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Volumn 19, Issue 5, 2005, Pages 595-605

The structural basis of myosin V processive movement as revealed by electron cryomicroscopy

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN V;

EID: 24044451511     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.07.015     Document Type: Article
Times cited : (84)

References (45)
  • 1
    • 1842681965 scopus 로고    scopus 로고
    • Myosin V processivity: Multiple kinetic pathways for head-to-head coordination
    • doi10.1073/pnas.0307247101
    • J.E. Baker, E.B. Krementsova, G.G. Kennedy, A. Armstrong, K.M. Trybus, and D.M. Warshaw Myosin V processivity: multiple kinetic pathways for head-to-head coordination Proc. Natl. Acad. Sci. USA 101 2004 5542 5546 10.1073/pnas.0307247101 Published online March 31, 2004
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5542-5546
    • Baker, J.E.1    Krementsova, E.B.2    Kennedy, G.G.3    Armstrong, A.4    Trybus, K.M.5    Warshaw, D.M.6
  • 2
    • 0030678623 scopus 로고    scopus 로고
    • Flexibility within myosin heads revealed by negative stain and single- particle analysis
    • S.A. Burgess, M.L. Walker, H.D. White, and J. Trinick Flexibility within myosin heads revealed by negative stain and single- particle analysis J. Cell Biol. 139 1997 675 681
    • (1997) J. Cell Biol. , vol.139 , pp. 675-681
    • Burgess, S.A.1    Walker, M.L.2    White, H.D.3    Trinick, J.4
  • 5
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemo-mechanical transduction
    • P.D. Coureux, H.L. Sweeney, and A. Houdusse Three myosin V structures delineate essential features of chemo-mechanical transduction EMBO J. 23 2004 4527 4537
    • (2004) EMBO J. , vol.23 , pp. 4527-4537
    • Coureux, P.D.1    Sweeney, H.L.2    Houdusse, A.3
  • 7
    • 0034700284 scopus 로고    scopus 로고
    • Actin and light chain isoform dependence of myosin V kinetics
    • E.M. De La Cruz, A.L. Wells, H.L. Sweeney, and E.M. Ostap Actin and light chain isoform dependence of myosin V kinetics Biochemistry 39 2000 14196 14202
    • (2000) Biochemistry , vol.39 , pp. 14196-14202
    • De La Cruz, E.M.1    Wells, A.L.2    Sweeney, H.L.3    Ostap, E.M.4
  • 8
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • R. Dominguez, Y. Freyzon, K.M. Trybus, and C. Cohen Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state Cell 94 1998 559 571
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 9
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • E.H. Egelman A robust algorithm for the reconstruction of helical filaments using single-particle methods Ultramicroscopy 85 2000 225 234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 11
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • V.E. Galkin, A. Orlova, N. Lukoyanova, W. Wriggers, and E.H. Egelman Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits J. Cell Biol. 153 2001 75 86
    • (2001) J. Cell Biol. , vol.153 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggers, W.4    Egelman, E.H.5
  • 12
    • 0037092046 scopus 로고    scopus 로고
    • The utrophin actin-binding domain binds F-actin in two different modes: Implications for the spectrin superfamily of proteins
    • 10.1083/jcb.200111097
    • V.E. Galkin, A. Orlova, M.S. VanLoock, I.N. Rybakova, J.M. Ervasti, and E.H. Egelman The utrophin actin-binding domain binds F-actin in two different modes: implications for the spectrin superfamily of proteins J. Cell Biol. 157 2002 243 251 10.1083/jcb.200111097 Published online April 15, 2002
    • (2002) J. Cell Biol. , vol.157 , pp. 243-251
    • Galkin, V.E.1    Orlova, A.2    Vanloock, M.S.3    Rybakova, I.N.4    Ervasti, J.M.5    Egelman, E.H.6
  • 13
    • 0041620499 scopus 로고    scopus 로고
    • Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?
    • V.E. Galkin, A. Orlova, M.S. VanLoock, and E.H. Egelman Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation? J. Mol. Biol. 331 2003 967 972
    • (2003) J. Mol. Biol. , vol.331 , pp. 967-972
    • Galkin, V.E.1    Orlova, A.2    Vanloock, M.S.3    Egelman, E.H.4
  • 14
    • 0346849714 scopus 로고    scopus 로고
    • ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments
    • doi10.1083/jcb.200308144
    • V.E. Galkin, A. Orlova, M.S. VanLoock, A. Shvetsov, E. Reisler, and E.H. Egelman ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments J. Cell Biol. 163 2003 1057 1066 10.1083/jcb.200308144 Published online December 1, 2003
    • (2003) J. Cell Biol. , vol.163 , pp. 1057-1066
    • Galkin, V.E.1    Orlova, A.2    Vanloock, M.S.3    Shvetsov, A.4    Reisler, E.5    Egelman, E.H.6
  • 15
    • 0030768794 scopus 로고    scopus 로고
    • X-ray structures of the MgADP, MgATPγS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain
    • A.M. Gulick, C.B. Bauer, J.B. Thoden, and I. Rayment X-ray structures of the MgADP, MgATPγS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain Biochemistry 36 1997 11619 11628
    • (1997) Biochemistry , vol.36 , pp. 11619-11628
    • Gulick, A.M.1    Bauer, C.B.2    Thoden, J.B.3    Rayment, I.4
  • 16
    • 0033119483 scopus 로고    scopus 로고
    • A new algorithm to align three-dimensional maps of helical structures
    • D. Hanein, and D. DeRosier A new algorithm to align three-dimensional maps of helical structures Ultramicroscopy 76 1999 233 238
    • (1999) Ultramicroscopy , vol.76 , pp. 233-238
    • Hanein, D.1    Derosier, D.2
  • 17
    • 0030727339 scopus 로고    scopus 로고
    • Evidence for a conformational change in actin induced by fimbrin (N375) binding
    • D. Hanein, P. Matsudaira, and D.J. DeRosier Evidence for a conformational change in actin induced by fimbrin (N375) binding J. Cell Biol. 139 1997 387 396
    • (1997) J. Cell Biol. , vol.139 , pp. 387-396
    • Hanein, D.1    Matsudaira, P.2    Derosier, D.J.3
  • 19
    • 0141843643 scopus 로고    scopus 로고
    • Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • K.C. Holmes, I. Angert, F.J. Kull, W. Jahn, and R.R. Schroder Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide Nature 425 2003 423 427
    • (2003) Nature , vol.425 , pp. 423-427
    • Holmes, K.C.1    Angert, I.2    Kull, F.J.3    Jahn, W.4    Schroder, R.R.5
  • 20
    • 0042165822 scopus 로고    scopus 로고
    • Addition of lysines to the 50/20 kDa junction of myosin strengthens weak binding to actin without affecting the maximum ATPase activity
    • P.B. Joel, H.L. Sweeney, and K.M. Trybus Addition of lysines to the 50/20 kDa junction of myosin strengthens weak binding to actin without affecting the maximum ATPase activity Biochemistry 42 2003 9160 9166
    • (2003) Biochemistry , vol.42 , pp. 9160-9166
    • Joel, P.B.1    Sweeney, H.L.2    Trybus, K.M.3
  • 21
    • 1642286846 scopus 로고    scopus 로고
    • Myosin V: Regulation by calcium, calmodulin, and the tail domain
    • doi10.1083/jcb.200310065
    • D.N. Krementsov, E.B. Krementsova, and K.M. Trybus Myosin V: regulation by calcium, calmodulin, and the tail domain J. Cell Biol. 164 2004 877 886 10.1083/jcb.200310065 Published online March 8, 2004
    • (2004) J. Cell Biol. , vol.164 , pp. 877-886
    • Krementsov, D.N.1    Krementsova, E.B.2    Trybus, K.M.3
  • 22
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • S.J. Ludtke, P.R. Baldwin, and W. Chiu EMAN: semiautomated software for high-resolution single-particle reconstructions J. Struct. Biol. 128 1999 82 97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 24
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • R.A. Milligan Protein-protein interactions in the rigor actomyosin complex Proc. Natl. Acad. Sci. USA 93 1996 21 26
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 28
    • 11144226184 scopus 로고    scopus 로고
    • Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization
    • doi10.1073/pnas.0407525102
    • A. Orlova, A. Shvetsov, V.E. Galkin, D.S. Kudryashov, P.A. Rubenstein, E.H. Egelman, and E. Reisler Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization Proc. Natl. Acad. Sci. USA 101 2004 17664 17668 10.1073/pnas.0407525102 Published online December 10, 2004
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17664-17668
    • Orlova, A.1    Shvetsov, A.2    Galkin, V.E.3    Kudryashov, D.S.4    Rubenstein, P.A.5    Egelman, E.H.6    Reisler, E.7
  • 29
    • 0029916489 scopus 로고    scopus 로고
    • Image analysis of helical objects: The Brandeis Helical Package
    • C.H. Owen, D.G. Morgan, and D.J. DeRosier Image analysis of helical objects: the Brandeis Helical Package J. Struct. Biol. 116 1996 167 175
    • (1996) J. Struct. Biol. , vol.116 , pp. 167-175
    • Owen, C.H.1    Morgan, D.G.2    Derosier, D.J.3
  • 32
    • 0032078226 scopus 로고    scopus 로고
    • Reconstruction of symmetry deviations: A procedure to analyze partially decorated F-actin and other incomplete structures
    • L.E. Rost, D. Hanein, and D.J. DeRosier Reconstruction of symmetry deviations: a procedure to analyze partially decorated F-actin and other incomplete structures Ultramicroscopy 72 1998 187 197
    • (1998) Ultramicroscopy , vol.72 , pp. 187-197
    • Rost, L.E.1    Hanein, D.2    Derosier, D.J.3
  • 34
    • 0242677759 scopus 로고    scopus 로고
    • Myosin V motor proteins: Marching stepwise towards a mechanism
    • R.D. Vale Myosin V motor proteins: marching stepwise towards a mechanism J. Cell Biol. 163 2003 445 450
    • (2003) J. Cell Biol. , vol.163 , pp. 445-450
    • Vale, R.D.1
  • 35
    • 0036424944 scopus 로고    scopus 로고
    • A novel three-dimensional variant of the watershed transform for segmentation of electron density maps
    • N. Volkmann A novel three-dimensional variant of the watershed transform for segmentation of electron density maps J. Struct. Biol. 138 2002 123 130
    • (2002) J. Struct. Biol. , vol.138 , pp. 123-130
    • Volkmann, N.1
  • 36
    • 0032779888 scopus 로고    scopus 로고
    • Quantitative fitting of atomic models into observed densities derived by electron microscopy
    • N. Volkmann, and D. Hanein Quantitative fitting of atomic models into observed densities derived by electron microscopy J. Struct. Biol. 125 1999 176 184
    • (1999) J. Struct. Biol. , vol.125 , pp. 176-184
    • Volkmann, N.1    Hanein, D.2
  • 37
    • 0033952309 scopus 로고    scopus 로고
    • Actomyosin: Law and order in motility
    • N. Volkmann, and D. Hanein Actomyosin: law and order in motility Curr. Opin. Cell Biol. 12 2000 26 34
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 26-34
    • Volkmann, N.1    Hanein, D.2
  • 38
    • 0347380212 scopus 로고    scopus 로고
    • Docking of atomic models into reconstructions from electron microscopy
    • N. Volkmann, and D. Hanein Docking of atomic models into reconstructions from electron microscopy Methods Enzymol. 374 2003 204 225
    • (2003) Methods Enzymol. , vol.374 , pp. 204-225
    • Volkmann, N.1    Hanein, D.2
  • 40
    • 0037452929 scopus 로고    scopus 로고
    • Myosin isoforms show unique conformations in the actin-bound state
    • doi10.1073/pnas.0536510100
    • N. Volkmann, G. Ouyang, K.M. Trybus, D.J. DeRosier, S. Lowey, and D. Hanein Myosin isoforms show unique conformations in the actin-bound state Proc. Natl. Acad. Sci. USA 100 2003 3227 3232 10.1073/pnas.0536510100 Published online February 28, 2003
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3227-3232
    • Volkmann, N.1    Ouyang, G.2    Trybus, K.M.3    Derosier, D.J.4    Lowey, S.5    Hanein, D.6
  • 43
    • 0345414561 scopus 로고    scopus 로고
    • Issues of resolution and polymorphism in single-particle reconstruction
    • S. Yang, X. Yu, V.E. Galkin, and E.H. Egelman Issues of resolution and polymorphism in single-particle reconstruction J. Struct. Biol. 144 2003 162 171
    • (2003) J. Struct. Biol. , vol.144 , pp. 162-171
    • Yang, S.1    Yu, X.2    Galkin, V.E.3    Egelman, E.H.4
  • 44
    • 1542267772 scopus 로고    scopus 로고
    • Functional role of loop 2 in myosin V
    • C.M. Yengo, and H.L. Sweeney Functional role of loop 2 in myosin V Biochemistry 43 2004 2605 2612
    • (2004) Biochemistry , vol.43 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.