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Volumn 158, Issue 2, 2007, Pages 137-147

Structure and thermodynamics of the tubulin-stathmin interaction

Author keywords

Intrinsically disordered protein; Microtubule; Protein protein interaction; Stathmin; Tubulin binding protein

Indexed keywords

STATHMIN; TUBULIN;

EID: 34248225770     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.07.018     Document Type: Review
Times cited : (78)

References (51)
  • 1
    • 0034633944 scopus 로고    scopus 로고
    • Stathmin slows down guanosine diphosphate dissociation from tubulin in a phosphorylation-controlled fashion
    • Amayed P., Carlier M.F., and Pantaloni D. Stathmin slows down guanosine diphosphate dissociation from tubulin in a phosphorylation-controlled fashion. Biochemistry 39 (2000) 12295-12302
    • (2000) Biochemistry , vol.39 , pp. 12295-12302
    • Amayed, P.1    Carlier, M.F.2    Pantaloni, D.3
  • 2
    • 0037151124 scopus 로고    scopus 로고
    • The effect of stathmin phosphorylation on microtubule assembly depends on tubulin critical concentration
    • Amayed P., Pantaloni D., and Carlier M.F. The effect of stathmin phosphorylation on microtubule assembly depends on tubulin critical concentration. J. Biol. Chem. 277 (2002) 22718-22724
    • (2002) J. Biol. Chem. , vol.277 , pp. 22718-22724
    • Amayed, P.1    Pantaloni, D.2    Carlier, M.F.3
  • 3
    • 0034237676 scopus 로고    scopus 로고
    • Spindle assembly and the art of regulating microtubule dynamics by MAPs and stathmin/Op18
    • Andersen S.S. Spindle assembly and the art of regulating microtubule dynamics by MAPs and stathmin/Op18. Trends Cell Biol. 10 (2000) 261-267
    • (2000) Trends Cell Biol. , vol.10 , pp. 261-267
    • Andersen, S.S.1
  • 6
    • 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. Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 84 (1996) 623-631
    • (1996) Cell , vol.84 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 7
    • 0035795412 scopus 로고    scopus 로고
    • Regulation of Op18 during spindle assembly in Xenopus egg extracts
    • Budde P.P., Kumagai A., Dunphy W.G., and Heald R. Regulation of Op18 during spindle assembly in Xenopus egg extracts. J. Cell Biol. 153 (2001) 149-158
    • (2001) J. Cell Biol. , vol.153 , pp. 149-158
    • Budde, P.P.1    Kumagai, A.2    Dunphy, W.G.3    Heald, R.4
  • 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 (2002) 18-24
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 18-24
    • Cassimeris, L.1
  • 13
    • 0030781157 scopus 로고    scopus 로고
    • Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin
    • Di P.G., Antonsson B., Kassel D., Riederer B.M., and Grenningloh G. Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin. FEBS Lett. 416 (1997) 149-152
    • (1997) FEBS Lett. , vol.416 , pp. 149-152
    • Di, P.G.1    Antonsson, B.2    Kassel, D.3    Riederer, B.M.4    Grenningloh, G.5
  • 15
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6 (2005) 197-208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 19
    • 33744915563 scopus 로고    scopus 로고
    • Control of intrinsically disordered stathmin by multisite phosphorylation
    • Honnappa S., Jahnke W., Seelig J., and Steinmetz M.O. Control of intrinsically disordered stathmin by multisite phosphorylation. J. Biol. Chem. (2006)
    • (2006) J. Biol. Chem.
    • Honnappa, S.1    Jahnke, W.2    Seelig, J.3    Steinmetz, M.O.4
  • 20
    • 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. The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation. J. Biol. Chem. 272 (1997) 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
  • 21
    • 0032923913 scopus 로고    scopus 로고
    • Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin
    • Howell B., Larsson N., Gullberg M., and Cassimeris L. Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin. Mol. Biol. Cell 10 (1999) 105-118
    • (1999) Mol. Biol. Cell , vol.10 , pp. 105-118
    • Howell, B.1    Larsson, N.2    Gullberg, M.3    Cassimeris, L.4
  • 23
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov I., and Bosshard H.R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recognit. 12 (1999) 3-18
    • (1999) J. Mol. Recognit. , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 24
    • 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. Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry 36 (1997) 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
  • 25
    • 0038170238 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy analysis of the dynamics of tubulin interaction with RB3, a stathmin family protein
    • Krouglova T., Amayed P., Engelborghs Y., and Carlier M.F. Fluorescence correlation spectroscopy analysis of the dynamics of tubulin interaction with RB3, a stathmin family protein. FEBS Lett. 546 (2003) 365-368
    • (2003) FEBS Lett. , vol.546 , pp. 365-368
    • Krouglova, T.1    Amayed, P.2    Engelborghs, Y.3    Carlier, M.F.4
  • 26
    • 0035933896 scopus 로고    scopus 로고
    • Differential effect of two stathmin/Op18 phosphorylation mutants on Xenopus embryo development
    • Kuntziger T., Gavet O., Sobel A., and Bornens M. Differential effect of two stathmin/Op18 phosphorylation mutants on Xenopus embryo development. J. Biol. Chem. 276 (2001) 22979-22984
    • (2001) J. Biol. Chem. , vol.276 , pp. 22979-22984
    • Kuntziger, T.1    Gavet, O.2    Sobel, A.3    Bornens, M.4
  • 27
    • 0030750560 scopus 로고    scopus 로고
    • Control of microtubule dynamics by oncoprotein 18: dissection of the regulatory role of multisite phosphorylation during mitosis
    • Larsson N., Marklund U., Gradin H.M., Brattsand G., and Gullberg M. Control of microtubule dynamics by oncoprotein 18: dissection of the regulatory role of multisite phosphorylation during mitosis. Mol. Cell. Biol. 17 (1997) 5530-5539
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5530-5539
    • Larsson, N.1    Marklund, U.2    Gradin, H.M.3    Brattsand, G.4    Gullberg, M.5
  • 28
    • 0033588976 scopus 로고    scopus 로고
    • Op18/stathmin mediates multiple region-specific tubulin and microtubule-regulating activities
    • Larsson N., Segerman B., Howell B., Fridell K., Cassimeris L., and Gullberg M. Op18/stathmin mediates multiple region-specific tubulin and microtubule-regulating activities. J. Cell Biol. 146 (1999) 1289-1302
    • (1999) J. Cell Biol. , vol.146 , pp. 1289-1302
    • Larsson, N.1    Segerman, B.2    Howell, B.3    Fridell, K.4    Cassimeris, L.5    Gullberg, M.6
  • 29
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt S., and Freire E. Direct measurement of protein binding energetics by isothermal titration calorimetry. Curr. Opin. Struct. Biol. 11 (2001) 560-566
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 30
    • 0032318864 scopus 로고    scopus 로고
    • Structure-based prediction of binding affinities and molecular design of peptide ligands
    • Luque I., and Freire E. Structure-based prediction of binding affinities and molecular design of peptide ligands. Methods Enzymol. 295 (1998) 100-127
    • (1998) Methods Enzymol. , vol.295 , pp. 100-127
    • Luque, I.1    Freire, E.2
  • 31
    • 33644862731 scopus 로고    scopus 로고
    • Stathmin strongly increases the minus end catastrophe frequency and induces rapid treadmilling of bovine brain microtubules at steady state in vitro
    • Manna T., Thrower D., Miller H.P., Curmi P., and Wilson L. Stathmin strongly increases the minus end catastrophe frequency and induces rapid treadmilling of bovine brain microtubules at steady state in vitro. J. Biol. Chem. 281 (2006) 2071-2078
    • (2006) J. Biol. Chem. , vol.281 , pp. 2071-2078
    • Manna, T.1    Thrower, D.2    Miller, H.P.3    Curmi, P.4    Wilson, L.5
  • 32
    • 0025290193 scopus 로고
    • A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations
    • Maucuer A., Doye V., and Sobel A. A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations. FEBS Lett. 264 (1990) 275-278
    • (1990) FEBS Lett. , vol.264 , pp. 275-278
    • Maucuer, A.1    Doye, V.2    Sobel, A.3
  • 33
    • 0035903221 scopus 로고    scopus 로고
    • Stathmin inhibition enhances okadaic acid-induced mitotic arrest: a potential role for stathmin in mitotic exit
    • Mistry S.J., and Atweh G.F. Stathmin inhibition enhances okadaic acid-induced mitotic arrest: a potential role for stathmin in mitotic exit. J. Biol. Chem. 276 (2001) 31209-31215
    • (2001) J. Biol. Chem. , vol.276 , pp. 31209-31215
    • Mistry, S.J.1    Atweh, G.F.2
  • 34
    • 0035326345 scopus 로고    scopus 로고
    • Isotope-tagged cross-linking reagents. A new tool in mass spectrometric protein interaction analysis
    • Muller D.R., Schindler P., Towbin H., Wirth U., Voshol H., Hoving S., and Steinmetz M.O. Isotope-tagged cross-linking reagents. A new tool in mass spectrometric protein interaction analysis. Anal. Chem. 73 (2001) 1927-1934
    • (2001) Anal. Chem. , vol.73 , pp. 1927-1934
    • Muller, D.R.1    Schindler, P.2    Towbin, H.3    Wirth, U.4    Voshol, H.5    Hoving, S.6    Steinmetz, M.O.7
  • 35
    • 1642322097 scopus 로고    scopus 로고
    • Stathmin-tubulin interaction gradients in motile and mitotic cells
    • Niethammer P., Bastiaens P., and Karsenti E. Stathmin-tubulin interaction gradients in motile and mitotic cells. Science 303 (2004) 1862-1866
    • (2004) Science , vol.303 , pp. 1862-1866
    • Niethammer, P.1    Bastiaens, P.2    Karsenti, E.3
  • 37
    • 0036179285 scopus 로고    scopus 로고
    • Drosophila stathmin: a microtubule-destabilizing factor involved in nervous system formation
    • Ozon S., Guichet A., Gavet O., Roth S., and Sobel A. Drosophila stathmin: a microtubule-destabilizing factor involved in nervous system formation. Mol. Biol. Cell 13 (2002) 698-710
    • (2002) Mol. Biol. Cell , vol.13 , pp. 698-710
    • Ozon, S.1    Guichet, A.2    Gavet, O.3    Roth, S.4    Sobel, A.5
  • 38
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
    • Ravelli R.B., Gigant B., Curmi P.A., Jourdain I., Lachkar S., Sobel A., and Knossow M. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature 428 (2004) 198-202
    • (2004) Nature , vol.428 , pp. 198-202
    • Ravelli, R.B.1    Gigant, B.2    Curmi, P.A.3    Jourdain, I.4    Lachkar, S.5    Sobel, A.6    Knossow, M.7
  • 39
    • 0034629506 scopus 로고    scopus 로고
    • Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry
    • Redeker V., Lachkar S., Siavoshian S., Charbaut E., Rossier J., Sobel A., and Curmi P.A. Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry. J. Biol. Chem. 275 (2000) 6841-6849
    • (2000) J. Biol. Chem. , vol.275 , pp. 6841-6849
    • Redeker, V.1    Lachkar, S.2    Siavoshian, S.3    Charbaut, E.4    Rossier, J.5    Sobel, A.6    Curmi, P.A.7
  • 41
    • 16544382801 scopus 로고    scopus 로고
    • The role of stathmin in the regulation of the cell cycle
    • Rubin C.I., and Atweh G.F. The role of stathmin in the regulation of the cell cycle. J. Cell. Biochem. 93 (2004) 242-250
    • (2004) J. Cell. Biochem. , vol.93 , pp. 242-250
    • Rubin, C.I.1    Atweh, G.F.2
  • 42
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig J. Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta 1666 (2004) 40-50
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 44
    • 0025745372 scopus 로고
    • Stathmin: a relay phosphoprotein for multiple signal transduction?
    • Sobel A. Stathmin: a relay phosphoprotein for multiple signal transduction?. Trends Biochem. Sci. 16 (1991) 301-305
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 301-305
    • Sobel, A.1
  • 47
    • 0032906903 scopus 로고    scopus 로고
    • Direct effects of phosphorylation on the preferred backbone conformation of peptides: a nuclear magnetic resonance study
    • Tholey A., Lindemann A., Kinzel V., and Reed J. Direct effects of phosphorylation on the preferred backbone conformation of peptides: a nuclear magnetic resonance study. Biophys. J. 76 (1999) 76-87
    • (1999) Biophys. J. , vol.76 , pp. 76-87
    • Tholey, A.1    Lindemann, A.2    Kinzel, V.3    Reed, J.4
  • 48
    • 0030769624 scopus 로고    scopus 로고
    • Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis
    • Tournebize R., Andersen S.S., Verde F., Doree M., Karsenti E., and Hyman A.A. Distinct roles of PP1 and PP2A-like phosphatases in control of microtubule dynamics during mitosis. EMBO J. 16 (1997) 5537-5549
    • (1997) EMBO J. , vol.16 , pp. 5537-5549
    • Tournebize, R.1    Andersen, S.S.2    Verde, F.3    Doree, M.4    Karsenti, E.5    Hyman, A.A.6
  • 49
    • 0033965785 scopus 로고    scopus 로고
    • Microtubule dynamics and tubulin interacting proteins
    • Walczak C.E. Microtubule dynamics and tubulin interacting proteins. Curr. Opin. Cell Biol. 12 (2000) 52-56
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 52-56
    • Walczak, C.E.1
  • 50
    • 0034677220 scopus 로고    scopus 로고
    • Model for stathmin/OP18 binding to tubulin
    • Wallon G., Rappsilber J., Mann M., and Serrano L. Model for stathmin/OP18 binding to tubulin. EMBO J. 19 (2000) 213-222
    • (2000) EMBO J. , vol.19 , pp. 213-222
    • Wallon, G.1    Rappsilber, J.2    Mann, M.3    Serrano, L.4
  • 51
    • 1242271991 scopus 로고    scopus 로고
    • Regulation of microtubule destabilizing activity of Op18/stathmin downstream of Rac1
    • Wittmann T., Bokoch G.M., and Waterman-Storer C.M. Regulation of microtubule destabilizing activity of Op18/stathmin downstream of Rac1. J. Biol. Chem. 279 (2004) 6196-6203
    • (2004) J. Biol. Chem. , vol.279 , pp. 6196-6203
    • Wittmann, T.1    Bokoch, G.M.2    Waterman-Storer, C.M.3


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