메뉴 건너뛰기




Volumn 110, Issue 51, 2013, Pages 20449-20454

Mechanism for the catastrophe-promoting activity of the microtubule destabilizer Op18/stathmin

Author keywords

Computer simulation; GMPCPP; T2S complex; Zn sheets

Indexed keywords

DOLASTATIN 10; MEMBRANE PROTEIN; OP18 PROTEIN; POLYMER; STATHMIN; TUBULIN; UNCLASSIFIED DRUG;

EID: 84890845323     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1309958110     Document Type: Article
Times cited : (64)

References (30)
  • 1
    • 33846962838 scopus 로고    scopus 로고
    • A novel cancer therapy approach targeting microtubule function
    • Murphy ME, Cassimeris L (2006) A novel cancer therapy approach targeting microtubule function. Cancer Biol Ther 5(12):1721-1723.
    • (2006) Cancer Biol Ther , vol.5 , Issue.12 , pp. 1721-1723
    • Murphy, M.E.1    Cassimeris, L.2
  • 3
    • 34248225770 scopus 로고    scopus 로고
    • Structure and thermodynamics of the tubulin-Stathmin interaction
    • Steinmetz MO (2007) Structure and thermodynamics of the tubulin-Stathmin interaction. J Struct Biol 158(2):137-147.
    • (2007) J Struct Biol , vol.158 , Issue.2 , pp. 137-147
    • Steinmetz, M.O.1
  • 4
    • 0036468982 scopus 로고    scopus 로고
    • The oncoprotein 18/stathmin family of microtubule destabilizers
    • Cassimeris L (2002) The oncoprotein 18/stathmin family of microtubule destabilizers. Curr Opin Cell Biol 14(1):18-24.
    • (2002) Curr Opin Cell Biol , vol.14 , Issue.1 , pp. 18-24
    • Cassimeris, L.1
  • 5
    • 0030048731 scopus 로고    scopus 로고
    • Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
    • Belmont LD, Mitchison TJ (1996) Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules. Cell 84(4):623-631.
    • (1996) Cell , vol.84 , Issue.4 , pp. 623-631
    • Belmont, L.D.1    Mitchison, T.J.2
  • 6
    • 0032923913 scopus 로고    scopus 로고
    • Dissociation of the tubulinsequestering and microtubule catastrophe-Promoting activities of oncoprotein 18/stathmin
    • Howell B, Larsson N, Gullberg M, Cassimeris L (1999) Dissociation of the tubulinsequestering and microtubule catastrophe-Promoting activities of oncoprotein 18/stathmin. Mol Biol Cell 10(1):105-118.
    • (1999) Mol Biol Cell , vol.10 , Issue.1 , pp. 105-118
    • Howell, B.1    Larsson, N.2    Gullberg, M.3    Cassimeris, L.4
  • 7
    • 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 HP, Curmi P, Wilson L (2006) 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(4):2071-2078.
    • (2006) J Biol Chem , vol.281 , Issue.4 , pp. 2071-2078
    • Manna, T.1    Thrower, D.2    Miller, H.P.3    Curmi, P.4    Wilson, L.5
  • 8
    • 0037151124 scopus 로고    scopus 로고
    • The effect of stathmin phosphorylation on microtubule assembly depends on tubulin critical concentration
    • Amayed P, Pantaloni D, Carlier MF (2002) The effect of stathmin phosphorylation on microtubule assembly depends on tubulin critical concentration. J Biol Chem 277(25): 22718-22724.
    • (2002) J Biol Chem , vol.277 , Issue.25 , pp. 22718-22724
    • Amayed, P.1    Pantaloni, D.2    Carlier, M.F.3
  • 9
    • 33644853818 scopus 로고    scopus 로고
    • Structural intermediates in microtubule assembly and disassembly: How and why
    • Nogales E, Wang HW (2006) Structural intermediates in microtubule assembly and disassembly: How and why Curr Opin Cell Biol 18(2):179-184.
    • (2006) Curr Opin Cell Biol , vol.18 , Issue.2 , pp. 179-184
    • Nogales, E.1    Wang, H.W.2
  • 10
    • 84863162345 scopus 로고    scopus 로고
    • The mechanisms of microtubule catastrophe and rescue: Implications from analysis of a dimer-Scale computational model
    • Margolin G, et al. (2012) The mechanisms of microtubule catastrophe and rescue: Implications from analysis of a dimer-Scale computational model. Mol Biol Cell 23(4): 642-656.
    • (2012) Mol Biol Cell , vol.23 , Issue.4 , pp. 642-656
    • Margolin, G.1
  • 11
    • 65449174344 scopus 로고    scopus 로고
    • Minimal plus-End tracking unit of the cytoplasmic linker protein CLIP-170
    • Gupta KK, et al. (2009) Minimal plus-End tracking unit of the cytoplasmic linker protein CLIP-170. J Biol Chem 284(11):6735-6742.
    • (2009) J Biol Chem , vol.284 , Issue.11 , pp. 6735-6742
    • Gupta, K.K.1
  • 12
    • 0029347192 scopus 로고
    • How does taxol stabilize microtubules
    • Arnal I, Wade RH (1995) How does taxol stabilize microtubules Curr Biol 5(8): 900-908.
    • (1995) Curr Biol , vol.5 , Issue.8 , pp. 900-908
    • Arnal, I.1    Wade, R.H.2
  • 13
    • 35348866321 scopus 로고    scopus 로고
    • Straight GDP-Tubulin protofilaments form in the presence of taxol
    • Elie-Caille C, et al. (2007) Straight GDP-Tubulin protofilaments form in the presence of taxol. Curr Biol 17(20):1765-1770.
    • (2007) Curr Biol , vol.17 , Issue.20 , pp. 1765-1770
    • Elie-Caille, C.1
  • 14
    • 0032584067 scopus 로고    scopus 로고
    • Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha,beta)methylenediphosphonate
    • Müller-Reichert T, Chrétien D, Severin F, Hyman AA (1998) Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha,beta) methylenediphosphonate. Proc Natl Acad Sci USA 95(7):3661-3666.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.7 , pp. 3661-3666
    • Müller-Reichert, T.1    Chrétien, D.2    Severin, F.3    Hyman, A.A.4
  • 15
    • 40849139089 scopus 로고    scopus 로고
    • Visualisation of a kinesin-13 motor on microtubule end mimics
    • Moores CA, Milligan RA (2008) Visualisation of a kinesin-13 motor on microtubule end mimics. J Mol Biol 377(3):647-654.
    • (2008) J Mol Biol , vol.377 , Issue.3 , pp. 647-654
    • Moores, C.A.1    Milligan, R.A.2
  • 16
    • 65249163575 scopus 로고    scopus 로고
    • A new model for binding of kinesin 13 to curved microtubule protofilaments
    • Mulder AM, et al. (2009) A new model for binding of kinesin 13 to curved microtubule protofilaments. J Cell Biol 185(1):51-57.
    • (2009) J Cell Biol , vol.185 , Issue.1 , pp. 51-57
    • Mulder, A.M.1
  • 18
    • 55549135317 scopus 로고    scopus 로고
    • Structural insight into the inhibition of tubulin by vinca domain peptide ligands
    • Cormier A, Marchand M, Ravelli RB, Knossow M, Gigant B (2008) Structural insight into the inhibition of tubulin by vinca domain peptide ligands. EMBO Rep 9(11):1101-1106.
    • (2008) EMBO Rep , vol.9 , Issue.11 , pp. 1101-1106
    • Cormier, A.1    Marchand, M.2    Ravelli, R.B.3    Knossow, M.4    Gigant, B.5
  • 19
    • 0026768118 scopus 로고
    • Tubulin protofilaments and kinesin-Dependent motility
    • Kamimura S, Mandelkow E (1992) Tubulin protofilaments and kinesin-Dependent motility. J Cell Biol 118(4):865-875.
    • (1992) J Cell Biol , vol.118 , Issue.4 , pp. 865-875
    • Kamimura, S.1    Mandelkow, E.2
  • 20
    • 0037731545 scopus 로고    scopus 로고
    • Different protofilament-Dependence of the microtubule binding between MAP2 and MAP4
    • Kawachi A, et al. (2003) Different protofilament-Dependence of the microtubule binding between MAP2 and MAP4. Biochem Biophys Res Commun 305(1):72-78.
    • (2003) Biochem Biophys Res Commun , vol.305 , Issue.1 , pp. 72-78
    • Kawachi, A.1
  • 21
    • 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, Carlier MF (2003) Fluorescence correlation spectroscopy analysis of the dynamics of tubulin interaction with RB3, a stathmin family protein. FEBS Lett 546(2-3):365-368.
    • (2003) FEBS Lett , vol.546 , Issue.2-3 , pp. 365-368
    • Krouglova, T.1    Amayed, P.2    Engelborghs, Y.3    Carlier, M.F.4
  • 22
    • 38449119832 scopus 로고    scopus 로고
    • Measurements of stathmin-Tubulin interaction in solution
    • Carlier MF (2007) Measurements of stathmin-Tubulin interaction in solution. Methods Mol Med 137:103-110.
    • (2007) Methods Mol Med , vol.137 , pp. 103-110
    • Carlier, M.F.1
  • 23
    • 0034664244 scopus 로고    scopus 로고
    • The 4 A X-Ray structure of a tubulin:stathmin-Like domain complex
    • Gigant B, et al. (2000) The 4 A X-Ray structure of a tubulin:stathmin- Like domain complex. Cell 102(6):809-816.
    • (2000) Cell , vol.102 , Issue.6 , pp. 809-816
    • Gigant, B.1
  • 24
    • 1642401199 scopus 로고    scopus 로고
    • Insight into tubulin regulation from a complex with colchicine and a stathmin-Like domain
    • Ravelli RB, et al. (2004) Insight into tubulin regulation from a complex with colchicine and a stathmin-Like domain. Nature 428(6979):198-202.
    • (2004) Nature , vol.428 , Issue.6979 , pp. 198-202
    • Ravelli, R.B.1
  • 25
    • 84860390007 scopus 로고    scopus 로고
    • The determinants that govern microtubule assembly from the atomic structure of GTP-Tubulin
    • Nawrotek A, Knossow M, Gigant B (2011) The determinants that govern microtubule assembly from the atomic structure of GTP-Tubulin. J Mol Biol 412(1):35-42.
    • (2011) J Mol Biol , vol.412 , Issue.1 , pp. 35-42
    • Nawrotek, A.1    Knossow, M.2    Gigant, B.3
  • 26
    • 77957763787 scopus 로고    scopus 로고
    • Stathmin and interfacial microtubule inhibitors recognize a naturally curved conformation of tubulin dimers
    • Barbier P, et al. (2010) Stathmin and interfacial microtubule inhibitors recognize a naturally curved conformation of tubulin dimers. J Biol Chem 285(41):31672-31681.
    • (2010) J Biol Chem , vol.285 , Issue.41 , pp. 31672-31681
    • Barbier, P.1
  • 27
    • 34548675565 scopus 로고    scopus 로고
    • Insight into the GTPase activity of tubulin from complexes with stathmin-Like domains
    • Wang C, Cormier A, Gigant B, Knossow M (2007) Insight into the GTPase activity of tubulin from complexes with stathmin-Like domains. Biochemistry 46(37):10595-10602.
    • (2007) Biochemistry , vol.46 , Issue.37 , pp. 10595-10602
    • Wang, C.1    Cormier, A.2    Gigant, B.3    Knossow, M.4
  • 28
    • 27644585170 scopus 로고    scopus 로고
    • N-Terminal stathmin-Like peptides bind tubulin and impede microtubule assembly
    • Clément MJ, et al. (2005) N-Terminal stathmin-Like peptides bind tubulin and impede microtubule assembly. Biochemistry 44(44):14616-14625.
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14616-14625
    • Clément, M.J.1
  • 29
    • 33845720353 scopus 로고    scopus 로고
    • Insights into cytoskeletal behavior from computational modeling of dynamic microtubules in a cell-Like environment
    • Gregoretti IV, Margolin G, Alber MS, Goodson HV (2006) Insights into cytoskeletal behavior from computational modeling of dynamic microtubules in a cell-Like environment. J Cell Sci 119(Pt 22):4781-4788.
    • (2006) J Cell Sci , vol.119 , Issue.PART 22 , pp. 4781-4788
    • Gregoretti, I.V.1    Margolin, G.2    Alber, M.S.3    Goodson, H.V.4
  • 30
    • 0036711845 scopus 로고    scopus 로고
    • Life cycle of MTs: Persistent growth in the cell interior, asymmetric transition frequencies and effects of the cell boundary
    • Komarova YA, Vorobjev IA, Borisy GG (2002) Life cycle of MTs: Persistent growth in the cell interior, asymmetric transition frequencies and effects of the cell boundary. J Cell Sci 115(Pt 17):3527-3539.
    • (2002) J Cell Sci , vol.115 , Issue.PART 17 , pp. 3527-3539
    • Komarova, Y.A.1    Vorobjev, I.A.2    Borisy, G.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.