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Volumn 107, Issue 9, 2014, Pages 2204-2213

Kinesin-5 allosteric inhibitors uncouple the dynamics of nucleotide, microtubule, and neck-linker binding sites

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; KIF11 PROTEIN, HUMAN; KINESIN; NUCLEOTIDE; PROTEIN BINDING;

EID: 84908544641     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.09.019     Document Type: Article
Times cited : (50)

References (47)
  • 1
    • 84885425344 scopus 로고    scopus 로고
    • Kinesin-5: Cross-bridging mechanism to targeted clinical therapy
    • E.J. Wojcik, and R.S. Buckley S. Kim Kinesin-5: cross-bridging mechanism to targeted clinical therapy Gene 531 2013 133 149
    • (2013) Gene , vol.531 , pp. 133-149
    • Wojcik, E.J.1    Buckley, R.S.2    Kim, S.3
  • 2
    • 84884978380 scopus 로고    scopus 로고
    • MAPping out distribution routes for kinesin couriers
    • J. Atherton, A. Houdusse, and C. Moores MAPping out distribution routes for kinesin couriers Biol. Cell 105 2013 465 487
    • (2013) Biol. Cell , vol.105 , pp. 465-487
    • Atherton, J.1    Houdusse, A.2    Moores, C.3
  • 3
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • R.D. Vale, and R.A. Milligan The way things move: looking under the hood of molecular motor proteins Science 288 2000 88 95
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 4
    • 0347623370 scopus 로고    scopus 로고
    • Kinesin moves by an asymmetric hand-over-hand mechanism
    • C.L. Asbury, A.N. Fehr, and S.M. Block Kinesin moves by an asymmetric hand-over-hand mechanism Science 302 2003 2130 2134
    • (2003) Science , vol.302 , pp. 2130-2134
    • Asbury, C.L.1    Fehr, A.N.2    Block, S.M.3
  • 6
    • 0035942761 scopus 로고    scopus 로고
    • Switch-based mechanism of kinesin motors
    • M. Kikkawa, and E.P. Sablin N. Hirokawa Switch-based mechanism of kinesin motors Nature 411 2001 439 445
    • (2001) Nature , vol.411 , pp. 439-445
    • Kikkawa, M.1    Sablin, E.P.2    Hirokawa, N.3
  • 7
    • 82455211990 scopus 로고    scopus 로고
    • A seesaw model for intermolecular gating in the kinesin motor protein
    • C.V. Sindelar A seesaw model for intermolecular gating in the kinesin motor protein Biophys Rev 3 2011 85 100
    • (2011) Biophys Rev , vol.3 , pp. 85-100
    • Sindelar, C.V.1
  • 8
    • 0033576727 scopus 로고    scopus 로고
    • A structural change in the kinesin motor protein that drives motility
    • S. Rice, and A.W. Lin R.D. Vale A structural change in the kinesin motor protein that drives motility Nature 402 1999 778 784
    • (1999) Nature , vol.402 , pp. 778-784
    • Rice, S.1    Lin, A.W.2    Vale, R.D.3
  • 10
    • 84893496828 scopus 로고    scopus 로고
    • Comprehensive structural model of the mechanochemical cycle of a mitotic motor highlights molecular adaptations in the kinesin family
    • A. Goulet, and J. Major C.A. Moores Comprehensive structural model of the mechanochemical cycle of a mitotic motor highlights molecular adaptations in the kinesin family Proc. Natl. Acad. Sci. USA 111 2014 1837 1842
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 1837-1842
    • Goulet, A.1    Major, J.2    Moores, C.A.3
  • 11
    • 84871744734 scopus 로고    scopus 로고
    • The structural basis of force generation by the mitotic motor kinesin-5
    • A. Goulet, and W.M. Behnke-Parks C.A. Moores The structural basis of force generation by the mitotic motor kinesin-5 J. Biol. Chem. 287 2012 44654 44666
    • (2012) J. Biol. Chem. , vol.287 , pp. 44654-44666
    • Goulet, A.1    Behnke-Parks, W.M.2    Moores, C.A.3
  • 12
    • 27444445780 scopus 로고    scopus 로고
    • Docking and rolling, a model of how the mitotic motor Eg5 works
    • S.S. Rosenfeld, and J. Xing P.H. King Docking and rolling, a model of how the mitotic motor Eg5 works J. Biol. Chem. 280 2005 35684 35695
    • (2005) J. Biol. Chem. , vol.280 , pp. 35684-35695
    • Rosenfeld, S.S.1    Xing, J.2    King, P.H.3
  • 13
    • 84888268596 scopus 로고    scopus 로고
    • Mapping the structural and dynamical features of kinesin motor domains
    • G. Scarabelli, and B.J. Grant Mapping the structural and dynamical features of kinesin motor domains PLOS Comput. Biol. 9 2013 e1003329
    • (2013) PLOS Comput. Biol. , vol.9 , pp. 1003329
    • Scarabelli, G.1    Grant, B.J.2
  • 14
    • 84877258986 scopus 로고    scopus 로고
    • Kinesin-5 seems to step to its own unique tune, but really it's a cover
    • S.E. Rice Kinesin-5 seems to step to its own unique tune, but really it's a cover Biophys. J. 104 2013 1846 1848
    • (2013) Biophys. J. , vol.104 , pp. 1846-1848
    • Rice, S.E.1
  • 15
    • 77953315697 scopus 로고    scopus 로고
    • Allosteric drug discrimination is coupled to mechanochemical changes in the kinesin-5 motor core
    • E.D. Kim, and R. Buckley S. Kim Allosteric drug discrimination is coupled to mechanochemical changes in the kinesin-5 motor core J. Biol. Chem. 285 2010 18650 18661
    • (2010) J. Biol. Chem. , vol.285 , pp. 18650-18661
    • Kim, E.D.1    Buckley, R.2    Kim, S.3
  • 16
    • 77951221121 scopus 로고    scopus 로고
    • Real-time structural transitions are coupled to chemical steps in ATP hydrolysis by Eg5 kinesin
    • B. Jun, and S. Kim Real-time structural transitions are coupled to chemical steps in ATP hydrolysis by Eg5 kinesin J. Biol. Chem. 285 2010 11073 11077
    • (2010) J. Biol. Chem. , vol.285 , pp. 11073-11077
    • Jun, B.1    Kim, S.2
  • 17
    • 79953129078 scopus 로고    scopus 로고
    • Loop L5 acts as a conformational latch in the mitotic kinesin Eg5
    • W.M. Behnke-Parks, and J. Vendome S.S. Rosenfeld Loop L5 acts as a conformational latch in the mitotic kinesin Eg5 J. Biol. Chem. 286 2011 5242 5253
    • (2011) J. Biol. Chem. , vol.286 , pp. 5242-5253
    • Behnke-Parks, W.M.1    Vendome, J.2    Rosenfeld, S.S.3
  • 18
    • 84877311437 scopus 로고    scopus 로고
    • Modular aspects of kinesin force generation machinery
    • W.R. Hesse, and M. Steiner M.J. Lang Modular aspects of kinesin force generation machinery Biophys. J. 104 2013 1969 1978
    • (2013) Biophys. J. , vol.104 , pp. 1969-1978
    • Hesse, W.R.1    Steiner, M.2    Lang, M.J.3
  • 19
    • 63549096871 scopus 로고    scopus 로고
    • Ras conformational switching: Simulating nucleotide-dependent conformational transitions with accelerated molecular dynamics
    • B.J. Grant, A.A. Gorfe, and J.A. McCammon Ras conformational switching: simulating nucleotide-dependent conformational transitions with accelerated molecular dynamics PLOS Comput. Biol. 5 2009 e1000325
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000325
    • Grant, B.J.1    Gorfe, A.A.2    McCammon, J.A.3
  • 20
    • 78649801418 scopus 로고    scopus 로고
    • Conformational selection in G-proteins: Lessons from Ras and Rho
    • B.J. Grant, J.A. McCammon, and A.A. Gorfe Conformational selection in G-proteins: lessons from Ras and Rho Biophys. J. 99 2010 L87 L89
    • (2010) Biophys. J. , vol.99 , pp. 87-L89
    • Grant, B.J.1    McCammon, J.A.2    Gorfe, A.A.3
  • 21
    • 84889008365 scopus 로고    scopus 로고
    • Loop L5 assumes three distinct orientations during the ATPase cycle of the mitotic kinesin Eg5: A transient and time-resolved fluorescence study
    • J.M. Muretta, and W.M. Behnke-Parks S.S. Rosenfeld Loop L5 assumes three distinct orientations during the ATPase cycle of the mitotic kinesin Eg5: a transient and time-resolved fluorescence study J. Biol. Chem. 288 2013 34839 34849
    • (2013) J. Biol. Chem. , vol.288 , pp. 34839-34849
    • Muretta, J.M.1    Behnke-Parks, W.M.2    Rosenfeld, S.S.3
  • 22
    • 44649199260 scopus 로고    scopus 로고
    • Mapping the nucleotide and isoform-dependent structural and dynamical features of Ras proteins
    • A.A. Gorfe, B.J. Grant, and J.A. McCammon Mapping the nucleotide and isoform-dependent structural and dynamical features of Ras proteins Structure 16 2008 885 896
    • (2008) Structure , vol.16 , pp. 885-896
    • Gorfe, A.A.1    Grant, B.J.2    McCammon, J.A.3
  • 23
    • 84880359502 scopus 로고    scopus 로고
    • Domain-opening and dynamic coupling in the α-subunit of heterotrimeric G proteins
    • X.Q. Yao, and B.J. Grant Domain-opening and dynamic coupling in the α-subunit of heterotrimeric G proteins Biophys. J. 105 2013 L08 L10
    • (2013) Biophys. J. , vol.105 , pp. 08-L10
    • Yao, X.Q.1    Grant, B.J.2
  • 24
    • 77949318844 scopus 로고    scopus 로고
    • ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism
    • C.L. Parke, and E.J. Wojcik D.K. Worthylake ATP hydrolysis in Eg5 kinesin involves a catalytic two-water mechanism J. Biol. Chem. 285 2010 5859 5867
    • (2010) J. Biol. Chem. , vol.285 , pp. 5859-5867
    • Parke, C.L.1    Wojcik, E.J.2    Worthylake, D.K.3
  • 25
    • 0035816597 scopus 로고    scopus 로고
    • Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker
    • J. Turner, and R. Anderson R. Sakowicz Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker J. Biol. Chem. 276 2001 25496 25502
    • (2001) J. Biol. Chem. , vol.276 , pp. 25496-25502
    • Turner, J.1    Anderson, R.2    Sakowicz, R.3
  • 27
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 28
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • M.Y. Shen, and A. Sali Statistical potential for assessment and prediction of protein structures Protein Sci. 15 2006 2507 2524
    • (2006) Protein Sci. , vol.15 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 30
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • V. Hornak, and R. Abel C. Simmerling Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65 2006 712 725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Simmerling, C.3
  • 31
    • 0037495965 scopus 로고    scopus 로고
    • Development of polyphosphate parameters for use with the AMBER force field
    • K.L. Meagher, L.T. Redman, and H.A. Carlson Development of polyphosphate parameters for use with the AMBER force field J. Comput. Chem. 24 2003 1016 1025
    • (2003) J. Comput. Chem. , vol.24 , pp. 1016-1025
    • Meagher, K.L.1    Redman, L.T.2    Carlson, H.A.3
  • 32
    • 2942532422 scopus 로고    scopus 로고
    • Development and testing of a general Amber force field
    • J. Wang, and R.M. Wolf D.A. Case Development and testing of a general Amber force field J. Comput. Chem. 25 2004 1157 1174
    • (2004) J. Comput. Chem. , vol.25 , pp. 1157-1174
    • Wang, J.1    Wolf, R.M.2    Case, D.A.3
  • 34
    • 33750398103 scopus 로고    scopus 로고
    • Bio3d: An R package for the comparative analysis of protein structures
    • B.J. Grant, and A.P. Rodrigues L.S. Caves Bio3d: an R package for the comparative analysis of protein structures Bioinformatics 22 2006 2695 2696
    • (2006) Bioinformatics , vol.22 , pp. 2695-2696
    • Grant, B.J.1    Rodrigues, A.P.2    Caves, L.S.3
  • 35
    • 33644847828 scopus 로고    scopus 로고
    • Generalized correlation for biomolecular dynamics
    • O.F. Lange, and H. Grubmüller Generalized correlation for biomolecular dynamics Proteins 62 2006 1053 1061
    • (2006) Proteins , vol.62 , pp. 1053-1061
    • Lange, O.F.1    Grubmüller, H.2
  • 36
    • 84894119536 scopus 로고    scopus 로고
    • Weighted implementation of suboptimal paths (WISP): An optimized algorithm and tool for dynamical network analysis
    • A.T. Van Wart, and J. Durrant R.E. Amaro Weighted implementation of suboptimal paths (WISP): an optimized algorithm and tool for dynamical network analysis J. Chem. Theory Comput. 10 2014 511 517
    • (2014) J. Chem. Theory Comput. , vol.10 , pp. 511-517
    • Van Wart, A.T.1    Durrant, J.2    Amaro, R.E.3
  • 37
    • 79952822799 scopus 로고    scopus 로고
    • Exploring the intermediate states of ADP-ATP exchange: A simulation study on Eg5
    • W. Zhang Exploring the intermediate states of ADP-ATP exchange: a simulation study on Eg5 J. Phys. Chem. B 115 2011 784 795
    • (2011) J. Phys. Chem. B , vol.115 , pp. 784-795
    • Zhang, W.1
  • 38
    • 84867626070 scopus 로고    scopus 로고
    • Altered nucleotide-microtubule coupling and increased mechanical output by a kinesin mutant
    • H.L. Liu, M.A. Hallen, and S.A. Endow Altered nucleotide-microtubule coupling and increased mechanical output by a kinesin mutant PLoS ONE 7 2012 e47148
    • (2012) PLoS ONE , vol.7 , pp. 47148
    • Liu, H.L.1    Hallen, M.A.2    Endow, S.A.3
  • 39
    • 58049202168 scopus 로고    scopus 로고
    • Kinesin's cover-neck bundle folds forward to generate force
    • A.S. Khalil, and D.C. Appleyard M.J. Lang Kinesin's cover-neck bundle folds forward to generate force Proc. Natl. Acad. Sci. USA 105 2008 19247 19252
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19247-19252
    • Khalil, A.S.1    Appleyard, D.C.2    Lang, M.J.3
  • 41
    • 84871836555 scopus 로고    scopus 로고
    • Allosteric networks in thrombin distinguish procoagulant vs.Anticoagulant activities
    • P.M. Gasper, and B. Fuglestad J.A. McCammon Allosteric networks in thrombin distinguish procoagulant vs. anticoagulant activities Proc. Natl. Acad. Sci. USA 109 2012 21216 21222
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 21216-21222
    • Gasper, P.M.1    Fuglestad, B.2    McCammon, J.A.3
  • 42
    • 84878477071 scopus 로고    scopus 로고
    • A mechanistic understanding of allosteric immune escape pathways in the HIV-1 envelope glycoprotein
    • A. Sethi, and J. Tian S. Gnanakaran A mechanistic understanding of allosteric immune escape pathways in the HIV-1 envelope glycoprotein PLOS Comput. Biol. 9 2013 e1003046
    • (2013) PLOS Comput. Biol. , vol.9 , pp. 1003046
    • Sethi, A.1    Tian, J.2    Gnanakaran, S.3
  • 43
    • 0034628619 scopus 로고    scopus 로고
    • Role of the kinesin neck linker and catalytic core in microtubule-based motility
    • R.B. Case, and S. Rice R.D. Vale Role of the kinesin neck linker and catalytic core in microtubule-based motility Curr. Biol. 10 2000 157 160
    • (2000) Curr. Biol. , vol.10 , pp. 157-160
    • Case, R.B.1    Rice, S.2    Vale, R.D.3
  • 44
    • 0028355574 scopus 로고
    • Pre-steady-state kinetics of the microtubule-kinesin ATPase
    • S.P. Gilbert, and K.A. Johnson Pre-steady-state kinetics of the microtubule-kinesin ATPase Biochemistry 33 1994 1951 1960
    • (1994) Biochemistry , vol.33 , pp. 1951-1960
    • Gilbert, S.P.1    Johnson, K.A.2
  • 45
    • 0028865659 scopus 로고
    • Mechanism of microtubule kinesin ATPase
    • Y.Z. Ma, and E.W. Taylor Mechanism of microtubule kinesin ATPase Biochemistry 34 1995 13242 13251
    • (1995) Biochemistry , vol.34 , pp. 13242-13251
    • Ma, Y.Z.1    Taylor, E.W.2
  • 46
    • 84879993265 scopus 로고    scopus 로고
    • Role of kinesin-1 in the pathogenesis of SPG10, a rare form of hereditary spastic paraplegia
    • K. Kawaguchi Role of kinesin-1 in the pathogenesis of SPG10, a rare form of hereditary spastic paraplegia Neuroscientist 19 2013 336 344
    • (2013) Neuroscientist , vol.19 , pp. 336-344
    • Kawaguchi, K.1
  • 47
    • 84866060266 scopus 로고    scopus 로고
    • Three routes to suppression of the neurodegenerative phenotypes caused by kinesin heavy chain mutations
    • I. Djagaeva, and D.J. Rose W.M. Saxton Three routes to suppression of the neurodegenerative phenotypes caused by kinesin heavy chain mutations Genetics 192 2012 173 183
    • (2012) Genetics , vol.192 , pp. 173-183
    • Djagaeva, I.1    Rose, D.J.2    Saxton, W.M.3


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