메뉴 건너뛰기




Volumn 18, Issue 3, 1999, Pages 565-577

Identification of MINUS, a small polypeptide that functions as a microtubule nucleation suppressor

Author keywords

Centrosome; Cytoskeleton; Microtubules; Nucleation

Indexed keywords

PACLITAXEL; POLYPEPTIDE; TAU PROTEIN;

EID: 0033081060     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.3.565     Document Type: Article
Times cited : (20)

References (47)
  • 1
    • 0026758423 scopus 로고
    • Gamma-tubulin distribution in the neuron: Implications for the origins of neuritic microtubules
    • Baas, P.W. and Joshi, H.C. (1992) Gamma-tubulin distribution in the neuron: implications for the origins of neuritic microtubules. J. Cell Biol., 119, 171-178.
    • (1992) J. Cell Biol. , vol.119 , pp. 171-178
    • Baas, P.W.1    Joshi, H.C.2
  • 2
    • 0023039174 scopus 로고
    • Control of nucleation in microtubule self-assembly
    • Bayley, P.M., Butler, F.M. and Manser, E.J. (1986) Control of nucleation in microtubule self-assembly. FEBS Lett., 205, 230-234.
    • (1986) FEBS Lett. , vol.205 , pp. 230-234
    • Bayley, P.M.1    Butler, F.M.2    Manser, E.J.3
  • 3
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont, L.D. and Mitchison, T.J. (1996) Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell, 84, 623-631.
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 4
    • 0027406644 scopus 로고
    • Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation and bundle formation in vitro
    • Brandt, R. and Lee, G. (1993) Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation and bundle formation in vitro. J. Biol. Chem., 268, 3414-3419.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3414-3419
    • Brandt, R.1    Lee, G.2
  • 5
    • 0028785525 scopus 로고
    • Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain
    • Brandt, R., Léger, J. and Lee, G. (1995) Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol., 131, 1327-1340.
    • (1995) J. Cell Biol. , vol.131 , pp. 1327-1340
    • Brandt, R.1    Léger, J.2    Lee, G.3
  • 6
    • 0019381919 scopus 로고
    • Serial analysis of microtubules in cultured rat sensory axons
    • Bray, D. and Bunge, M.B. (1981) Serial analysis of microtubules in cultured rat sensory axons. J. Neurocytol., 10, 589-605.
    • (1981) J. Neurocytol. , vol.10 , pp. 589-605
    • Bray, D.1    Bunge, M.B.2
  • 7
    • 0023582253 scopus 로고
    • Control of microtubule nucleation and stability in Madin-Darby canine kidney cells: The occurrence of noncentrosomal, stable detyrosinated microtubules
    • Bré, M., Kreis, T.E. and Karsenti, E. (1987) Control of microtubule nucleation and stability in Madin-Darby canine kidney cells: the occurrence of noncentrosomal, stable detyrosinated microtubules. J. Cell Biol., 105, 1283-1296.
    • (1987) J. Cell Biol. , vol.105 , pp. 1283-1296
    • Bré, M.1    Kreis, T.E.2    Karsenti, E.3
  • 9
    • 0028316882 scopus 로고
    • Sense and antisense transfection analysis of tau function - Tau influences net microtubule assembly, neurite outgrowth and neuritic stability
    • Esmaeli-Azad, B., McCarty, J.H. and Feinstein, S.C. (1994) Sense and antisense transfection analysis of tau function - tau influences net microtubule assembly, neurite outgrowth and neuritic stability. J. Cell Sci., 107, 869-879.
    • (1994) J. Cell Sci. , vol.107 , pp. 869-879
    • Esmaeli-Azad, B.1    McCarty, J.H.2    Feinstein, S.C.3
  • 10
    • 0345035898 scopus 로고    scopus 로고
    • Immunofluorescence population assays for studying MAP function
    • Avila, J., Brandt, R. and Kosik, K. (eds), Harwood, Amsterdam
    • Fanara, P. and Brandt, R. (1997) Immunofluorescence population assays for studying MAP function. In Avila, J., Brandt, R. and Kosik, K. (eds), Brain Microtubule Associated Proteins: Modifications in Disease. Harwood, Amsterdam, pp. 259-273.
    • (1997) Brain Microtubule Associated Proteins: Modifications in Disease , pp. 259-273
    • Fanara, P.1    Brandt, R.2
  • 11
    • 0029977264 scopus 로고    scopus 로고
    • Kinetics of self-assembling microtubules: An 'inverse problem' in biochemistry
    • Flyvbjerg, H., Jobs, E. and Leibler, S. (1996) Kinetics of self-assembling microtubules: an 'inverse problem' in biochemistry. Proc. Natl Acad. Sci. USA, 93, 5975-5979.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5975-5979
    • Flyvbjerg, H.1    Jobs, E.2    Leibler, S.3
  • 12
    • 0028118917 scopus 로고
    • Microtubule organization and dynamics dependent on microtubule-associated proteins
    • Hirokawa, N. (1994) Microtubule organization and dynamics dependent on microtubule-associated proteins. Curr. Opin. Cell Biol., 6, 74-81.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 74-81
    • Hirokawa, N.1
  • 13
    • 0030968633 scopus 로고    scopus 로고
    • The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation
    • Horwitz, S.B., Shen, H.-J., He, L., Dittmar, P., Neef, R., Chen, J. and Schubart, U.K. (1997) The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation. J. Biol. Chem., 272, 8129-8132.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8129-8132
    • Horwitz, S.B.1    Shen, H.-J.2    He, L.3    Dittmar, P.4    Neef, R.5    Chen, J.6    Schubart, U.K.7
  • 14
    • 0028879976 scopus 로고
    • Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins
    • Houthaeve, T., Gausepohl, H., Mann, M. and Ashman, K. (1995) Automation of micro-preparation and enzymatic cleavage of gel electrophoretically separated proteins. FEBS Lett., 376, 91-94.
    • (1995) FEBS Lett. , vol.376 , pp. 91-94
    • Houthaeve, T.1    Gausepohl, H.2    Mann, M.3    Ashman, K.4
  • 15
    • 0031696060 scopus 로고    scopus 로고
    • The role of nucleation in patterning microtubule networks
    • Hyman, A. and Karsenti, E. (1998) The role of nucleation in patterning microtubule networks. J. Cell Sci., 111, 2077-2083.
    • (1998) J. Cell Sci. , vol.111 , pp. 2077-2083
    • Hyman, A.1    Karsenti, E.2
  • 16
    • 0030267241 scopus 로고    scopus 로고
    • The transition of microglia to a ramified phenotype is associated with the formation of stable acetylated and detyrosinated microtubules
    • Ilschner, S. and Brandt, R. (1996) The transition of microglia to a ramified phenotype is associated with the formation of stable acetylated and detyrosinated microtubules. Glia, 18, 129-140.
    • (1996) Glia , vol.18 , pp. 129-140
    • Ilschner, S.1    Brandt, R.2
  • 17
    • 0029808148 scopus 로고    scopus 로고
    • Delayed extraction improves specificity in database searches by matrix-assisted laser desorption/ionization peptide maps
    • Jensen, O.N., Podtelejnikov, A. and Mann, M. (1996) Delayed extraction improves specificity in database searches by matrix-assisted laser desorption/ionization peptide maps. Rapid Commun. Mass Spectrosc., 10, 1371-1378.
    • (1996) Rapid Commun. Mass Spectrosc. , vol.10 , pp. 1371-1378
    • Jensen, O.N.1    Podtelejnikov, A.2    Mann, M.3
  • 18
    • 0017670547 scopus 로고
    • Kinetic analysis of microtubule self-assembly in vitro
    • Johnson, K.A. and Borisy, G.G. (1977) Kinetic analysis of microtubule self-assembly in vitro. J. Mol. Biol., 117, 1-31.
    • (1977) J. Mol. Biol. , vol.117 , pp. 1-31
    • Johnson, K.A.1    Borisy, G.G.2
  • 19
    • 0032006024 scopus 로고    scopus 로고
    • Microtubule dynamics in living cells
    • Joshi, H.C. (1998) Microtubule dynamics in living cells. Curr. Opin. Cell Biol., 10, 35-44.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 35-44
    • Joshi, H.C.1
  • 20
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin: A tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • Jourdain, L., Curmi, P., Sobel, A., Pantaloni, D. and Carlier, M.F. (1997) Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry, 36, 10817-10821.
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.F.5
  • 21
    • 0021265321 scopus 로고
    • The role of centrosome in organizing of microtubule array: Properties of cytoplasts containing or lacking centrosomes
    • Karsenti, E., Kobayashi, S., Mitchison, T. and Kirschner, M.W. (1984) The role of centrosome in organizing of microtubule array: properties of cytoplasts containing or lacking centrosomes. J. Cell Biol., 98, 1763-1776.
    • (1984) J. Cell Biol. , vol.98 , pp. 1763-1776
    • Karsenti, E.1    Kobayashi, S.2    Mitchison, T.3    Kirschner, M.W.4
  • 22
    • 0023837441 scopus 로고
    • Polewards chromosome movement driven by microtubule depolymerization in vitro
    • Koshland, D.E., Mitchison, T.J. and Kirschner, M.W. (1988) Polewards chromosome movement driven by microtubule depolymerization in vitro. Nature, 331, 499-504.
    • (1988) Nature , vol.331 , pp. 499-504
    • Koshland, D.E.1    Mitchison, T.J.2    Kirschner, M.W.3
  • 23
    • 0023785108 scopus 로고
    • Microtubule-assembly inhibitor protein: Its distribution, localization and physicochemical properties
    • Kotani, S., Ikai, A., Kawai, G., Maekawa, S., Yokoyama, S. and Sakai, H. (1988) Microtubule-assembly inhibitor protein: its distribution, localization and physicochemical properties. Eur. J. Biochem., 176, 573-580.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 573-580
    • Kotani, S.1    Ikai, A.2    Kawai, G.3    Maekawa, S.4    Yokoyama, S.5    Sakai, H.6
  • 24
    • 0023403268 scopus 로고
    • Microtubules containing detyrosinated tubulin are less dynamic
    • Kreis, T.E. (1987) Microtubules containing detyrosinated tubulin are less dynamic. EMBO J., 6, 2597-2606.
    • (1987) EMBO J. , vol.6 , pp. 2597-2606
    • Kreis, T.E.1
  • 25
    • 0019805521 scopus 로고
    • Taxol-induced polymerization of purified tubulin. Mechanism of action
    • Kumar, N. (1981) Taxol-induced polymerization of purified tubulin. Mechanism of action. J. Biol. Chem., 256, 10435-10442.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10435-10442
    • Kumar, N.1
  • 26
    • 0026704256 scopus 로고
    • Expression of tau protein in non-neuronal cells: Microtubule binding and stabilization
    • Lee, G. and Rook, S.L. (1992) Expression of tau protein in non-neuronal cells: microtubule binding and stabilization. J. Cell Sci., 102, 227-237.
    • (1992) J. Cell Sci. , vol.102 , pp. 227-237
    • Lee, G.1    Rook, S.L.2
  • 27
    • 0038982381 scopus 로고    scopus 로고
    • Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau
    • Léger, J., Kempf, M., Lee, G. and Brandt, R. (1997) Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau. J. Biol. Chem., 272, 8441-8446.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8441-8446
    • Léger, J.1    Kempf, M.2    Lee, G.3    Brandt, R.4
  • 28
    • 0343710890 scopus 로고
    • Surface-specific iodination of membrane proteins of viruses and eukaryotic cells using 1,3,4,6-tetrachlori-3δ-glycouril
    • Markwell, M.A.K. and Fox, C.F. (1978) Surface-specific iodination of membrane proteins of viruses and eukaryotic cells using 1,3,4,6-tetrachlori-3δ-glycouril. Biochemistry, 112, 278-281.
    • (1978) Biochemistry , vol.112 , pp. 278-281
    • Markwell, M.A.K.1    Fox, C.F.2
  • 29
    • 0030060174 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics during the cell cycle
    • McNally, F.J. (1996) Modulation of microtubule dynamics during the cell cycle. Curr. Opin. Cell Biol., 8, 23-29.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 23-29
    • McNally, F.J.1
  • 30
    • 0027424297 scopus 로고
    • Identification of katanin, an ATPase that severs and disassembles stable microtubules
    • McNally, F.J. and Vale, R.D. (1993) Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell, 75, 419-429.
    • (1993) Cell , vol.75 , pp. 419-429
    • McNally, F.J.1    Vale, R.D.2
  • 31
    • 0023916549 scopus 로고
    • Organization of microtuhules in centrosome-free cytoplasm
    • McNiven, M.A. and Porter, K. (1988) Organization of microtuhules in centrosome-free cytoplasm. J. Cell Biol., 106, 1593-1605.
    • (1988) J. Cell Biol. , vol.106 , pp. 1593-1605
    • McNiven, M.A.1    Porter, K.2
  • 32
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T. and Kirschner, M. (1984a) Dynamic instability of microtubule growth. Nature, 312, 237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 33
    • 0021711717 scopus 로고
    • Microtubule assembly nucleated by isolated centrosomes
    • Mitchison, T. and Kirschner, M. (1984b) Microtubule assembly nucleated by isolated centrosomes. Nature, 312, 232-237.
    • (1984) Nature , vol.312 , pp. 232-237
    • Mitchison, T.1    Kirschner, M.2
  • 34
    • 0028973450 scopus 로고
    • Microtubule nucleation by gamma-tubulin-containing rings in the centrosome
    • Moritz, M., Braunfeld, M.B., Sedat, J.W., Alberts, B. and Agard, D.A. (1995) Microtubule nucleation by gamma-tubulin-containing rings in the centrosome. Nature, 378, 638-640.
    • (1995) Nature , vol.378 , pp. 638-640
    • Moritz, M.1    Braunfeld, M.B.2    Sedat, J.W.3    Alberts, B.4    Agard, D.A.5
  • 35
    • 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
  • 36
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975) High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem., 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 37
    • 0019859353 scopus 로고
    • Taxol binds to polymerized tubulin in vitro
    • Parness, J. and Horwitz, S.B. (1981) Taxol binds to polymerized tubulin in vitro. J. Cell Biol., 91, 479-487.
    • (1981) J. Cell Biol. , vol.91 , pp. 479-487
    • Parness, J.1    Horwitz, S.B.2
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and Von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 40
    • 15844416222 scopus 로고    scopus 로고
    • Normal development of mice lacking metablastin (P19), a phosphoprotein implicated in cell cycle regulation
    • Schubert, U.K., Yu, J., Amat, J.A., Wang, Z., Hoffmann, M.K. and Edelmann, W. (1996) Normal development of mice lacking metablastin (P19), a phosphoprotein implicated in cell cycle regulation. J. Biol. Chem., 271, 14062-14066.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14062-14066
    • Schubert, U.K.1    Yu, J.2    Amat, J.A.3    Wang, Z.4    Hoffmann, M.K.5    Edelmann, W.6
  • 41
    • 0016391111 scopus 로고
    • Preparation of adsorbents for biospecific affinity chromatography I. Attachment of group-containing ligands to insoluble polymers by means of bifunctional oxiranes
    • Sundberg, L. and Porath, J. (1974) Preparation of adsorbents for biospecific affinity chromatography I. Attachment of group-containing ligands to insoluble polymers by means of bifunctional oxiranes. J. Chromatogr., 90, 87-98.
    • (1974) J. Chromatogr. , vol.90 , pp. 87-98
    • Sundberg, L.1    Porath, J.2
  • 42
    • 0026331699 scopus 로고
    • Identification of an inhibitor of microtubule assembly present in juvenile brain which displays a novel mechanism of action involving suppression of self-nucleation
    • Surridge, C.D. and Burns, R.G. (1991) Identification of an inhibitor of microtubule assembly present in juvenile brain which displays a novel mechanism of action involving suppression of self-nucleation. Biochemistry, 30, 10813-10817.
    • (1991) Biochemistry , vol.30 , pp. 10813-10817
    • Surridge, C.D.1    Burns, R.G.2
  • 43
    • 0029858894 scopus 로고    scopus 로고
    • Dynamic properties of nucleated microtubules: GTP utilisation in the subcritical concentration regime
    • Symmons, M.F., Martin, S.R. and Bayley, P.M. (1996) Dynamic properties of nucleated microtubules: GTP utilisation in the subcritical concentration regime. J. Cell Sci., 109, 2755-2766.
    • (1996) J. Cell Sci. , vol.109 , pp. 2755-2766
    • Symmons, M.F.1    Martin, S.R.2    Bayley, P.M.3
  • 45
    • 0030665266 scopus 로고    scopus 로고
    • Cytoplasmic assembly of microtubules in cultured cells
    • Vorobjev, I.A., Svitkina, T.M. and Borisy, G.G. (1997) Cytoplasmic assembly of microtubules in cultured cells. J. Cell Sci., 110, 2635-2645.
    • (1997) J. Cell Sci. , vol.110 , pp. 2635-2645
    • Vorobjev, I.A.1    Svitkina, T.M.2    Borisy, G.G.3
  • 46
    • 0021258393 scopus 로고
    • The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism
    • Voter, W.A. and Erickson, H.P. (1984) The kinetics of microtubule assembly. Evidence for a two-stage nucleation mechanism. J. Biol. Chem., 259, 10430-10438.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10430-10438
    • Voter, W.A.1    Erickson, H.P.2
  • 47
    • 0028879986 scopus 로고
    • Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex
    • Zheng, Y., Wong, M.L., Alberts, B. and Mitchison, T. (1995) Nucleation of microtubule assembly by a gamma-tubulin-containing ring complex. Nature, 378, 578-583.
    • (1995) Nature , vol.378 , pp. 578-583
    • Zheng, Y.1    Wong, M.L.2    Alberts, B.3    Mitchison, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.