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Volumn 159, Issue 4, 2014, Pages 857-868

Allosteric communication in the dynein motor domain

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DYNEIN ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DYN1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84910052449     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2014.10.018     Document Type: Article
Times cited : (79)

References (66)
  • 2
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • M. Babst, B. Wendland, E.J. Estepa, and S.D. Emr The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function EMBO J. 17 1998 2982 2993
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 3
    • 84855195754 scopus 로고    scopus 로고
    • ClpXP, an ATP-powered unfolding and protein-degradation machine
    • T.A. Baker, and R.T. Sauer ClpXP, an ATP-powered unfolding and protein-degradation machine Biochim. Biophys. Acta 1823 2012 15 28
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 15-28
    • Baker, T.A.1    Sauer, R.T.2
  • 6
    • 84876330295 scopus 로고    scopus 로고
    • Crystal clear insights into how the dynein motor moves
    • A.P. Carter Crystal clear insights into how the dynein motor moves J. Cell Sci. 126 2013 705 713
    • (2013) J. Cell Sci. , vol.126 , pp. 705-713
    • Carter, A.P.1
  • 7
    • 79952254224 scopus 로고    scopus 로고
    • Crystal structure of the dynein motor domain
    • A.P. Carter, C. Cho, L. Jin, and R.D. Vale Crystal structure of the dynein motor domain Science 331 2011 1159 1165
    • (2011) Science , vol.331 , pp. 1159-1165
    • Carter, A.P.1    Cho, C.2    Jin, L.3    Vale, R.D.4
  • 8
    • 54449089820 scopus 로고    scopus 로고
    • Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation
    • C. Cho, S.L. Reck-Peterson, and R.D. Vale Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation J. Biol. Chem. 283 2008 25839 25845
    • (2008) J. Biol. Chem. , vol.283 , pp. 25839-25845
    • Cho, C.1    Reck-Peterson, S.L.2    Vale, R.D.3
  • 9
    • 84855200343 scopus 로고    scopus 로고
    • The mechanism of dynein motility: Insight from crystal structures of the motor domain
    • C. Cho, and R.D. Vale The mechanism of dynein motility: insight from crystal structures of the motor domain Biochim. Biophys. Acta 1823 2012 182 191
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 182-191
    • Cho, C.1    Vale, R.D.2
  • 10
    • 84855828496 scopus 로고    scopus 로고
    • Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains
    • M.A. DeWitt, A.Y. Chang, P.A. Combs, and A. Yildiz Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains Science 335 2012 221 225
    • (2012) Science , vol.335 , pp. 221-225
    • Dewitt, M.A.1    Chang, A.Y.2    Combs, P.A.3    Yildiz, A.4
  • 12
    • 0041736713 scopus 로고    scopus 로고
    • Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 A resolution
    • J. Furst, R.B. Sutton, J. Chen, A.T. Brunger, and N. Grigorieff Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 A resolution EMBO J. 22 2003 4365 4374
    • (2003) EMBO J. , vol.22 , pp. 4365-4374
    • Furst, J.1    Sutton, R.B.2    Chen, J.3    Brunger, A.T.4    Grigorieff, N.5
  • 13
    • 0023655044 scopus 로고
    • Vanadate-sensitized cleavage of dynein heavy chains by 365-nm irradiation of demembranated sperm flagella and its effect on the flagellar motility
    • B.H. Gibbons, and I.R. Gibbons Vanadate-sensitized cleavage of dynein heavy chains by 365-nm irradiation of demembranated sperm flagella and its effect on the flagellar motility J. Biol. Chem. 262 1987 8354 8359
    • (1987) J. Biol. Chem. , vol.262 , pp. 8354-8359
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 14
    • 21244479076 scopus 로고    scopus 로고
    • The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk
    • I.R. Gibbons, J.E. Garbarino, C.E. Tan, S.L. Reck-Peterson, R.D. Vale, and A.P. Carter The affinity of the dynein microtubule-binding domain is modulated by the conformation of its coiled-coil stalk J. Biol. Chem. 280 2005 23960 23965
    • (2005) J. Biol. Chem. , vol.280 , pp. 23960-23965
    • Gibbons, I.R.1    Garbarino, J.E.2    Tan, C.E.3    Reck-Peterson, S.L.4    Vale, R.D.5    Carter, A.P.6
  • 15
    • 70350772363 scopus 로고    scopus 로고
    • Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine
    • S.E. Glynn, A. Martin, A.R. Nager, T.A. Baker, and R.T. Sauer Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine Cell 139 2009 744 756
    • (2009) Cell , vol.139 , pp. 744-756
    • Glynn, S.E.1    Martin, A.2    Nager, A.R.3    Baker, T.A.4    Sauer, R.T.5
  • 16
    • 84861876642 scopus 로고    scopus 로고
    • Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine
    • S.E. Glynn, A.R. Nager, T.A. Baker, and R.T. Sauer Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine Nat. Struct. Mol. Biol. 19 2012 616 622
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 616-622
    • Glynn, S.E.1    Nager, A.R.2    Baker, T.A.3    Sauer, R.T.4
  • 19
    • 84865679752 scopus 로고    scopus 로고
    • Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor
    • J. Huang, A.J. Roberts, A.E. Leschziner, and S.L. Reck-Peterson Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor Cell 150 2012 975 986
    • (2012) Cell , vol.150 , pp. 975-986
    • Huang, J.1    Roberts, A.J.2    Leschziner, A.E.3    Reck-Peterson, S.L.4
  • 20
    • 4444330119 scopus 로고    scopus 로고
    • Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein
    • T. Kon, M. Nishiura, R. Ohkura, Y.Y. Toyoshima, and K. Sutoh Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein Biochemistry 43 2004 11266 11274
    • (2004) Biochemistry , vol.43 , pp. 11266-11274
    • Kon, T.1    Nishiura, M.2    Ohkura, R.3    Toyoshima, Y.Y.4    Sutoh, K.5
  • 23
    • 79958844185 scopus 로고    scopus 로고
    • X-ray structure of a functional full-length dynein motor domain
    • T. Kon, K. Sutoh, and G. Kurisu X-ray structure of a functional full-length dynein motor domain Nat. Struct. Mol. Biol. 18 2011 638 642
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 638-642
    • Kon, T.1    Sutoh, K.2    Kurisu, G.3
  • 25
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • A. Kucukelbir, F.J. Sigworth, and H.D. Tagare Quantifying the local resolution of cryo-EM density maps Nat. Methods 11 2014 63 65
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 26
    • 84875590005 scopus 로고    scopus 로고
    • Force generation by kinesin and myosin cytoskeletal motor proteins
    • F.J. Kull, and S.A. Endow Force generation by kinesin and myosin cytoskeletal motor proteins J. Cell Sci. 126 2013 9 19
    • (2013) J. Cell Sci. , vol.126 , pp. 9-19
    • Kull, F.J.1    Endow, S.A.2
  • 27
    • 33846188909 scopus 로고    scopus 로고
    • Visualizing the ATPase cycle in a protein disaggregating machine: Structural basis for substrate binding by ClpB
    • S. Lee, J.M. Choi, and F.T. Tsai Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB Mol. Cell 25 2007 261 271
    • (2007) Mol. Cell , vol.25 , pp. 261-271
    • Lee, S.1    Choi, J.M.2    Tsai, F.T.3
  • 29
    • 84892882219 scopus 로고    scopus 로고
    • Marching to the beat of the ring: Polypeptide translocation by AAA+ proteases
    • K. Nyquist, and A. Martin Marching to the beat of the ring: polypeptide translocation by AAA+ proteases Trends Biochem. Sci. 39 2014 53 60
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 53-60
    • Nyquist, K.1    Martin, A.2
  • 30
    • 1642377971 scopus 로고    scopus 로고
    • Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    • T. Ogura, S.W. Whiteheart, and A.J. Wilkinson Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases J. Struct. Biol. 146 2004 106 112
    • (2004) J. Struct. Biol. , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 34
    • 1242319567 scopus 로고    scopus 로고
    • Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae
    • S.L. Reck-Peterson, and R.D. Vale Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae Proc. Natl. Acad. Sci. USA 101 2004 1491 1495
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1491-1495
    • Reck-Peterson, S.L.1    Vale, R.D.2
  • 38
    • 84855818650 scopus 로고    scopus 로고
    • A Bayesian view on cryo-EM structure determination
    • S.H. Scheres A Bayesian view on cryo-EM structure determination J. Mol. Biol. 415 2012 406 418
    • (2012) J. Mol. Biol. , vol.415 , pp. 406-418
    • Scheres, S.H.1
  • 39
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • S.H. Scheres RELION: implementation of a Bayesian approach to cryo-EM structure determination J. Struct. Biol. 180 2012 519 530
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 41
    • 84860721580 scopus 로고    scopus 로고
    • Insights into dynein motor domain function from a 3.3-A crystal structure
    • S491
    • H. Schmidt, E.S. Gleave, and A.P. Carter Insights into dynein motor domain function from a 3.3-A crystal structure Nat. Struct. Mol. Biol. 19 2012 492 497 S491
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 492-497
    • Schmidt, H.1    Gleave, E.S.2    Carter, A.P.3
  • 42
    • 0037559627 scopus 로고    scopus 로고
    • Structure of the Rho transcription terminator: Mechanism of mRNA recognition and helicase loading
    • E. Skordalakes, and J.M. Berger Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading Cell 114 2003 135 146
    • (2003) Cell , vol.114 , pp. 135-146
    • Skordalakes, E.1    Berger, J.M.2
  • 43
    • 36549048006 scopus 로고    scopus 로고
    • The AAA+ superfamily - A myriad of motions
    • P.A. Tucker, and L. Sallai The AAA+ superfamily - a myriad of motions Curr. Opin. Struct. Biol. 17 2007 641 652
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 641-652
    • Tucker, P.A.1    Sallai, L.2
  • 44
    • 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
  • 45
    • 0037155139 scopus 로고    scopus 로고
    • Roles of the two ATP binding sites of ClpB from Thermus thermophilus
    • Y.H. Watanabe, K. Motohashi, and M. Yoshida Roles of the two ATP binding sites of ClpB from Thermus thermophilus J. Biol. Chem. 277 2002 5804 5809
    • (2002) J. Biol. Chem. , vol.277 , pp. 5804-5809
    • Watanabe, Y.H.1    Motohashi, K.2    Yoshida, M.3
  • 46
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • S.C. West Molecular views of recombination proteins and their control Nat. Rev. Mol. Cell Biol. 4 2003 435 445
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 435-445
    • West, S.C.1
  • 48
    • 41449108157 scopus 로고    scopus 로고
    • An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments
    • C.E. Aitken, R.A. Marshall, and J.D. Puglisi An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments Biophys. J. 94 2008 1826 1835
    • (2008) Biophys. J. , vol.94 , pp. 1826-1835
    • Aitken, C.E.1    Marshall, R.A.2    Puglisi, J.D.3
  • 51
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, and A. Leith SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 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
  • 55
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • X. Li, P. Mooney, S. Zheng, C.R. Booth, M.B. Braunfeld, S. Gubbens, D.A. Agard, and Y. Cheng Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM Nat. Methods 10 2013 584 590
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 56
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • M. Liao, E. Cao, D. Julius, and Y. Cheng Structure of the TRPV1 ion channel determined by electron cryo-microscopy Nature 504 2013 107 112
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 58
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • J.A. Mindell, and N. Grigorieff Accurate determination of local defocus and specimen tilt in electron microscopy J. Struct. Biol. 142 2003 334 347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 60
    • 0346816491 scopus 로고    scopus 로고
    • FindEM - A fast, efficient program for automatic selection of particles from electron micrographs
    • A.M. Roseman FindEM - a fast, efficient program for automatic selection of particles from electron micrographs J. Struct. Biol. 145 2004 91 99
    • (2004) J. Struct. Biol. , vol.145 , pp. 91-99
    • Roseman, A.M.1
  • 61
    • 27544478958 scopus 로고    scopus 로고
    • Fast maximum-likelihood refinement of electron microscopy images
    • S.H. Scheres, M. Valle, and J.M. Carazo Fast maximum-likelihood refinement of electron microscopy images Bioinformatics 21 Suppl 2 2005 ii243 ii244
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 2 , pp. 243-ii244
    • Scheres, S.H.1    Valle, M.2    Carazo, J.M.3
  • 63
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • M. Strong, M.R. Sawaya, S. Wang, M. Phillips, D. Cascio, and D. Eisenberg Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis Proc. Natl. Acad. Sci. USA 103 2006 8060 8065
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 65
    • 84884676741 scopus 로고    scopus 로고
    • Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains
    • M.E. Tanenbaum, R.D. Vale, and R.J. McKenney Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains Elife 2 2013 e00943
    • (2013) Elife , vol.2 , pp. 00943
    • Tanenbaum, M.E.1    Vale, R.D.2    McKenney, R.J.3
  • 66
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy
    • N.R. Voss, C.K. Yoshioka, M. Radermacher, C.S. Potter, and B. Carragher DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy J. Struct. Biol. 166 2009 205 213
    • (2009) J. Struct. Biol. , vol.166 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5


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