메뉴 건너뛰기




Volumn 287, Issue 53, 2012, Pages 44654-44666

The structural basis of force generation by the mitotic motor kinesin-5

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC INHIBITOR; ANTI-CANCER THERAPEUTICS; ATP BINDING; BIPOLAR SPINDLES; CONFORMATIONAL CHANGE; CRYO-ELECTRON MICROSCOPY; FORCE GENERATION; MECHANICAL ELEMENTS; MICROTUBULES; MITOTIC MOTOR; MOLECULAR MECHANISM; MOTOR DOMAIN; N-TERMINALS; NORMAL FUNCTION; NUCLEOTIDE BINDING; SEQUENCE VARIATIONS; STRUCTURAL BASIS; SUBNANOMETER RESOLUTION;

EID: 84871744734     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.404228     Document Type: Article
Times cited : (62)

References (63)
  • 2
    • 18344371892 scopus 로고    scopus 로고
    • The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks
    • Kapitein, L. C., Peterman, E. J., Kwok, B. H., Kim, J. H., Kapoor, T. M., and Schmidt, C. F. (2005) The bipolar mitotic kinesin Eg5 moves on both microtubules that it crosslinks. Nature 435, 114-118
    • (2005) Nature , vol.435 , pp. 114-118
    • Kapitein, L.C.1    Peterman, E.J.2    Kwok, B.H.3    Kim, J.H.4    Kapoor, T.M.5    Schmidt, C.F.6
  • 3
    • 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., and Block, S. M. (2006) Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro. Nat. Cell Biol. 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
  • 4
    • 84866494584 scopus 로고    scopus 로고
    • Necklinker length dependence of processive kinesin-5 motility
    • Düselder, A., Thiede, C., Schmidt, C. F., and Lakämper, S. (2012) Necklinker length dependence of processive kinesin-5 motility. J. Mol. Biol. 423, 159-168
    • (2012) J. Mol. Biol. , vol.423 , pp. 159-168
    • Düselder, A.1    Thiede, C.2    Schmidt, C.F.3    Lakämper, S.4
  • 6
    • 82455211990 scopus 로고    scopus 로고
    • A seesaw model for intermolecular gating in the kinesin motor protein
    • Sindelar, C. V. (2011) A seesaw model for intermolecular gating in the kinesin motor protein. Biophys. Rev. 3, 85-100
    • (2011) Biophys. Rev. , vol.3 , pp. 85-100
    • Sindelar, C.V.1
  • 9
    • 37548999364 scopus 로고    scopus 로고
    • Force generation in kinesin hinges on cover-neck bundle formation
    • Hwang, W., Lang, M. J., and Karplus, M. (2008) Force generation in kinesin hinges on cover-neck bundle formation. Structure 16, 62-71
    • (2008) Structure , vol.16 , pp. 62-71
    • Hwang, W.1    Lang, M.J.2    Karplus, M.3
  • 11
    • 0035816597 scopus 로고    scopus 로고
    • Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker
    • Turner, J., Anderson, R., Guo, J., Beraud, C., Fletterick, R., and Sakowicz, R. (2001) Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. J. Biol. Chem. 276, 25496-25502
    • (2001) J. Biol. Chem. , vol.276 , pp. 25496-25502
    • Turner, J.1    Anderson, R.2    Guo, J.3    Beraud, C.4    Fletterick, R.5    Sakowicz, R.6
  • 13
  • 14
    • 77952977790 scopus 로고    scopus 로고
    • The conserved L5 loop establishes the pre-powerstroke conformation of the kinesin-5 motor, eg5
    • Larson, A. G., Naber, N., Cooke, R., Pate, E., and Rice, S. E. (2010) The conserved L5 loop establishes the pre-powerstroke conformation of the kinesin-5 motor, eg5. Biophys. J. 98, 2619-2627
    • (2010) Biophys. J. , vol.98 , pp. 2619-2627
    • Larson, A.G.1    Naber, N.2    Cooke, R.3    Pate, E.4    Rice, S.E.5
  • 18
    • 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., and Mitchison, T. J. (1999) Small molecule inhibitor of mitotic spindle bipolarity identified in a phenotype-based screen. Science 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
  • 19
    • 59449102892 scopus 로고    scopus 로고
    • Targeting the kinesin spindle protein. Basic principles and clinical implications
    • Sarli, V., and Giannis, A. (2008) Targeting the kinesin spindle protein. Basic principles and clinical implications. Clin. Cancer Res. 14, 7583-7587
    • (2008) Clin. Cancer Res. , vol.14 , pp. 7583-7587
    • Sarli, V.1    Giannis, A.2
  • 20
    • 77949318844 scopus 로고    scopus 로고
    • ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism
    • Parke, C. L., Wojcik, E. J., Kim, S., and Worthylake, D. K. (2010) ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism. J. Biol. Chem. 285, 5859-5867
    • (2010) J. Biol. Chem. , vol.285 , pp. 5859-5867
    • Parke, C.L.1    Wojcik, E.J.2    Kim, S.3    Worthylake, D.K.4
  • 21
    • 72449183762 scopus 로고    scopus 로고
    • An allosteric transition trapped in an intermediate state of a new kinesin-inhibitor complex
    • Kaan, H. Y., Ulaganathan, V., Hackney, D. D., and Kozielski, F. (2010) An allosteric transition trapped in an intermediate state of a new kinesin-inhibitor complex. Biochem. J. 425, 55-60
    • (2010) Biochem. J. , vol.425 , pp. 55-60
    • Kaan, H.Y.1    Ulaganathan, V.2    Hackney, D.D.3    Kozielski, F.4
  • 22
    • 79953167875 scopus 로고    scopus 로고
    • Loop 5-directed compounds inhibit chimeric kinesin-5 motors. Implications for conserved allosteric mechanisms
    • Liu, L., Parameswaran, S., Liu, J., Kim, S., and Wojcik, E. J. (2011) Loop 5-directed compounds inhibit chimeric kinesin-5 motors. Implications for conserved allosteric mechanisms. J. Biol. Chem. 286, 6201-6210
    • (2011) J. Biol. Chem. , vol.286 , pp. 6201-6210
    • Liu, L.1    Parameswaran, S.2    Liu, J.3    Kim, S.4    Wojcik, E.J.5
  • 23
    • 0343415156 scopus 로고    scopus 로고
    • The way things move. Looking under the hood of molecular motor proteins
    • Vale, R. D., and Milligan, R. A. (2000) The way things move. Looking under the hood of molecular motor proteins. Science 288, 88-95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 24
    • 0036830220 scopus 로고    scopus 로고
    • Two conformations in the human kinesin power stroke defined by x-ray crystallography and EPR spectroscopy
    • Sindelar, C. V., Budny, M. J., Rice, S., Naber, N., Fletterick, R., and Cooke, R. (2002) Two conformations in the human kinesin power stroke defined by x-ray crystallography and EPR spectroscopy. Nat. Struct. Biol. 9, 844-848
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 844-848
    • Sindelar, C.V.1    Budny, M.J.2    Rice, S.3    Naber, N.4    Fletterick, R.5    Cooke, R.6
  • 25
    • 77749239756 scopus 로고    scopus 로고
    • An atomic-level mechanism for activation of the kinesin molecular motors
    • Sindelar, C. V., and Downing, K. H. (2010) An atomic-level mechanism for activation of the kinesin molecular motors. Proc. Natl. Acad. Sci. U.S.A. 107, 4111-4116
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4111-4116
    • Sindelar, C.V.1    Downing, K.H.2
  • 26
    • 39949083937 scopus 로고    scopus 로고
    • The role of microtubules in processive kinesin movement
    • Kikkawa, M. (2008) The role of microtubules in processive kinesin movement. Trends Cell Biol. 18, 128-135
    • (2008) Trends Cell Biol. , vol.18 , pp. 128-135
    • Kikkawa, M.1
  • 27
    • 0034675854 scopus 로고    scopus 로고
    • Structural comparison of dimeric Eg5, Neurospora kinesin (Nkin) and Ncd head-Nkin neck chimera with conventional kinesin
    • Hirose, K., Henningsen, U., Schliwa, M., Toyoshima, C., Shimizu, T., Alonso, M., Cross, R. A., and Amos, L. A. (2000) Structural comparison of dimeric Eg5, Neurospora kinesin (Nkin) and Ncd head-Nkin neck chimera with conventional kinesin. EMBO J. 19, 5308-5314
    • (2000) EMBO J. , vol.19 , pp. 5308-5314
    • Hirose, K.1    Henningsen, U.2    Schliwa, M.3    Toyoshima, C.4    Shimizu, T.5    Alonso, M.6    Cross, R.A.7    Amos, L.A.8
  • 29
    • 64049086564 scopus 로고    scopus 로고
    • 9-Angstrom structure of a microtubule-bound mitotic motor
    • Bodey, A. J., Kikkawa, M., and Moores, C. A. (2009) 9-Angstrom structure of a microtubule-bound mitotic motor. J. Mol. Biol. 388, 218-224
    • (2009) J. Mol. Biol. , vol.388 , pp. 218-224
    • Bodey, A.J.1    Kikkawa, M.2    Moores, C.A.3
  • 30
    • 33646358250 scopus 로고    scopus 로고
    • Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol
    • Maliga, Z., and Mitchison, T. J. (2006) Small-molecule and mutational analysis of allosteric Eg5 inhibition by monastrol. BMC Chem. Biol. 6, 2
    • (2006) BMC Chem. Biol. , vol.6 , pp. 2
    • Maliga, Z.1    Mitchison, T.J.2
  • 31
    • 27444445780 scopus 로고    scopus 로고
    • Docking and rolling, a model of how the mitotic motor Eg5 works
    • Rosenfeld, S. S., Xing, J., Jefferson, G. M., and King, P. H. (2005) Docking and rolling, a model of how the mitotic motor Eg5 works. J. Biol. Chem. 280, 35684-35695
    • (2005) J. Biol. Chem. , vol.280 , pp. 35684-35695
    • Rosenfeld, S.S.1    Xing, J.2    Jefferson, G.M.3    King, P.H.4
  • 32
    • 77955493466 scopus 로고    scopus 로고
    • Modulation of the kinesin ATPase cycle by neck linker docking and microtubule binding
    • Zhao, Y. C., Kull, F. J., and Cochran, J. C. (2010) Modulation of the kinesin ATPase cycle by neck linker docking and microtubule binding. J. Biol. Chem. 285, 25213-25220
    • (2010) J. Biol. Chem. , vol.285 , pp. 25213-25220
    • Zhao, Y.C.1    Kull, F.J.2    Cochran, J.C.3
  • 34
    • 0032758215 scopus 로고    scopus 로고
    • Undecagold cluster labeling of proteins at reactive cysteine residues
    • Safer, D. (1999) Undecagold cluster labeling of proteins at reactive cysteine residues. J. Struct. Biol. 127, 101-105
    • (1999) J. Struct. Biol. , vol.127 , pp. 101-105
    • Safer, D.1
  • 35
    • 0033377664 scopus 로고    scopus 로고
    • EMAN. Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R., and Chiu, W. (1999) EMAN. Semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 36
    • 34248200882 scopus 로고    scopus 로고
    • The beginning of kinesin's force-generating cycle visualized at 9-Å resolution
    • Sindelar, C. V., and Downing, K. H. (2007) The beginning of kinesin's force-generating cycle visualized at 9-Å resolution. J. Cell Biol. 177, 377-385
    • (2007) J. Cell Biol. , vol.177 , pp. 377-385
    • Sindelar, C.V.1    Downing, K.H.2
  • 37
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB. Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. (1996) SPIDER and WEB. Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 38
    • 33845348200 scopus 로고    scopus 로고
    • FREALIGN. High-resolution refinement of single particle structures
    • Grigorieff, N. (2007) FREALIGN. High-resolution refinement of single particle structures. J. Struct. Biol. 157, 117-125
    • (2007) J. Struct. Biol. , vol.157 , pp. 117-125
    • Grigorieff, N.1
  • 39
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J. A., and Grigorieff, N. (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 40
    • 0023090371 scopus 로고
    • Similarity measures between images
    • van Heel, M. (1987) Similarity measures between images. Ultramicroscopy 21, 95-100
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 41
    • 33845291163 scopus 로고    scopus 로고
    • Ab initio resolution measurement for single particle structures
    • Sousa, D., and Grigorieff, N. (2007) Ab initio resolution measurement for single particle structures. J. Struct. Biol. 157, 201-210
    • (2007) J. Struct. Biol. , vol.157 , pp. 201-210
    • Sousa, D.1    Grigorieff, N.2
  • 44
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of αβ-tubulin at 3.5 Å resolution
    • Löwe, J., Li, H., Downing, K. H., and Nogales, E. (2001) Refined structure of αβ-tubulin at 3.5 Å resolution. J. Mol. Biol. 313, 1045-1057
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 45
    • 38949092920 scopus 로고    scopus 로고
    • Protein structure fitting and refinement guided by cryo-EM density
    • Topf, M., Lasker, K., Webb, B., Wolfson, H., Chiu, W., and Sali, A. (2008) Protein structure fitting and refinement guided by cryo-EM density. Structure 16, 295-307
    • (2008) Structure , vol.16 , pp. 295-307
    • Topf, M.1    Lasker, K.2    Webb, B.3    Wolfson, H.4    Chiu, W.5    Sali, A.6
  • 46
    • 84857033345 scopus 로고    scopus 로고
    • Finding rigid bodies in protein structures. Application to flexible fitting into cryoEM maps
    • Pandurangan, A. P., and Topf, M. (2012) Finding rigid bodies in protein structures. Application to flexible fitting into cryoEM maps. J. Struct. Biol. 177, 520-531
    • (2012) J. Struct. Biol. , vol.177 , pp. 520-531
    • Pandurangan, A.P.1    Topf, M.2
  • 47
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer
    • Dale, R. E., Eisinger, J., and Blumberg, W. E. (1979) The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys. J. 26, 161-193
    • (1979) Biophys. J. , vol.26 , pp. 161-193
    • Dale, R.E.1    Eisinger, J.2    Blumberg, W.E.3
  • 48
    • 0035955690 scopus 로고    scopus 로고
    • ATP reorients the neck linker of kinesin in two sequential steps
    • Rosenfeld, S. S., Jefferson, G. M., and King, P. H. (2001) ATP reorients the neck linker of kinesin in two sequential steps. J. Biol. Chem. 276, 40167-40174
    • (2001) J. Biol. Chem. , vol.276 , pp. 40167-40174
    • Rosenfeld, S.S.1    Jefferson, G.M.2    King, P.H.3
  • 49
    • 33748931452 scopus 로고    scopus 로고
    • High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations
    • Kikkawa, M., and Hirokawa, N. (2006) High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations. EMBO J. 25, 4187-4194
    • (2006) EMBO J. , vol.25 , pp. 4187-4194
    • Kikkawa, M.1    Hirokawa, N.2
  • 50
    • 84862875366 scopus 로고    scopus 로고
    • All-atom structural investigation of kinesin-microtubule complex constrained by high-quality cryo-electron-microscopy maps
    • Li, M., and Zheng, W. (2012) All-atom structural investigation of kinesin-microtubule complex constrained by high-quality cryo-electron-microscopy maps. Biochemistry 51, 5022-5032
    • (2012) Biochemistry , vol.51 , pp. 5022-5032
    • Li, M.1    Zheng, W.2
  • 51
    • 77953135927 scopus 로고    scopus 로고
    • Neck linker length determines the degree of processivity in kinesin-1 and kinesin-2 motors
    • Shastry, S., and Hancock, W. O. (2010) Neck linker length determines the degree of processivity in kinesin-1 and kinesin-2 motors. Curr. Biol. 20, 939-943
    • (2010) Curr. Biol. , vol.20 , pp. 939-943
    • Shastry, S.1    Hancock, W.O.2
  • 52
    • 0033969412 scopus 로고    scopus 로고
    • Dye-pair reporter systems for protein-peptide molecular interactions
    • Geoghegan, K. F., Rosner, P. J., and Hoth, L. R. (2000) Dye-pair reporter systems for protein-peptide molecular interactions. Bioconjug. Chem. 11, 71-77
    • (2000) Bioconjug. Chem. , vol.11 , pp. 71-77
    • Geoghegan, K.F.1    Rosner, P.J.2    Hoth, L.R.3
  • 56
    • 0033545186 scopus 로고    scopus 로고
    • The bipolar kinesin, KLP61F, cross-links microtubules within interpolar microtubule bundles of Drosophila embryonic mitotic spindles
    • Sharp, D. J., McDonald, K. L., Brown, H. M., Matthies, H. J., Walczak, C., Vale, R. D., Mitchison, T. J., and Scholey, J. M. (1999) The bipolar kinesin, KLP61F, cross-links microtubules within interpolar microtubule bundles of Drosophila embryonic mitotic spindles. J. Cell Biol. 144, 125-138
    • (1999) J. Cell Biol. , vol.144 , pp. 125-138
    • Sharp, D.J.1    McDonald, K.L.2    Brown, H.M.3    Matthies, H.J.4    Walczak, C.5    Vale, R.D.6    Mitchison, T.J.7    Scholey, J.M.8
  • 58
    • 29244476067 scopus 로고    scopus 로고
    • ATPase mechanism of Eg5 in the absence of microtubules. Insight into microtubule activation and allosteric inhibition by monastrol
    • Cochran, J. C., and Gilbert, S. P. (2005) ATPase mechanism of Eg5 in the absence of microtubules. Insight into microtubule activation and allosteric inhibition by monastrol. Biochemistry 44, 16633-16648
    • (2005) Biochemistry , vol.44 , pp. 16633-16648
    • Cochran, J.C.1    Gilbert, S.P.2
  • 60
    • 72749102210 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide and inhibitor binding to wild-type and ispinesib-resistant forms of human kinesin spindle protein
    • Sheth, P. R., Basso, A., Duca, J. S., Lesburg, C. A., Ogas, P., Gray, K., Nale, L., Mannarino, A. F., Prongay, A. J., and Le, H. V. (2009) Thermodynamics of nucleotide and inhibitor binding to wild-type and ispinesib-resistant forms of human kinesin spindle protein. Biochemistry 48, 11045-11055
    • (2009) Biochemistry , vol.48 , pp. 11045-11055
    • Sheth, P.R.1    Basso, A.2    Duca, J.S.3    Lesburg, C.A.4    Ogas, P.5    Gray, K.6    Nale, L.7    Mannarino, A.F.8    Prongay, A.J.9    Le, H.V.10
  • 62
    • 49349085404 scopus 로고    scopus 로고
    • The role of kinesin neck linker and neck in velocity regulation
    • Kalchishkova, N., and Böhm, K. J. (2008) The role of kinesin neck linker and neck in velocity regulation. J. Mol. Biol. 382, 127-135
    • (2008) J. Mol. Biol. , vol.382 , pp. 127-135
    • Kalchishkova, N.1    Böhm, K.J.2
  • 63
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee. A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000) T-Coffee. A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.