.2    Lasek, R.3    Katz, M.4
  • 40
    • 0028873958 scopus 로고
    • Calcium-activated proteolysis of neurofilament proteins in goldfish Mauthner axons
    • Raabe T. D., Nguyen T., and Bittner G. D. (1995) Calcium-activated proteolysis of neurofilament proteins in goldfish Mauthner axons. J. Neurobiol. 26, 253-261.
    • (1995) J. Neurobiol. , vol.26 , pp. 253-261
    • Raabe, T.D.1    Nguyen, T.2    Bittner, G.D.3
  • 41
    • 0025719976 scopus 로고
    • Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichometric ratios
    • Roder H. M. and Ingram V. M. (1991) Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichometric ratios. J. Neurosci. 11, 3325-3343.
    • (1991) J. Neurosci. , vol.11 , pp. 3325-3343
    • Roder, H.M.1    Ingram, V.M.2
  • 42
    • 0020478963 scopus 로고
    • Neurofilament protein phosphorylation: Species generality and reaction characteristics
    • Shecket G. and Lasek R. J. (1982) Neurofilament protein phosphorylation: species generality and reaction characteristics. J. Biol Chem. 257, 4788-4795.
    • (1982) J. Biol Chem. , vol.257 , pp. 4788-4795
    • Shecket, G.1    Lasek, R.J.2
  • 43
    • 0027165323 scopus 로고
    • Cdc2-like kinase from rat spinal cord specifically phosphorylates KSPXK motifs in neurofilament proteins: Isolation and characterization
    • Shetty K. T., Link W. T., and Pant H. C. (1993) cdc2-like kinase from rat spinal cord specifically phosphorylates KSPXK motifs in neurofilament proteins: isolation and characterization. Proc. Natl. Acad. Sci. USA 90, 6844-6848.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6844-6848
    • Shetty, K.T.1    Link, W.T.2    Pant, H.C.3
  • 44
    • 0024531851 scopus 로고
    • In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases
    • Sihag R. K. and Nixon R. A. (1989) In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases. J. Biol. Chem. 264, 457-464.
    • (1989) J. Biol. Chem. , vol.264 , pp. 457-464
    • Sihag, R.K.1    Nixon, R.A.2
  • 45
    • 0025257205 scopus 로고
    • Phosphorylation of the amino-terminal head domain of the middle molecular mass 145-kDa subunit of neurofilaments
    • Sihag R. K. and Nixon R A. (1990) Phosphorylation of the amino-terminal head domain of the middle molecular mass 145-kDa subunit of neurofilaments. J. Biol. Chem. 265, 4166-4171.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4166-4171
    • Sihag, R.K.1    Nixon, R.A.2
  • 46
    • 0023916538 scopus 로고
    • Phosphorylation of neurofilament proteins by protein kinase C
    • Sihag R. K., Jeng A. C., and Nixon R. A. (1988) Phosphorylation of neurofilament proteins by protein kinase C. FEBS Lett. 233, 181-185.
    • (1988) FEBS Lett. , vol.233 , pp. 181-185
    • Sihag, R.K.1    Jeng, A.C.2    Nixon, R.A.3
  • 48
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • Steinert P. M. and Roop D. R. (1988) Molecular and cellular biology of intermediate filaments. Annu. Rev. Biochem. 57, 593-625.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 50
    • 0022233712 scopus 로고
    • Phosphorylation of neurofilament proteins by endogenous calcium/ calmodulin-dependent protein kinase
    • Vallano M. L., Buckholz T. M., and DeLorenzo R. J. (1985) Phosphorylation of neurofilament proteins by endogenous calcium/ calmodulin-dependent protein kinase. Biochem. Biophys. Res. Commun. 130, 957-963.
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 957-963
    • Vallano, M.L.1    Buckholz, T.M.2    DeLorenzo, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.