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Volumn 23, Issue 9, 2015, Pages 1584-1595

α- and β-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ALPHA TUBULIN; AXONEMAL DYNEIN; BETA TUBULIN; BINDING PROTEIN; DIMER; KINESIN; CYTOSKELETON PROTEIN; PROTEIN BINDING; PROTOZOAL PROTEIN; TUBULIN;

EID: 84947033667     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.06.017     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 84901362834 scopus 로고    scopus 로고
    • High-resolution microtubule structures reveal the structural transitions in αβ-tubulin upon GTP hydrolysis
    • G.M. Alushin, G.C. Lander, E.H. Kellogg, R. Zhang, D. Baker, and E. Nogales High-resolution microtubule structures reveal the structural transitions in αβ-tubulin upon GTP hydrolysis Cell 157 2014 1117 1129
    • (2014) Cell , vol.157 , pp. 1117-1129
    • Alushin, G.M.1    Lander, G.C.2    Kellogg, E.H.3    Zhang, R.4    Baker, D.5    Nogales, E.6
  • 2
    • 0016367327 scopus 로고
    • Arrangement of subunits in flagellar microtubules
    • L. Amos, and A. Klug Arrangement of subunits in flagellar microtubules J. Cell Sci. 14 1974 523 549
    • (1974) J. Cell Sci. , vol.14 , pp. 523-549
    • Amos, L.1    Klug, A.2
  • 3
    • 0033102385 scopus 로고    scopus 로고
    • How Taxol stabilises microtubule structure
    • L.A. Amos, and J. Löwe How Taxol stabilises microtubule structure Chem. Biol. 6 1999 R65 R69
    • (1999) Chem. Biol. , vol.6 , pp. R65-R69
    • Amos, L.A.1    Löwe, J.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 58149291884 scopus 로고    scopus 로고
    • Molecular architecture of inner dynein arms in situ in Chlamydomonas reinhardtii flagella
    • K.H. Bui, H. Sakakibara, T. Movassagh, K. Oiwa, and T. Ishikawa Molecular architecture of inner dynein arms in situ in Chlamydomonas reinhardtii flagella J. Cell Biol. 183 2008 923 932
    • (2008) J. Cell Biol. , vol.183 , pp. 923-932
    • Bui, K.H.1    Sakakibara, H.2    Movassagh, T.3    Oiwa, K.4    Ishikawa, T.5
  • 6
    • 68549128833 scopus 로고    scopus 로고
    • Asymmetry of inner dynein arms and inter-doublet links in Chlamydomonas flagella
    • K.H. Bui, H. Sakakibara, T. Movassagh, K. Oiwa, and T. Ishikawa Asymmetry of inner dynein arms and inter-doublet links in Chlamydomonas flagella J. Cell Biol. 186 2009 437 446
    • (2009) J. Cell Biol. , vol.186 , pp. 437-446
    • Bui, K.H.1    Sakakibara, H.2    Movassagh, T.3    Oiwa, K.4    Ishikawa, T.5
  • 7
    • 84866371836 scopus 로고    scopus 로고
    • Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme
    • K.H. Bui, T. Yagi, R. Yamamoto, R. Kamiya, and T. Ishikawa Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme J. Cell Biol. 198 2012 913 925
    • (2012) J. Cell Biol. , vol.198 , pp. 913-925
    • Bui, K.H.1    Yagi, T.2    Yamamoto, R.3    Kamiya, R.4    Ishikawa, T.5
  • 8
    • 58149098730 scopus 로고    scopus 로고
    • ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement
    • J.C. Cochran, C.V. Sindelar, N.K. Mulko, K.A. Collins, S.E. Kong, R.S. Hawley, and F.J. Kull ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement Cell 136 2009 110 122
    • (2009) Cell , vol.136 , pp. 110-122
    • Cochran, J.C.1    Sindelar, C.V.2    Mulko, N.K.3    Collins, K.A.4    Kong, S.E.5    Hawley, R.S.6    Kull, F.J.7
  • 9
    • 0033372028 scopus 로고    scopus 로고
    • Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution
    • J.F. Conway, and A.C. Steven Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution J. Struct. Biol. 128 1999 106 118
    • (1999) J. Struct. Biol. , vol.128 , pp. 106-118
    • Conway, J.F.1    Steven, A.C.2
  • 10
    • 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
  • 11
    • 0022345812 scopus 로고
    • Outer and inner dynein arms of cilia and flagella
    • U.W. Goodenough, and J.E. Heuser Outer and inner dynein arms of cilia and flagella Cell 41 1985 341 342
    • (1985) Cell , vol.41 , pp. 341-342
    • Goodenough, U.W.1    Heuser, J.E.2
  • 12
    • 0021889149 scopus 로고
    • Substructure of inner dynein arms, radial spokes, and the central pair/projection complex of cilia and flagella
    • U.W. Goodenough, and J.E. Heuser Substructure of inner dynein arms, radial spokes, and the central pair/projection complex of cilia and flagella J. Cell Biol. 100 1985 2008 2018
    • (1985) J. Cell Biol. , vol.100 , pp. 2008-2018
    • Goodenough, U.W.1    Heuser, J.E.2
  • 13
    • 74049111826 scopus 로고    scopus 로고
    • The dynein regulatory complex is the nexin link and a major regulatory node in cilia and flagella
    • T. Heuser, M. Raytchev, J. Krell, M.E. Porter, and D. Nicastro The dynein regulatory complex is the nexin link and a major regulatory node in cilia and flagella J. Cell Biol. 187 2009 921 933
    • (2009) J. Cell Biol. , vol.187 , pp. 921-933
    • Heuser, T.1    Raytchev, M.2    Krell, J.3    Porter, M.E.4    Nicastro, D.5
  • 15
    • 0028597558 scopus 로고
    • Direct visualization of the microtubule lattice seam both in vitro and in vivo
    • M. Kikkawa, T. Ishikawa, T. Nakata, T. Wakabayashi, and N. Hirokawa Direct visualization of the microtubule lattice seam both in vitro and in vivo J. Cell Biol. 127 1994 1965 1971
    • (1994) J. Cell Biol. , vol.127 , pp. 1965-1971
    • Kikkawa, M.1    Ishikawa, T.2    Nakata, T.3    Wakabayashi, T.4    Hirokawa, N.5
  • 17
    • 84857426309 scopus 로고    scopus 로고
    • Ciliary and flagellar structure and function - Their regulations by posttranslational modifications of axonemal tubulin
    • A. Konno, M. Setou, and K. Ikegami Ciliary and flagellar structure and function - their regulations by posttranslational modifications of axonemal tubulin Int. Rev. Cell Mol. Biol. 294 2012 133 170
    • (2012) Int. Rev. Cell Mol. Biol. , vol.294 , pp. 133-170
    • Konno, A.1    Setou, M.2    Ikegami, K.3
  • 18
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • J.R. Kremer, D.N. Mastronarde, and J.R. McIntosh Computer visualization of three-dimensional image data using IMOD J. Struct. Biol. 116 1996 71 76
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 19
    • 34247558998 scopus 로고    scopus 로고
    • Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules
    • R.W. Linck, and R.E. Stephens Functional protofilament numbering of ciliary, flagellar, and centriolar microtubules Cell Motil. Cytoskeleton 64 2007 489 495
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 489-495
    • Linck, R.W.1    Stephens, R.E.2
  • 21
    • 84864390209 scopus 로고    scopus 로고
    • Heterogeneity of dynein structure implies coordinated suppression of dynein motor activity in the axoneme
    • A. Maheshwari, and T. Ishikawa Heterogeneity of dynein structure implies coordinated suppression of dynein motor activity in the axoneme J. Struct. Biol. 179 2012 235 241
    • (2012) J. Struct. Biol. , vol.179 , pp. 235-241
    • Maheshwari, A.1    Ishikawa, T.2
  • 22
    • 84859736946 scopus 로고    scopus 로고
    • EBs recognize a nucleotide-dependent structural cap at growing microtubule ends
    • S.P. Maurer, F.J. Fourniol, G. Bohner, C.A. Moores, and T. Surrey EBs recognize a nucleotide-dependent structural cap at growing microtubule ends Cell 149 2012 371 382
    • (2012) Cell , vol.149 , pp. 371-382
    • Maurer, S.P.1    Fourniol, F.J.2    Bohner, G.3    Moores, C.A.4    Surrey, T.5
  • 23
    • 38049098127 scopus 로고    scopus 로고
    • Three-dimensional structure of cytoplasmic dynein bound to microtubules
    • N. Mizuno, A. Narita, T. Kon, K. Sutoh, and M. Kikkawa Three-dimensional structure of cytoplasmic dynein bound to microtubules Proc. Natl. Acad. Sci. USA 104 2007 20832 20837
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20832-20837
    • Mizuno, N.1    Narita, A.2    Kon, T.3    Sutoh, K.4    Kikkawa, M.5
  • 24
    • 77953259866 scopus 로고    scopus 로고
    • Nucleotide-induced global conformational changes of flagellar dynein arms revealed by in situ analysis
    • T. Movassagh, K.H. Bui, H. Sakakibara, K. Oiwa, and T. Ishikawa Nucleotide-induced global conformational changes of flagellar dynein arms revealed by in situ analysis Nat. Struct. Mol. Biol. 17 2010 761 767
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 761-767
    • Movassagh, T.1    Bui, K.H.2    Sakakibara, H.3    Oiwa, K.4    Ishikawa, T.5
  • 26
    • 80054795016 scopus 로고    scopus 로고
    • Cryo-electron tomography reveals conserved features of doublet microtubules in flagella
    • D. Nicastro, X. Fu, T. Heuser, A. Tso, M.E. Porter, and R.W. Linck Cryo-electron tomography reveals conserved features of doublet microtubules in flagella Proc. Natl. Acad. Sci. USA 108 2011 E845 E853
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. E845-E853
    • Nicastro, D.1    Fu, X.2    Heuser, T.3    Tso, A.4    Porter, M.E.5    Linck, R.W.6
  • 27
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • E. Nogales, S.G. Wolf, and K.H. Downing Structure of the alpha beta tubulin dimer by electron crystallography Nature 391 1998 199 203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 28
    • 0033988376 scopus 로고    scopus 로고
    • Tetrahymena as a laboratory organism: Useful strains, cell culture, and cell line maintenance
    • E. Orias, E.P. Hamilton, and J.D. Orias Tetrahymena as a laboratory organism: useful strains, cell culture, and cell line maintenance Methods Cell Biol. 62 2000 189 211
    • (2000) Methods Cell Biol. , vol.62 , pp. 189-211
    • Orias, E.1    Hamilton, E.P.2    Orias, J.D.3
  • 32
    • 84860570233 scopus 로고    scopus 로고
    • Comparative structural analysis of eukaryotic flagella and cilia from Chlamydomonas, Tetrahymena, and sea urchins
    • G. Pigino, A. Maheshwari, K.H. Bui, C. Shingyoji, S. Kamimura, and T. Ishikawa Comparative structural analysis of eukaryotic flagella and cilia from Chlamydomonas, Tetrahymena, and sea urchins J. Struct. Biol. 178 2012 199 206
    • (2012) J. Struct. Biol. , vol.178 , pp. 199-206
    • Pigino, G.1    Maheshwari, A.2    Bui, K.H.3    Shingyoji, C.4    Kamimura, S.5    Ishikawa, T.6
  • 33
    • 0030027155 scopus 로고    scopus 로고
    • Axonemal dyneins: Assembly, organization, and regulation
    • M.E. Porter Axonemal dyneins: assembly, organization, and regulation Curr. Opin. Cell Biol. 8 1996 10 17
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 10-17
    • Porter, M.E.1
  • 36
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • P.B. Rosenthal, and R. Henderson Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy J. Mol. Biol. 333 2003 721 745
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 37
    • 77749239756 scopus 로고    scopus 로고
    • An atomic-level mechanism for activation of the kinesin molecular motors
    • C.V. Sindelar, and K.H. Downing An atomic-level mechanism for activation of the kinesin molecular motors Proc. Natl. Acad. Sci. USA 107 2010 4111 4116
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 4111-4116
    • Sindelar, C.V.1    Downing, K.H.2
  • 38
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice
    • Y.H. Song, and E. Mandelkow Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice Proc. Natl. Acad. Sci. USA 90 1993 1671 1675
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1671-1675
    • Song, Y.H.1    Mandelkow, E.2
  • 39
    • 0028854634 scopus 로고
    • The anatomy of flagellar microtubules: Polarity, seam, junctions, and lattice
    • Y.H. Song, and E. Mandelkow The anatomy of flagellar microtubules: polarity, seam, junctions, and lattice J. Cell Biol. 128 1995 81 94
    • (1995) J. Cell Biol. , vol.128 , pp. 81-94
    • Song, Y.H.1    Mandelkow, E.2
  • 40
    • 33747088253 scopus 로고    scopus 로고
    • Molecular architecture of axonemal microtubule doublets revealed by cryo-electron tomography
    • H. Sui, and K.H. Downing Molecular architecture of axonemal microtubule doublets revealed by cryo-electron tomography Nature 442 2006 475 478
    • (2006) Nature , vol.442 , pp. 475-478
    • Sui, H.1    Downing, K.H.2
  • 41
    • 0022962478 scopus 로고
    • Isolation of Chlamydomonas flagella and flagellar axonemes
    • G.B. Witman Isolation of Chlamydomonas flagella and flagellar axonemes Methods Enzymol. 134 1986 280 290
    • (1986) Methods Enzymol. , vol.134 , pp. 280-290
    • Witman, G.B.1
  • 42
    • 84899670189 scopus 로고    scopus 로고
    • FAP20 is an inner junction protein of doublet microtubules essential for both the planar asymmetrical waveform and stability of flagella in Chlamydomonas
    • H. Yanagisawa, G. Mathis, T. Oda, M. Hirono, E.A. Richey, H. Ishikawa, W.F. Marshall, M. Kikkawa, and H. Qin FAP20 is an inner junction protein of doublet microtubules essential for both the planar asymmetrical waveform and stability of flagella in Chlamydomonas Mol. Biol. Cell 25 2014 1472 1483
    • (2014) Mol. Biol. Cell , vol.25 , pp. 1472-1483
    • Yanagisawa, H.1    Mathis, G.2    Oda, T.3    Hirono, M.4    Richey, E.A.5    Ishikawa, H.6    Marshall, W.F.7    Kikkawa, M.8    Qin, H.9


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