메뉴 건너뛰기




Volumn 399, Issue 1, 2010, Pages 1-8

The effect of monastrol on the processive motility of a dimeric kinesin-5 head/kinesin-1 stalk chimera

Author keywords

Kinesin 5; Monastrol inhibition; Motor cooperativity; Processivity; Single molecule fluorescence

Indexed keywords

KINESIN 1; KINESIN 5; MONASTROL;

EID: 77953081400     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.03.009     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 0025326231 scopus 로고
    • Mutation of a gene that encodes a kinesin-like protein blocks nuclear division in A. nidulans
    • Enos A.P., Morris N.R. Mutation of a gene that encodes a kinesin-like protein blocks nuclear division in A. nidulans. Cell 1990, 60:1019-1027.
    • (1990) Cell , vol.60 , pp. 1019-1027
    • Enos, A.P.1    Morris, N.R.2
  • 2
    • 0025869168 scopus 로고
    • Cloning by differential screening of a Xenopus cDNA that encodes a kinesin-related protein
    • Le Guellec R., Paris J., Couturier A., Roghi C., Philippe M. Cloning by differential screening of a Xenopus cDNA that encodes a kinesin-related protein. Mol. Cell. Biol. 1991, 11:3395-3398.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3395-3398
    • Le Guellec, R.1    Paris, J.2    Couturier, A.3    Roghi, C.4    Philippe, M.5
  • 3
    • 0033615357 scopus 로고    scopus 로고
    • Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen
    • Mayer T.U., Kapoor T.M., Haggarty S.J., King R.W., Schreiber S.L., Mitchison T.J. Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 1999, 286:971-974.
    • (1999) Science , vol.286 , pp. 971-974
    • Mayer, T.U.1    Kapoor, T.M.2    Haggarty, S.J.3    King, R.W.4    Schreiber, S.L.5    Mitchison, T.J.6
  • 8
    • 34347375813 scopus 로고    scopus 로고
    • Load-dependent release limits the processive stepping of the tetrameric Eg5 motor
    • Korneev M.J., Lakamper S., Schmidt C.F. Load-dependent release limits the processive stepping of the tetrameric Eg5 motor. Eur. Biophys. J. 2007, 36:675-681.
    • (2007) Eur. Biophys. J. , vol.36 , pp. 675-681
    • Korneev, M.J.1    Lakamper, S.2    Schmidt, C.F.3
  • 9
    • 33744987629 scopus 로고    scopus 로고
    • Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro
    • Valentine M.T., Fordyce P.M., Krzysiak T.C., Gilbert S.P., Block S.M. Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro. Nat. Cell Biol. 2006, 8:470-476.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 470-476
    • Valentine, M.T.1    Fordyce, P.M.2    Krzysiak, T.C.3    Gilbert, S.P.4    Block, S.M.5
  • 10
    • 0030831244 scopus 로고    scopus 로고
    • The bimC family of kinesins: essential bipolar mitotic motors driving centrosome separation
    • Kashina A.S., Rogers G.C., Scholey J.M. The bimC family of kinesins: essential bipolar mitotic motors driving centrosome separation. Biochim. Biophys. Acta 1997, 1357:257-271.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 257-271
    • Kashina, A.S.1    Rogers, G.C.2    Scholey, J.M.3
  • 12
    • 0031576329 scopus 로고    scopus 로고
    • Kinetic evidence for low chemical processivity in ncd and Eg5
    • Crevel I.M., Lockhart A., Cross R.A. Kinetic evidence for low chemical processivity in ncd and Eg5. J. Mol. Biol. 1997, 273:160-170.
    • (1997) J. Mol. Biol. , vol.273 , pp. 160-170
    • Crevel, I.M.1    Lockhart, A.2    Cross, R.A.3
  • 14
    • 57649086182 scopus 로고    scopus 로고
    • The homotetrameric kinesin-5, KLP61F, preferentially cross-links microtubules into antiparallel orientations
    • van den Wildenberg S., Tao L., Kapitein L.C., Schmidt C.F.., Scholey J.M., Peterman E.J. The homotetrameric kinesin-5, KLP61F, preferentially cross-links microtubules into antiparallel orientations. Curr. Biol. 2008, 18:1860-1864.
    • (2008) Curr. Biol. , vol.18 , pp. 1860-1864
    • van den Wildenberg, S.1    Tao, L.2    Kapitein, L.C.3    Schmidt, C.F..4    Scholey, J.M.5    Peterman, E.J.6
  • 15
    • 0036752261 scopus 로고    scopus 로고
    • Evidence that monastrol is an allosteric inhibitor of the mitotic kinesin Eg5
    • Maliga Z., Kapoor T.M., Mitchison T.J. Evidence that monastrol is an allosteric inhibitor of the mitotic kinesin Eg5. Chem. Biol. 2002, 9:989-996.
    • (2002) Chem. Biol. , vol.9 , pp. 989-996
    • Maliga, Z.1    Kapoor, T.M.2    Mitchison, T.J.3
  • 17
    • 64049086564 scopus 로고    scopus 로고
    • 9-Angstrom structure of a microtubule-bound mitotic motor
    • Bodey A.J., Kikkawa M., Moores C.A. 9-Angstrom structure of a microtubule-bound mitotic motor. J. Mol. Biol. 2009, 388:218-224.
    • (2009) J. Mol. Biol. , vol.388 , pp. 218-224
    • Bodey, A.J.1    Kikkawa, M.2    Moores, C.A.3
  • 18
    • 2642572753 scopus 로고    scopus 로고
    • Monastrol stabilises an attached low-friction mode of Eg5
    • Crevel I.M., Alonso M.C., Cross R.A. Monastrol stabilises an attached low-friction mode of Eg5. Curr. Biol. 2004, 14:R411-R412.
    • (2004) Curr. Biol. , vol.14
    • Crevel, I.M.1    Alonso, M.C.2    Cross, R.A.3
  • 21
    • 0037183926 scopus 로고    scopus 로고
    • Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization
    • Tomishige M., Klopfenstein D.R., Vale R.D. Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization. Science 2002, 297:2263-2267.
    • (2002) Science , vol.297 , pp. 2263-2267
    • Tomishige, M.1    Klopfenstein, D.R.2    Vale, R.D.3
  • 22
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: kinesin superfamily protein KIF1A
    • Okada Y., Hirokawa N. A processive single-headed motor: kinesin superfamily protein KIF1A. Science 1999, 283:1152-1157.
    • (1999) Science , vol.283 , pp. 1152-1157
    • Okada, Y.1    Hirokawa, N.2
  • 23
    • 49349085404 scopus 로고    scopus 로고
    • The role of kinesin neck linker and neck in velocity regulation
    • Kalchishkova N., Bohm K.J. The role of kinesin neck linker and neck in velocity regulation. J. Mol. Biol. 2008, 382:127-135.
    • (2008) J. Mol. Biol. , vol.382 , pp. 127-135
    • Kalchishkova, N.1    Bohm, K.J.2
  • 24
    • 33748749372 scopus 로고    scopus 로고
    • Homotetrameric form of Cin8p, a Saccharomyces cerevisiae kinesin-5 motor, is essential for its in vivo function
    • Hildebrandt E.R., Gheber L., Kingsbury T., Hoyt M.A. Homotetrameric form of Cin8p, a Saccharomyces cerevisiae kinesin-5 motor, is essential for its in vivo function. J. Biol. Chem. 2006, 281:26004-26013.
    • (2006) J. Biol. Chem. , vol.281 , pp. 26004-26013
    • Hildebrandt, E.R.1    Gheber, L.2    Kingsbury, T.3    Hoyt, M.A.4
  • 25
    • 0033193864 scopus 로고    scopus 로고
    • Kinesin's tail domain is an inhibitory regulator of the motor domain
    • Coy D.L., Hancock W.O., Wagenbach M., Howard J. Kinesin's tail domain is an inhibitory regulator of the motor domain. Nat. Cell Biol. 1999, 1:288-292.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 288-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 26
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • Howard J., Hudspeth A.J., Vale R.D. Movement of microtubules by single kinesin molecules. Nature 1989, 342:154-158.
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 27
    • 27744552948 scopus 로고    scopus 로고
    • The E-hook of tubulin interacts with kinesin's head to increase processivity and speed
    • Lakamaper S., Meyhofer E. The E-hook of tubulin interacts with kinesin's head to increase processivity and speed. Biophys J. 2005, 89:3223-3234.
    • (2005) Biophys J. , vol.89 , pp. 3223-3234
    • Lakamaper, S.1    Meyhofer, E.2
  • 28
    • 0033536183 scopus 로고    scopus 로고
    • Single kinesin molecules studied with a molecular force clamp
    • Visscher K., Schnitzer M.J., Block S.M. Single kinesin molecules studied with a molecular force clamp. Nature 1999, 400:184-189.
    • (1999) Nature , vol.400 , pp. 184-189
    • Visscher, K.1    Schnitzer, M.J.2    Block, S.M.3
  • 29
    • 61449240125 scopus 로고    scopus 로고
    • The processivity of kinesin-2 motors suggests diminished front-head gating
    • Muthukrishnan G., Zhang Y., Shastry S., Hancock W.O. The processivity of kinesin-2 motors suggests diminished front-head gating. Curr. Biol. 2009, 19:442-447.
    • (2009) Curr. Biol. , vol.19 , pp. 442-447
    • Muthukrishnan, G.1    Zhang, Y.2    Shastry, S.3    Hancock, W.O.4
  • 30
    • 0142040356 scopus 로고    scopus 로고
    • Modulation of kinesin half-site ADP release and kinetic processivity by a spacer between the head groups
    • Hackney D.D., Stock M.F., Moore J., Patterson R.A. Modulation of kinesin half-site ADP release and kinetic processivity by a spacer between the head groups. Biochemistry 2003, 42:12011-12018.
    • (2003) Biochemistry , vol.42 , pp. 12011-12018
    • Hackney, D.D.1    Stock, M.F.2    Moore, J.3    Patterson, R.A.4
  • 31
    • 70350011897 scopus 로고    scopus 로고
    • Force and premature binding of ADP can regulate the processivity of individual Eg5 dimers
    • Valentine M.T., Block S.M. Force and premature binding of ADP can regulate the processivity of individual Eg5 dimers. Biophys. J. 2009, 97:1671-1677.
    • (2009) Biophys. J. , vol.97 , pp. 1671-1677
    • Valentine, M.T.1    Block, S.M.2
  • 32
    • 0032559824 scopus 로고    scopus 로고
    • Role of the kinesin neck region in processive microtubule-based motility
    • Romberg L., Pierce D.W., Vale R.D. Role of the kinesin neck region in processive microtubule-based motility. J. Cell Biol. 1998, 140:1407-1416.
    • (1998) J. Cell Biol. , vol.140 , pp. 1407-1416
    • Romberg, L.1    Pierce, D.W.2    Vale, R.D.3
  • 33
    • 0034722373 scopus 로고    scopus 로고
    • Engineering the processive run length of the kinesin motor
    • Thorn K.S., Ubersax J.A., Vale R.D. Engineering the processive run length of the kinesin motor. J. Cell Biol. 2000, 151:1093-1100.
    • (2000) J. Cell Biol. , vol.151 , pp. 1093-1100
    • Thorn, K.S.1    Ubersax, J.A.2    Vale, R.D.3
  • 35
    • 10044264293 scopus 로고    scopus 로고
    • Mechanism of inhibition of human KSP by monastrol: insights from kinetic analysis and the effect of ionic strength on KSP inhibition
    • Luo L., Carson J.D., Dhanak D., Jackson J.R., Huang P.S., Lee Y., et al. Mechanism of inhibition of human KSP by monastrol: insights from kinetic analysis and the effect of ionic strength on KSP inhibition. Biochemistry 2004, 43:15258-15266.
    • (2004) Biochemistry , vol.43 , pp. 15258-15266
    • Luo, L.1    Carson, J.D.2    Dhanak, D.3    Jackson, J.R.4    Huang, P.S.5    Lee, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.