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Volumn 66, Issue 3, 1996, Pages 1207-1213

Activation of cyclic AMP-dependent protein kinase in okadaic acid-treated neurons potentiates neurofilament fragmentation and stimulates phosphorylation of Ser2 in the low-molecular-mass neurofilament subunit

Author keywords

Neurofilament; Okadaic acid; Phosphatase; Phosphorylation; Protein kinase A

Indexed keywords

CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE;

EID: 0030065110     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66031207.x     Document Type: Article
Times cited : (33)

References (30)
  • 1
    • 0024600639 scopus 로고
    • Assembly and exchange of intermediate filament proteins of neurons: Neurofilaments are dynamic structures
    • Angelides K. J., Smith K. E., and Takeda M. (1989) Assembly and exchange of intermediate filament proteins of neurons: neurofilaments are dynamic structures. J. Cell Biol. 108, 1495-1506.
    • (1989) J. Cell Biol. , vol.108 , pp. 1495-1506
    • Angelides, K.J.1    Smith, K.E.2    Takeda, M.3
  • 2
    • 0021867264 scopus 로고
    • The structure, biochemical properties, and immunogenicity of neurofilament peripheral regions are determined by phosphorylation state
    • Carden M. J., Schlaepfer 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. 260, 9805-9817.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9805-9817
    • Carden, M.J.1    Schlaepfer, W.W.2    Lee, V.M.-Y.3
  • 3
    • 0024787034 scopus 로고
    • Expression of rat neurofilament proteins NF-L and NF-M in transfected nonneuronal cells
    • Chin S. S. M. and Liem R. K. H. (1989) Expression of rat neurofilament proteins NF-L and NF-M in transfected nonneuronal cells. Eur. J. Cell Biol. 50, 475-490.
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 475-490
    • Chin, S.S.M.1    Liem, R.K.H.2
  • 4
    • 0025514319 scopus 로고
    • Transfected rat high-molecular-weight neurofilament (NF-H) coassembles with vimentin in a predominantly nonphosphorylated form
    • Chin S. S. M. and Liem R. K. H. (1990) Transfected rat high-molecular-weight neurofilament (NF-H) coassembles with vimentin in a predominantly nonphosphorylated form. J. Neurosci. 10, 3714-3726.
    • (1990) J. Neurosci. , vol.10 , pp. 3714-3726
    • Chin, S.S.M.1    Liem, R.K.H.2
  • 6
    • 0024361302 scopus 로고
    • An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues
    • Cohen P., Klumpp S., and Schelling D. L. (1989) An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues. FEBS Lett. 250, 596-600.
    • (1989) FEBS Lett. , vol.250 , pp. 596-600
    • Cohen, P.1    Klumpp, S.2    Schelling, D.L.3
  • 7
    • 0026606341 scopus 로고
    • Association of cyclin-AMP-dependent protein kinase with neurofilaments
    • Dosemeci A. and Pant H. C. (1992) Association of cyclin-AMP-dependent protein kinase with neurofilaments. Biochem. J. 282, 477-481.
    • (1992) Biochem. J. , vol.282 , pp. 477-481
    • Dosemeci, A.1    Pant, H.C.2
  • 8
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • Fuchs E. and Weber K. (1994) Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63, 345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 9
    • 0021092750 scopus 로고
    • Neurofilament architecture combines structural principles of intermediate filaments with carboxy-terminal extensions increasing in size between triplet proteins
    • Geisler N., Kaufmann E., Fischer S., Plessmann U., and Weber K. (1983) Neurofilament architecture combines structural principles of intermediate filaments with carboxy-terminal extensions increasing in size between triplet proteins. EMBO J. 2, 1295-1302.
    • (1983) EMBO J. , vol.2 , pp. 1295-1302
    • Geisler, N.1    Kaufmann, E.2    Fischer, S.3    Plessmann, U.4    Weber, K.5
  • 10
    • 0022547173 scopus 로고
    • Dephosphorylation of neurofilaments by exogenous phosphatases has no effect on reassembly of subunits
    • Georges E., Levebvre S., and Mushynski W. E. (1986) Dephosphorylation of neurofilaments by exogenous phosphatases has no effect on reassembly of subunits. J. Neurochem. 47, 477-483.
    • (1986) J. Neurochem. , vol.47 , pp. 477-483
    • Georges, E.1    Levebvre, S.2    Mushynski, W.E.3
  • 13
    • 0025220189 scopus 로고
    • Effects of phosphorylation on the neurofilament L protein on filamentous structures
    • Hisanaga S., Gonda Y., Inagaki M., Ikai A., and Hirokawa N. (1990) Effects of phosphorylation on the neurofilament L protein on filamentous structures. Cell Regul. 1, 237-248.
    • (1990) Cell Regul. , vol.1 , pp. 237-248
    • Hisanaga, S.1    Gonda, Y.2    Inagaki, M.3    Ikai, A.4    Hirokawa, N.5
  • 14
    • 0028226737 scopus 로고
    • Phosphorylation of native and reassembled neurofilaments composed of NF-L, NF-M, and NF-H by the catalytic subunit of cAMP-dependent protein kinase
    • Hisanaga S., Matsuoka Y., Nishizawa K., Saito T., Inagaki M., and Hirokawa N. (1994) Phosphorylation of native and reassembled neurofilaments composed of NF-L, NF-M, and NF-H by the catalytic subunit of cAMP-dependent protein kinase. Mol. Biol. Cell 5, 161-172.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 161-172
    • Hisanaga, S.1    Matsuoka, Y.2    Nishizawa, K.3    Saito, T.4    Inagaki, M.5    Hirokawa, N.6
  • 15
    • 0016541063 scopus 로고
    • The slow component of axonal transport; identification of major structural polypeptides of the axon and their generality among mammalian neurons
    • Hoffman P. N. and Lasek R. J. (1975) The slow component of axonal transport; identification of major structural polypeptides of the axon and their generality among mammalian neurons. J. Cell Biol. 66, 351-366.
    • (1975) J. Cell Biol. , vol.66 , pp. 351-366
    • Hoffman, P.N.1    Lasek, R.J.2
  • 17
    • 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
  • 18
    • 0020519940 scopus 로고
    • The distribution of phosphorylation sites among identified proteolytic fragments of mammalian neurofilaments
    • Julien J.-P. and Mushynski W. E. (1983) The distribution of phosphorylation sites among identified proteolytic fragments of mammalian neurofilaments. J. Biol. Chem. 258, 4019-4025.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4019-4025
    • Julien, J.-P.1    Mushynski, W.E.2
  • 19
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly P. J. and Krebs E. G. (1991) Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J. Biol. Chem 266, 15555-15558.
    • (1991) J. Biol. Chem , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0023154089 scopus 로고
    • Nerve growth factor enhances the synthesis, phosphorylation, and metabolic stability of neurofilament proteins in PC12 cells
    • Lindenbaum M. L., Carbonetto S., and Mushynski W. E. (1987) Nerve growth factor enhances the synthesis, phosphorylation, and metabolic stability of neurofilament proteins in PC12 cells. J. Biol. Chem. 262, 605-610.
    • (1987) J. Biol. Chem. , vol.262 , pp. 605-610
    • Lindenbaum, M.L.1    Carbonetto, S.2    Mushynski, W.E.3
  • 22
    • 0025196189 scopus 로고
    • Effect of phosphorylation on 68 kDa neurofilament subunit protein assembly by the cyclic AMP dependent protein kinase in vitro
    • Nakamura Y., Takeda M., Angelides K. J., Tanaka T., Tada K., and Nishimura T. (1990) Effect of phosphorylation on 68 kDa neurofilament subunit protein assembly by the cyclic AMP dependent protein kinase in vitro. Biochem. Biophys. Res. Commun. 169, 744-750.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 744-750
    • Nakamura, Y.1    Takeda, M.2    Angelides, K.J.3    Tanaka, T.4    Tada, K.5    Nishimura, T.6
  • 23
    • 0023389378 scopus 로고
    • Complete amino acid sequence and in vitro expression of rat NF-M, the middle molecular weight neurofilament protein
    • Napolitano E. W., Chin S. S. M., Colman D. R., and Liem R. K. H. (1987) Complete amino acid sequence and in vitro expression of rat NF-M, the middle molecular weight neurofilament protein. J. Neurosci. 7, 2590-2599.
    • (1987) J. Neurosci. , vol.7 , pp. 2590-2599
    • Napolitano, E.W.1    Chin, S.S.M.2    Colman, D.R.3    Liem, R.K.H.4
  • 24
    • 0026779629 scopus 로고
    • Okadaic acid induces the rapid and reversible disruption of the neurofilament network in rat dorsal root ganglion neurons
    • Sacher M. G., Athlan E. S., and Mushynski W. E. (1992) Okadaic acid induces the rapid and reversible disruption of the neurofilament network in rat dorsal root ganglion neurons. Biochem. Biophys Res. Commun. 186, 524-530.
    • (1992) Biochem. Biophys Res. Commun. , vol.186 , pp. 524-530
    • Sacher, M.G.1    Athlan, E.S.2    Mushynski, W.E.3
  • 25
    • 0028227860 scopus 로고
    • Increased phosphorylation of the amino-terminal domain of the low molecular weight neurofilament subunit in okadaic acid-treated neurons
    • Sacher M. G., Athlan E. S., and Mushynski W. E. (1994) Increased phosphorylation of the amino-terminal domain of the low molecular weight neurofilament subunit in okadaic acid-treated neurons. J. Biol. Chem. 269, 18480-18484.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18480-18484
    • Sacher, M.G.1    Athlan, E.S.2    Mushynski, W.E.3
  • 26
    • 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
  • 27
    • 0025950711 scopus 로고
    • Identification of Ser-55 as a major protein kinase A phosphorylation site on the 70-kDa subunit of neurofilaments
    • Sihag R. K. and Nixon R. A. (1991) Identification of Ser-55 as a major protein kinase A phosphorylation site on the 70-kDa subunit of neurofilaments. J. Biol. Chem. 266, 18861-18867.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18861-18867
    • Sihag, R.K.1    Nixon, R.A.2
  • 28
    • 0023916538 scopus 로고
    • Phosphorylation of neurofilament proteins by protein kinase C
    • Sihag R. K., Jeng A. Y., 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.Y.2    Nixon, R.A.3
  • 29
    • 0020851516 scopus 로고
    • A batchwise purification procedure of neurofilament proteins
    • Tokutake S., Hutchison S. B., Pachter J. S., and Liem R. K. H. (1983) A batchwise purification procedure of neurofilament proteins. Anal. Biochem. 135, 102-105.
    • (1983) Anal. Biochem. , vol.135 , pp. 102-105
    • Tokutake, S.1    Hutchison, S.B.2    Pachter, J.S.3    Liem, R.K.H.4
  • 30
    • 0015217645 scopus 로고
    • Purification and characterization of a protein inhibitor of adenosine 3′,5′-monophosphate-dependent protein kinases
    • Walsh D. A., Ashby C. D , Gonzalez C., Calkins D., Fischer E. H., and Krebs E. G. (1971) Purification and characterization of a protein inhibitor of adenosine 3′,5′-monophosphate-dependent protein kinases. J. Biol. Chem. 246, 1977-1985.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1977-1985
    • Walsh, D.A.1    Ashby, C.D.2    Gonzalez, C.3    Calkins, D.4    Fischer, E.H.5    Krebs, E.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.