메뉴 건너뛰기




Volumn 428, Issue 6979, 2004, Pages 198-202

Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; DIMERS; POLYMERIZATION; PROTEINS; SWITCHES;

EID: 1642401199     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02393     Document Type: Article
Times cited : (1424)

References (30)
  • 1
    • 0029155318 scopus 로고
    • Kinetic stabilization of microtubule dynamics at steady state in vitro by substoichiometric concentrations of tubulin-colchicine complex
    • Panda, D., Daijo, J. E., Jordan, M. A. & Wilson, L. Kinetic stabilization of microtubule dynamics at steady state in vitro by substoichiometric concentrations of tubulin-colchicine complex. Biochemistry 34, 9921-9929 (1995).
    • (1995) Biochemistry , vol.34 , pp. 9921-9929
    • Panda, D.1    Daijo, J.E.2    Jordan, M.A.3    Wilson, L.4
  • 2
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont, L. D. & Mitchison, T. J. Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 84, 623-631 (1996).
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 3
    • 0035844234 scopus 로고    scopus 로고
    • Stathmin family proteins display specific molecular and tubulin binding properties
    • Charbaut, E. et al. Stathmin family proteins display specific molecular and tubulin binding properties. J. Biol. Chem. 276, 16146-16154 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 16146-16154
    • Charbaut, E.1
  • 4
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • Löwe, J., Li, H., Downing, K. H. & Nogales, E. Refined structure of αβ-tubulin at 3.5 Å resolution. J. Mol. Biol. 313, 1045-1057 (2001).
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 5
    • 0014382446 scopus 로고
    • The colchicine-binding protein of mammalian brain and its relation to microtubules
    • Weisenberg, R. C., Borisy, G. G. & Taylor, E. W. The colchicine-binding protein of mammalian brain and its relation to microtubules. Biochemistry 7, 4466-4479 (1968).
    • (1968) Biochemistry , vol.7 , pp. 4466-4479
    • Weisenberg, R.C.1    Borisy, G.G.2    Taylor, E.W.3
  • 6
    • 0026328348 scopus 로고
    • Interactions of colchicine with tubulin
    • Bane Hastie, S. Interactions of colchicine with tubulin. Pharmacol Ther. 51, 377-401 (1991).
    • (1991) Pharmacol Ther. , vol.51 , pp. 377-401
    • Bane Hastie, S.1
  • 7
    • 0034704077 scopus 로고    scopus 로고
    • Mapping the binding site of colchicinoids on β-tubulin
    • Bai, R. et al. Mapping the binding site of colchicinoids on β-tubulin. J. Biol. Chem. 275, 40443-40452 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 40443-40452
    • Bai, R.1
  • 8
    • 0036468982 scopus 로고    scopus 로고
    • The oncoprotein 18/stathmin family of microtubule destabilizers
    • Cassimeris, L. The oncoprotein 18/stathmin family of microtubule destabilizers. Curr. Opin. Cell Biol. 14, 18-24 (2002).
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 18-24
    • Cassimeris, L.1
  • 9
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin is a tubulin sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • Jourdain, L., Curmi, P., Sobel, A., Pantaloni, D. & Carlier, M.-F. Stathmin is a tubulin sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry 36, 10817-10821 (1997).
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.-F.5
  • 10
    • 0030826361 scopus 로고    scopus 로고
    • The stathmin tubulin interaction in vitro
    • Curmi, P. A. et al. The stathmin tubulin interaction in vitro. J. Biol. Chem. 272, 25029-25036 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 25029-25036
    • Curmi, P.A.1
  • 11
    • 0034664244 scopus 로고    scopus 로고
    • The 4 Å X-ray structure of a tubulin:stathmin-like domain complex
    • Gigant, B. et al. The 4 Å X-ray structure of a tubulin:stathmin-like domain complex. Cell 102, 809-816 (2000).
    • (2000) Cell , vol.102 , pp. 809-816
    • Gigant, B.1
  • 12
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling, F. T., Weis, W. I., Flaherty, K. M. & Brunger, A. T. Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science 271, 72-77 (1996).
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brunger, A.T.4
  • 13
    • 0027169646 scopus 로고
    • Stathmin gene family: Phylogenetic conservation and developmental regulation in Xenopus
    • Maucuer, A., Moreau, J., Mechali, M. & Sobel, A. Stathmin gene family: phylogenetic conservation and developmental regulation in Xenopus. J. Biol. Chem. 268, 16420-16429 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 16420-16429
    • Maucuer, A.1    Moreau, J.2    Mechali, M.3    Sobel, A.4
  • 14
    • 0027292675 scopus 로고
    • Multiple phosphorylation of stathmin: Identification of four sites phosphorylated in intact cells and in vitro by cyclic-AMP dependent protein kinase and p34cdc2
    • Beretta, L., Dobransky, T. & Sobel, A. Multiple phosphorylation of stathmin: identification of four sites phosphorylated in intact cells and in vitro by cyclic-AMP dependent protein kinase and p34cdc2. J. Biol. Chem. 268, 20076-20084 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 20076-20084
    • Beretta, L.1    Dobransky, T.2    Sobel, A.3
  • 16
    • 0034651986 scopus 로고    scopus 로고
    • Op18/stathmin caps a kinked protofilament-like tubulin tetramer
    • Steinmetz, M. O. et al. Op18/stathmin caps a kinked protofilament-like tubulin tetramer. EMBO J. 19, 572-580 (2000).
    • (2000) EMBO J. , vol.19 , pp. 572-580
    • Steinmetz, M.O.1
  • 20
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Löwe, J. & Amos, L. A. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391, 203-206 (1998).
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 21
    • 0032584067 scopus 로고    scopus 로고
    • Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (α,β)methylenediphosphonate
    • Müller-Reichert, T., Chrétien, D., Severin, F. & Hyman, A. A. Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (α,β)methylenediphosphonate. Proc. Natl Acad. Sci. USA 95, 3661-3666 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3661-3666
    • Müller-Reichert, T.1    Chrétien, D.2    Severin, F.3    Hyman, A.A.4
  • 22
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 24
    • 0027979404 scopus 로고
    • Effect of colchicine analogues on the dissociation of αβ tubulin into subunits: The locus of colchicine binding
    • Shearwin, K. E. & Timasheff, S. N. Effect of colchicine analogues on the dissociation of αβ tubulin into subunits: the locus of colchicine binding. Biochemistry 33, 894-901 (1994).
    • (1994) Biochemistry , vol.33 , pp. 894-901
    • Shearwin, K.E.1    Timasheff, S.N.2
  • 25
    • 0026503079 scopus 로고
    • Analysis of the colchicine-binding site of β-tubulin
    • Burns, R. G. Analysis of the colchicine-binding site of β-tubulin. FEBS Lett. 297, 205-208 (1992).
    • (1992) FEBS Lett. , vol.297 , pp. 205-208
    • Burns, R.G.1
  • 26
    • 0026558326 scopus 로고
    • Mechanism of inhibition of microtubule polymerization by colchicine: Inhibitory potencies of unliganded colchicine and tubulin-colchicine complexes
    • Skoufias, D. A. & Wilson, L. Mechanism of inhibition of microtubule polymerization by colchicine: inhibitory potencies of unliganded colchicine and tubulin-colchicine complexes. Biochemistry 31, 738-746 (1992).
    • (1992) Biochemistry , vol.31 , pp. 738-746
    • Skoufias, D.A.1    Wilson, L.2
  • 27
    • 0038521325 scopus 로고
    • Zero-dose extrapolation as part of macromolecular synchrotron data reduction
    • Diederichs, K., McSweeney, S. & Ravelli, R. B. Zero-dose extrapolation as part of macromolecular synchrotron data reduction. Acta Crystallogr. D 59, 903-909 (1992).
    • (1992) Acta Crystallogr. D , vol.59 , pp. 903-909
    • Diederichs, K.1    McSweeney, S.2    Ravelli, R.B.3
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • (eds Carter, C. W. & Sweet, R. M.) (Academic, New York)
    • De La Fortelle, E. & Bricogne, G. in Methods in Enzymology (eds Carter, C. W. & Sweet, R. M.) 472-494 (Academic, New York, 1997).
    • (1997) Methods in Enzymology , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 29
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N. & Murshudov, G. N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D 57, 122-133 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 30
    • 0036008503 scopus 로고    scopus 로고
    • A genetic algorithm for the identification of conformationally invariant regions in protein molecules
    • Schneider, T. R. A genetic algorithm for the identification of conformationally invariant regions in protein molecules. Acta Crystallogr. D 58, 195-208 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 195-208
    • Schneider, T.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.