메뉴 건너뛰기




Volumn 35, Issue 2, 1996, Pages 134-146

Differences in the Regulation of Microtubule Dynamics by Microtubule-Associated Proteins MAP1B and MAP2

Author keywords

Computer simulations; Critical concentration; Dynamic instability; Lateral cap model; Lattice stabilization

Indexed keywords

SUIDAE;

EID: 0030332245     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(1996)35:2<134::AID-CM6>3.0.CO;2-A     Document Type: Article
Times cited : (55)

References (46)
  • 1
    • 0028324308 scopus 로고
    • Inhibition of microtubule nucleation at the neuronal centrosome compromises axon growth
    • Ahmad, F.J. (1994): Inhibition of microtubule nucleation at the neuronal centrosome compromises axon growth. Neuron 12:271-280.
    • (1994) Neuron , vol.12 , pp. 271-280
    • Ahmad, F.J.1
  • 2
    • 0029093287 scopus 로고
    • Microtubules released from the neuronal centrosome are transported into the axon
    • Ahmad, F.J., and Baas, P.W. (1995): Microtubules released from the neuronal centrosome are transported into the axon. J. Cell Sci. 108:2761-2769.
    • (1995) J. Cell Sci. , vol.108 , pp. 2761-2769
    • Ahmad, F.J.1    Baas, P.W.2
  • 3
    • 0027403193 scopus 로고
    • Regional differences in microtubule dynamics in the axon
    • Ahmad, F.J., Pienkowski, T.P., and Baas, P.W. (1993): Regional differences in microtubule dynamics in the axon. J. Neurosci. 13:856-866.
    • (1993) J. Neurosci. , vol.13 , pp. 856-866
    • Ahmad, F.J.1    Pienkowski, T.P.2    Baas, P.W.3
  • 4
    • 0025103402 scopus 로고
    • Microtubule dynamic instability: Numerical simulation of microtubule transition properties using a lateral cap model
    • Bayley, P.M., Schilstra, M.J., and Martin, S.R. (1990): Microtubule dynamic instability: numerical simulation of microtubule transition properties using a lateral cap model. J. Cell Sci. 95:33-48.
    • (1990) J. Cell Sci. , vol.95 , pp. 33-48
    • Bayley, P.M.1    Schilstra, M.J.2    Martin, S.R.3
  • 5
    • 0000146079 scopus 로고
    • Microtubule-associated protein IB: Identification of a major component of the neuronal cytoskeleton
    • Bloom, G.S., Luca, P.C., and Vallee, R.B. (1985): Microtubule-associated protein IB: identification of a major component of the neuronal cytoskeleton. Proc. Natl. Acad. Sci. U.S.A. 82:5404-5408.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 5404-5408
    • Bloom, G.S.1    Luca, P.C.2    Vallee, R.B.3
  • 6
    • 0025886404 scopus 로고
    • Assembly of chick brain MAP2-tubulin microtubule protein. Characterization of the protein and the MAP2-dependent addition of tubulin dimers
    • Burns, R.G. (1991): Assembly of chick brain MAP2-tubulin microtubule protein. Characterization of the protein and the MAP2-dependent addition of tubulin dimers. Biochemistry J. 277:231-238.
    • (1991) Biochemistry J. , vol.277 , pp. 231-238
    • Burns, R.G.1
  • 7
    • 0022066949 scopus 로고
    • A microtubule-associated protein (MAP1) which is expressed at elevated levels during development of the rat cerebellum
    • Calvert, R. and Anderton, B.H. (1985): A microtubule-associated protein (MAP1) which is expressed at elevated levels during development of the rat cerebellum. EMBO J. 4:1171-1176.
    • (1985) EMBO J. , vol.4 , pp. 1171-1176
    • Calvert, R.1    Anderton, B.H.2
  • 8
    • 0019486594 scopus 로고
    • Conformation and assembly characteristics of tubulin and microtubule protein from bovine brain
    • Clark D.C., Martin, S.R., and Bayley, P.M. (1981): Conformation and assembly characteristics of tubulin and microtubule protein from bovine brain. Biochemistry 20:1924-1932.
    • (1981) Biochemistry , vol.20 , pp. 1924-1932
    • Clark, D.C.1    Martin, S.R.2    Bayley, P.M.3
  • 9
    • 0017649032 scopus 로고
    • Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
    • Cleveland, D.W., Hwo, S.-Y., and Kirschner, M.W. (1977): Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J. Mol. Biol. 116:207-225.
    • (1977) J. Mol. Biol. , vol.116 , pp. 207-225
    • Cleveland, D.W.1    Hwo, S.-Y.2    Kirschner, M.W.3
  • 10
    • 0028281029 scopus 로고
    • A protein related to brain microtubule-associated protein MAP1B is a component of the mammalian centrosome
    • Dominguez, J.E., Buendia, B., López-Otín, C., Antony, C., Karsenti, E., and Avila, J. (1994): A protein related to brain microtubule-associated protein MAP1B is a component of the mammalian centrosome. J. Cell Sci. 107:601-611.
    • (1994) J. Cell Sci. , vol.107 , pp. 601-611
    • Dominguez, J.E.1    Buendia, B.2    López-Otín, C.3    Antony, C.4    Karsenti, E.5    Avila, J.6
  • 11
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D.N., Hyman, A.A., Cobb, M.H., and Kirschner, M.W. (1992): Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Cell. Biol. 3:1141-1154.
    • (1992) Mol. Cell. Biol. , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 12
    • 0019474894 scopus 로고
    • The role of subunit entropy in cooperative assembly. Nucleation of microtubules and other two-dimensional polymers
    • Erickson, H.P., and Pantaloni, D. (1981): The role of subunit entropy in cooperative assembly. Nucleation of microtubules and other two-dimensional polymers. Biophys. J. 34:293-309.
    • (1981) Biophys. J. , vol.34 , pp. 293-309
    • Erickson, H.P.1    Pantaloni, D.2
  • 13
    • 0023199264 scopus 로고
    • Phase dynamics at microtubule ends: The coexistence of microtubule length changes and treadmilling
    • Farrell, K.W., Jordan, M.A., Miller, H.P., and Wilson, L. (1987) Phase dynamics at microtubule ends: the coexistence of microtubule length changes and treadmilling. J. Cell Biol. 104:1035-1046.
    • (1987) J. Cell Biol. , vol.104 , pp. 1035-1046
    • Farrell, K.W.1    Jordan, M.A.2    Miller, H.P.3    Wilson, L.4
  • 15
    • 0022492523 scopus 로고
    • Visualisation of the dynamic instability of individual microtubules by dark-field microscopy
    • Horio, T., and Hotani, H. (1986): Visualisation of the dynamic instability of individual microtubules by dark-field microscopy. Nature 321:605-607.
    • (1986) Nature , vol.321 , pp. 605-607
    • Horio, T.1    Hotani, H.2
  • 16
    • 0023688553 scopus 로고
    • Dynamics of microtubules visualised by dark-field microscopy: Treadmilling and dynamic instability
    • Hotani, H., and Horio, T. (1988): Dynamics of microtubules visualised by dark-field microscopy: treadmilling and dynamic instability. Cell Motil. Cytoskeleton 10:229-236.
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 229-236
    • Hotani, H.1    Horio, T.2
  • 17
    • 0028132184 scopus 로고
    • Microtubule-stabilizing activity of microtubule-associated proteins (MAPs) is due to increase in frequency of rescue in dynamic instability: Shortening length decreases with binding of MAPs onto microtubules
    • Itoh, T.J., and Hotani, H. (1994) Microtubule-stabilizing activity of microtubule-associated proteins (MAPs) is due to increase in frequency of rescue in dynamic instability: shortening length decreases with binding of MAPs onto microtubules. Cell Struct. Funct. 19:279-290.
    • (1994) Cell Struct. Funct. , vol.19 , pp. 279-290
    • Itoh, T.J.1    Hotani, H.2
  • 18
    • 0022370234 scopus 로고
    • Generation of microtubule stability subclasses by microtubule-associated proteins: Implications for the microtubule "dynamic instability" model
    • Job, D., Pabion, M., and Margolis, R.L. (1985): Generation of microtubule stability subclasses by microtubule-associated proteins: implications for the microtubule "dynamic instability" model. J. Cell Biol. 101:1680-1689.
    • (1985) J. Cell Biol. , vol.101 , pp. 1680-1689
    • Job, D.1    Pabion, M.2    Margolis, R.L.3
  • 19
    • 0025134481 scopus 로고
    • Traces of brain microtubule-associated proteins affect dynamic properties of microtubules
    • Keates, R.A.B. (1990): Traces of brain microtubule-associated proteins affect dynamic properties of microtubules. Biochem. Cell Biol. 68:1202-1209.
    • (1990) Biochem. Cell Biol. , vol.68 , pp. 1202-1209
    • Keates, R.A.B.1
  • 20
    • 0027285334 scopus 로고
    • Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly
    • Kowalski, R.J., and Williams, R.C. (1993): Microtubule-associated protein 2 alters the dynamic properties of microtubule assembly and disassembly. J. Biol. Chem. 268:9847-9855.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9847-9855
    • Kowalski, R.J.1    Williams, R.C.2
  • 21
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen, J. (1984): Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 10:203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970): Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0027199079 scopus 로고
    • Dynamic instability of microtubules: Monte Carlo simulation and application to different types of microtubule lattice
    • Martin, S.R., Schilstra, M.J., and Bayley, P.M. (1993): Dynamic instability of microtubules: Monte Carlo simulation and application to different types of microtubule lattice. Biophys. J. 64:578-596.
    • (1993) Biophys. J. , vol.64 , pp. 578-596
    • Martin, S.R.1    Schilstra, M.J.2    Bayley, P.M.3
  • 24
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T., and Kirschner, M.W. (1984): Dynamic instability of microtubule growth. Nature 312:237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.W.2
  • 25
    • 0345432759 scopus 로고
    • Association of high-molecular-weight proteins with microtubules and their role in microtubule assembly in vitro
    • Murphy, D.B., and Borisy, G.G. (1975): Association of high-molecular-weight proteins with microtubules and their role in microtubule assembly in vitro. Proc. Natl. Acad. Sci. U.S.A. 72:2696-2700.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 2696-2700
    • Murphy, D.B.1    Borisy, G.G.2
  • 26
    • 0017718447 scopus 로고
    • Role of tubulin-associated proteins in microtubule nucleation and elongation
    • Murphy, D.B., Johnson, K.A., and Borisy, G.G. (1977): Role of tubulin-associated proteins in microtubule nucleation and elongation. J. Mol. Biol. 117:33-52.
    • (1977) J. Mol. Biol. , vol.117 , pp. 33-52
    • Murphy, D.B.1    Johnson, K.A.2    Borisy, G.G.3
  • 27
    • 0029098802 scopus 로고
    • Kinetic stabilization of microtubule dynamics at steady-state by tau and microtubule-binding domains of tau
    • Panda, D., Goode, B.L., Feinstein, S.C., and Wilson, L. (1995): Kinetic stabilization of microtubule dynamics at steady-state by tau and microtubule-binding domains of tau. Biochemistry 34:11117-11127.
    • (1995) Biochemistry , vol.34 , pp. 11117-11127
    • Panda, D.1    Goode, B.L.2    Feinstein, S.C.3    Wilson, L.4
  • 28
    • 0022557194 scopus 로고
    • Involvement of guanosine triphosphate (GTP) hydrolysis in the mechanism of tubulin polymerization: Regulation of microtubule dynamics at steady-state by a GTP cap
    • Pantaloni, D., and Carlier, M.-F. (1986): Involvement of guanosine triphosphate (GTP) hydrolysis in the mechanism of tubulin polymerization: regulation of microtubule dynamics at steady-state by a GTP cap. Ann. N.Y. Acad. Sci. 466:496-509.
    • (1986) Ann. N.Y. Acad. Sci. , vol.466 , pp. 496-509
    • Pantaloni, D.1    Carlier, M.-F.2
  • 29
    • 0028007526 scopus 로고
    • Purified native microtubule associated protein MAP1A: Kinetics of microtubule assembly and MAP1A/tubulin stoichiometry
    • Pedrotti, B., and Islam, K. (1994): Purified native microtubule associated protein MAP1A: kinetics of microtubule assembly and MAP1A/tubulin stoichiometry. Biochemistry 33:12463-12470.
    • (1994) Biochemistry , vol.33 , pp. 12463-12470
    • Pedrotti, B.1    Islam, K.2
  • 30
    • 0028954795 scopus 로고
    • Purification of microtubule associated protein MAP1B from bovine brain: MAP1B binds to microtubules but not to microfilaments
    • Pedrotti, B. and Islam, K. (1995a): Purification of microtubule associated protein MAP1B from bovine brain: MAP1B binds to microtubules but not to microfilaments. Cell Motil. Cytoskeleton 30:301-309.
    • (1995) Cell Motil. Cytoskeleton , vol.30 , pp. 301-309
    • Pedrotti, B.1    Islam, K.2
  • 31
    • 0028977919 scopus 로고
    • Microtubule associated protein 1B (MAP1B) promotes efficient tubulin polymerisation in vitro
    • Pedrotti, B., and Islam, K. (1995b): Microtubule associated protein 1B (MAP1B) promotes efficient tubulin polymerisation in vitro. FEBS Lett. 371:29-31.
    • (1995) FEBS Lett. , vol.371 , pp. 29-31
    • Pedrotti, B.1    Islam, K.2
  • 32
    • 0028110888 scopus 로고
    • Interactions of microtubule-associated protein MAP2 with unpolymerized and polymerized tubulin and actin using a 96-well microtiter plate solid-phase immunoassay
    • Pedrotti, B., Colombo, R., and Islam, K. (1994): Interactions of microtubule-associated protein MAP2 with unpolymerized and polymerized tubulin and actin using a 96-well microtiter plate solid-phase immunoassay. Biochemistry 33:8798-8806.
    • (1994) Biochemistry , vol.33 , pp. 8798-8806
    • Pedrotti, B.1    Colombo, R.2    Islam, K.3
  • 33
    • 0029869272 scopus 로고    scopus 로고
    • Characterization of microtubule-associated protein MAP1B: Phosphorylation state, light chains, and binding to microtubules
    • Pedrotti, B., Ulloa, L., Avila, J., and Islam, K. (1996): Characterization of microtubule-associated protein MAP1B: phosphorylation state, light chains, and binding to microtubules. Biochemistry 35:3016-3023.
    • (1996) Biochemistry , vol.35 , pp. 3016-3023
    • Pedrotti, B.1    Ulloa, L.2    Avila, J.3    Islam, K.4
  • 34
    • 0027048607 scopus 로고
    • Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro. Real-time observations using video microscopy
    • Pryer, N.K., Walker, R.A., Skeen, V.P., Bourns, B.D., Soboeiro, M.F., and Salmon, E.D. (1992): Brain microtubule-associated proteins modulate microtubule dynamic instability in vitro. Real-time observations using video microscopy. J Cell Sci. 103:965-976.
    • (1992) J Cell Sci. , vol.103 , pp. 965-976
    • Pryer, N.K.1    Walker, R.A.2    Skeen, V.P.3    Bourns, B.D.4    Soboeiro, M.F.5    Salmon, E.D.6
  • 35
    • 0022972987 scopus 로고
    • MAPS: A novel brain microtubule-associated protein under strong development regulation
    • Riederer, B.M., Cohen, R., and Matus, A. (1986): MAPS: a novel brain microtubule-associated protein under strong development regulation. J. Neurocytol. 15:763-775.
    • (1986) J. Neurocytol. , vol.15 , pp. 763-775
    • Riederer, B.M.1    Cohen, R.2    Matus, A.3
  • 36
    • 0028822622 scopus 로고
    • Characterization of microtubule-associated protein phosphoisoforms present in isolated growth cones
    • Rocha, M.G., and Avila, J. (1995): Characterization of microtubule-associated protein phosphoisoforms present in isolated growth cones. Dev. Brain Res. 89:47-55.
    • (1995) Dev. Brain Res. , vol.89 , pp. 47-55
    • Rocha, M.G.1    Avila, J.2
  • 37
    • 0025823655 scopus 로고
    • The effect of solution composition on microtubule dynamic instability
    • Schilstra M.J., Bayley, P.M., and Martin, S.R. (1991): The effect of solution composition on microtubule dynamic instability. Biochem. J. 277:839-847.
    • (1991) Biochem. J. , vol.277 , pp. 839-847
    • Schilstra, M.J.1    Bayley, P.M.2    Martin, S.R.3
  • 38
    • 0024410833 scopus 로고
    • MAP1A and MAP1B are structurally related microtubule associated proteins with distinct developmental patterns in the CNS
    • Schoenfeld, T.A., McKerracher, L., Obar, R., and Vallee, R.B. (1989): MAP1A and MAP1B are structurally related microtubule associated proteins with distinct developmental patterns in the CNS. J. Neurosci. 9:1712-1730.
    • (1989) J. Neurosci. , vol.9 , pp. 1712-1730
    • Schoenfeld, T.A.1    McKerracher, L.2    Obar, R.3    Vallee, R.B.4
  • 39
    • 0017107172 scopus 로고
    • Microtubule-associated proteins and the stimulation of tubulin assembly in vitro
    • Sloboda, R.D., Denter, W.L., and Rosenbaum, J.L. (1976): Microtubule-associated proteins and the stimulation of tubulin assembly in vitro. Biochemistry 15:4497-4505.
    • (1976) Biochemistry , vol.15 , pp. 4497-4505
    • Sloboda, R.D.1    Denter, W.L.2    Rosenbaum, J.L.3
  • 40
    • 0025913867 scopus 로고
    • Assembly of chick brain MAP2-tubulin microtubule protein. Analysis of tubulin subunit flux rates by immunofluorescence microscopy
    • Symmons, M.F., and Burns, R.G. (1991): Assembly of chick brain MAP2-tubulin microtubule protein. Analysis of tubulin subunit flux rates by immunofluorescence microscopy. Biochem. J. 277:245-253.
    • (1991) Biochem. J. , vol.277 , pp. 245-253
    • Symmons, M.F.1    Burns, R.G.2
  • 41
    • 0025930998 scopus 로고
    • Microtubule behaviour in the growth cones of living neurons during axon elongation
    • Tanaka, E.M., and Kirschner, M.W. (1991): Microtubule behaviour in the growth cones of living neurons during axon elongation. J Cell Biol. 115:345-363.
    • (1991) J Cell Biol. , vol.115 , pp. 345-363
    • Tanaka, E.M.1    Kirschner, M.W.2
  • 42
    • 0028820411 scopus 로고
    • Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules
    • Trinczek, B., Biernat, J., Baumann, K., Mandelkow, E.-M., and Mandelkow, E. (1995): Domains of tau protein, differential phosphorylation, and dynamic instability of microtubules. Mol. Biol. Cell 6:1887-1902.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1887-1902
    • Trinczek, B.1    Biernat, J.2    Baumann, K.3    Mandelkow, E.-M.4    Mandelkow, E.5
  • 43
    • 0028917703 scopus 로고
    • Regulation of microtubule dynamic instability by tubulin-GDP
    • Vandecandelaere, A., Martin, S.R., and Bayley, P.M. (1995): Regulation of microtubule dynamic instability by tubulin-GDP. Biochemistry 34:1332-1343.
    • (1995) Biochemistry , vol.34 , pp. 1332-1343
    • Vandecandelaere, A.1    Martin, S.R.2    Bayley, P.M.3
  • 44
    • 0028062756 scopus 로고
    • XMAP from Xenopus eggs promotes rapid plus end assembly of microtubules and rapid microtubule polymer turnover
    • Vasquez, R.J., Gard, D.L., and Cassimeris, L. (1994): XMAP from Xenopus eggs promotes rapid plus end assembly of microtubules and rapid microtubule polymer turnover, J. Cell Biol. 127:985-993.
    • (1994) J. Cell Biol. , vol.127 , pp. 985-993
    • Vasquez, R.J.1    Gard, D.L.2    Cassimeris, L.3
  • 45
    • 0027218491 scopus 로고
    • The mechanism of equilibrium binding of microtubule-associated protein 2 to microtubules
    • Wallis, K.T., Azhar, S., Rho, M.B., Lewis, S.A., Cowan, N.J., and Murphy, D.C.B. (1993): The mechanism of equilibrium binding of microtubule-associated protein 2 to microtubules. J. Biol. Chem. 268:15158-15167.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15158-15167
    • Wallis, K.T.1    Azhar, S.2    Rho, M.B.3    Lewis, S.A.4    Cowan, N.J.5    Murphy, D.C.B.6
  • 46
    • 0027474128 scopus 로고
    • Reduction in microtubule dynamics in vitro by brain microtubule-associated proteins and by a microtubule-associated protein-2 second repeated sequence analogue
    • Yamauchi, P.S., Flynn, G.C., Marsh, R.L., and Purich, D.L. (1993): Reduction in microtubule dynamics in vitro by brain microtubule-associated proteins and by a microtubule-associated protein-2 second repeated sequence analogue. J Neurochem. 60:817-826.
    • (1993) J Neurochem. , vol.60 , pp. 817-826
    • Yamauchi, P.S.1    Flynn, G.C.2    Marsh, R.L.3    Purich, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.