메뉴 건너뛰기




Volumn 104, Issue 9, 2013, Pages 1989-1998

Displacement-weighted velocity analysis of gliding assays reveals that Chlamydomonas axonemal dynein preferentially moves conspecific microtubules

Author keywords

[No Author keywords available]

Indexed keywords

AXONEMAL DYNEIN; TUBULIN;

EID: 84877251139     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.03.041     Document Type: Article
Times cited : (17)

References (52)
  • 1
    • 84856710211 scopus 로고    scopus 로고
    • Dynein achieves processive motion using both stochastic and coordinated stepping
    • W. Qiu, and N.D. Derr S.L. Reck-Peterson Dynein achieves processive motion using both stochastic and coordinated stepping Nat. Struct. Mol. Biol. 19 2012 193 200
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 193-200
    • Qiu, W.1    Derr, N.D.2    Reck-Peterson, S.L.3
  • 2
    • 84855828496 scopus 로고    scopus 로고
    • Cytoplasmic dynein moves through uncoordinated stepping of the AAA+ ring domains
    • M.A. DeWitt, and A.Y. Chang 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    Yildiz, A.3
  • 3
    • 0028362896 scopus 로고
    • Force and velocity measured for single kinesin molecules
    • K. Svoboda, and S.M. Block Force and velocity measured for single kinesin molecules Cell 77 1994 773 784
    • (1994) Cell , vol.77 , pp. 773-784
    • Svoboda, K.1    Block, S.M.2
  • 4
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • S.J. Kron, and J.A. Spudich Fluorescent actin filaments move on myosin fixed to a glass surface Proc. Natl. Acad. Sci. USA 83 1986 6272 6276
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 5
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • R.D. Vale, T.S. Reese, and M.P. Sheetz Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility Cell 42 1985 39 50
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 6
    • 0024463944 scopus 로고
    • Movement of microtubules by single kinesin molecules
    • J. Howard, A.J. Hudspeth, and R.D. Vale Movement of microtubules by single kinesin molecules Nature 342 1989 154 158
    • (1989) Nature , vol.342 , pp. 154-158
    • Howard, J.1    Hudspeth, A.J.2    Vale, R.D.3
  • 8
    • 34547477550 scopus 로고    scopus 로고
    • Detection of fractional steps in cargo movement by the collective operation of kinesin-1 motors
    • C. Leduc, and F. Ruhnow S. Diez Detection of fractional steps in cargo movement by the collective operation of kinesin-1 motors Proc. Natl. Acad. Sci. USA 104 2007 10847 10852
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10847-10852
    • Leduc, C.1    Ruhnow, F.2    Diez, S.3
  • 9
    • 0028113846 scopus 로고
    • Fluctuation analysis of motor protein movement and single enzyme kinetics
    • K. Svoboda, P.P. Mitra, and S.M. Block Fluctuation analysis of motor protein movement and single enzyme kinetics Proc. Natl. Acad. Sci. USA 91 1994 11782 11786
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11782-11786
    • Svoboda, K.1    Mitra, P.P.2    Block, S.M.3
  • 10
    • 0028876063 scopus 로고
    • Mechanochemical aspects of axonemal dynein activity studied by in vitro microtubule translocation
    • T. Hamasaki, and M.E. Holwill P. Satir Mechanochemical aspects of axonemal dynein activity studied by in vitro microtubule translocation Biophys. J. 69 1995 2569 2579
    • (1995) Biophys. J. , vol.69 , pp. 2569-2579
    • Hamasaki, T.1    Holwill, M.E.2    Satir, P.3
  • 11
    • 65549157059 scopus 로고    scopus 로고
    • Systematic comparison of in vitro motile properties between Chlamydomonas wild-type and mutant outer arm dyneins each lacking one of the three heavy chains
    • A. Furuta, and T. Yagi R. Kamiya Systematic comparison of in vitro motile properties between Chlamydomonas wild-type and mutant outer arm dyneins each lacking one of the three heavy chains J. Biol. Chem. 284 2009 5927 5935
    • (2009) J. Biol. Chem. , vol.284 , pp. 5927-5935
    • Furuta, A.1    Yagi, T.2    Kamiya, R.3
  • 12
    • 0023009146 scopus 로고
    • Microtubule sliding in mutant Chlamydomonas axonemes devoid of outer or inner dynein arms
    • T. Okagaki, and R. Kamiya Microtubule sliding in mutant Chlamydomonas axonemes devoid of outer or inner dynein arms J. Cell Biol. 103 1986 1895 1902
    • (1986) J. Cell Biol. , vol.103 , pp. 1895-1902
    • Okagaki, T.1    Kamiya, R.2
  • 13
    • 10344257251 scopus 로고    scopus 로고
    • Effects of imposed bending on microtubule sliding in sperm flagella
    • Y. Morita, and C. Shingyoji Effects of imposed bending on microtubule sliding in sperm flagella Curr. Biol. 14 2004 2113 2118
    • (2004) Curr. Biol. , vol.14 , pp. 2113-2118
    • Morita, Y.1    Shingyoji, C.2
  • 14
    • 34547666969 scopus 로고    scopus 로고
    • Mechanical properties of inner-arm dynein-f (dynein I1) studied with in vitro motility assays
    • N. Kotani, and H. Sakakibara K. Oiwa Mechanical properties of inner-arm dynein-f (dynein I1) studied with in vitro motility assays Biophys. J. 93 2007 886 894
    • (2007) Biophys. J. , vol.93 , pp. 886-894
    • Kotani, N.1    Sakakibara, H.2    Oiwa, K.3
  • 15
    • 1842781701 scopus 로고    scopus 로고
    • Slow ADP-dependent acceleration of microtubule translocation produced by an axonemal dynein
    • K. Kikushima, T. Yagi, and R. Kamiya Slow ADP-dependent acceleration of microtubule translocation produced by an axonemal dynein FEBS Lett. 563 2004 119 122
    • (2004) FEBS Lett. , vol.563 , pp. 119-122
    • Kikushima, K.1    Yagi, T.2    Kamiya, R.3
  • 16
    • 0034533181 scopus 로고    scopus 로고
    • ADP-dependent microtubule translocation by flagellar inner-arm dyneins
    • T. Yagi ADP-dependent microtubule translocation by flagellar inner-arm dyneins Cell Struct. Funct. 25 2000 263 267
    • (2000) Cell Struct. Funct. , vol.25 , pp. 263-267
    • Yagi, T.1
  • 17
    • 34748899672 scopus 로고    scopus 로고
    • The roles of noncatalytic ATP binding and ADP binding in the regulation of dynein motile activity in flagella
    • Y. Inoue, and C. Shingyoji The roles of noncatalytic ATP binding and ADP binding in the regulation of dynein motile activity in flagella Cell Motil. Cytoskeleton 64 2007 690 704
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 690-704
    • Inoue, Y.1    Shingyoji, C.2
  • 18
    • 0031801655 scopus 로고    scopus 로고
    • Translocation of microtubules caused by the αβ, β and γ outer arm dynein subparticles of Chlamydomonas
    • H. Sakakibara, and H. Nakayama Translocation of microtubules caused by the αβ, β and γ outer arm dynein subparticles of Chlamydomonas J. Cell Sci. 111 1998 1155 1164
    • (1998) J. Cell Sci. , vol.111 , pp. 1155-1164
    • Sakakibara, H.1    Nakayama, H.2
  • 19
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: Different gene products and covalent modifications
    • R.F. Ludueña Multiple forms of tubulin: different gene products and covalent modifications Int. Rev. Cytol. 178 1998 207 275
    • (1998) Int. Rev. Cytol. , vol.178 , pp. 207-275
    • Ludueña, R.F.1
  • 20
    • 81855196008 scopus 로고    scopus 로고
    • Post-translational regulation of the microtubule cytoskeleton: Mechanisms and functions
    • C. Janke, and J.C. Bulinski Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions Nat. Rev. Mol. Cell Biol. 12 2011 773 786
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 773-786
    • Janke, C.1    Bulinski, J.C.2
  • 21
    • 27644448463 scopus 로고    scopus 로고
    • Direct involvement of the isotype-specific C-terminus of β tubulin in ciliary beating
    • J. Vent, and T.A. Wyatt R. Hallworth Direct involvement of the isotype-specific C-terminus of β tubulin in ciliary beating J. Cell Sci. 118 2005 4333 4341
    • (2005) J. Cell Sci. , vol.118 , pp. 4333-4341
    • Vent, J.1    Wyatt, T.A.2    Hallworth, R.3
  • 22
    • 79960918056 scopus 로고    scopus 로고
    • Purification of tubulin from porcine brain
    • C. Gell, and C.T. Friel J. Howard Purification of tubulin from porcine brain Methods Mol. Biol. 777 2011 15 28
    • (2011) Methods Mol. Biol. , vol.777 , pp. 15-28
    • Gell, C.1    Friel, C.T.2    Howard, J.3
  • 23
    • 84869224914 scopus 로고    scopus 로고
    • One-step purification of assembly-competent tubulin from diverse eukaryotic sources
    • P.O. Widlund, and M. Podolski D.N. Drechsel One-step purification of assembly-competent tubulin from diverse eukaryotic sources Mol. Biol. Cell 23 2012 4393 4401
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4393-4401
    • Widlund, P.O.1    Podolski, M.2    Drechsel, D.N.3
  • 24
    • 0035957923 scopus 로고    scopus 로고
    • The Tctex1/Tctex2 class of dynein light chains. Dimerization, differential expression, and interaction with the LC8 protein family
    • L.M. DiBella, and S.E. Benashski S.M. King The Tctex1/Tctex2 class of dynein light chains. Dimerization, differential expression, and interaction with the LC8 protein family J. Biol. Chem. 276 2001 14366 14373
    • (2001) J. Biol. Chem. , vol.276 , pp. 14366-14373
    • Dibella, L.M.1    Benashski, S.E.2    King, S.M.3
  • 25
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: Their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi
    • D.S. Gorman, and R.P. Levine Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi Proc. Natl. Acad. Sci. USA 54 1965 1665 1669
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 26
    • 0022962478 scopus 로고
    • Isolation of Chlamydomonas flagella and flagellar axonemes
    • G. Witman, and R. Vallee Isolation of Chlamydomonas flagella and flagellar axonemes Methods Enzymol. 134 1986 280 290
    • (1986) Methods Enzymol. , vol.134 , pp. 280-290
    • Witman, G.1    Vallee, R.2
  • 27
    • 0027097082 scopus 로고
    • Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein
    • O. Kagami, and R. Kamiya Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein J. Cell Sci. 103 1992 653 664
    • (1992) J. Cell Sci. , vol.103 , pp. 653-664
    • Kagami, O.1    Kamiya, R.2
  • 28
    • 79960315009 scopus 로고    scopus 로고
    • Tracking single particles and elongated filaments with nanometer precision
    • F. Ruhnow, D. Zwicker, and S. Diez Tracking single particles and elongated filaments with nanometer precision Biophys. J. 100 2011 2820 2828
    • (2011) Biophys. J. , vol.100 , pp. 2820-2828
    • Ruhnow, F.1    Zwicker, D.2    Diez, S.3
  • 29
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • A. Savitzky, and M.J.E. Golay Smoothing and differentiation of data by simplified least squares procedures Anal. Chem. 36 1964 1627 1639
    • (1964) Anal. Chem. , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 30
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • T.Q.P. Uyeda, S.J. Kron, and J.A. Spudich Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin J. Mol. Biol. 214 1990 699 710
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 31
    • 0022525167 scopus 로고
    • Activation of the dynein adenosinetriphosphatase by microtubules
    • C.K. Omoto, and K.A. Johnson Activation of the dynein adenosinetriphosphatase by microtubules Biochemistry 25 1986 419 427
    • (1986) Biochemistry , vol.25 , pp. 419-427
    • Omoto, C.K.1    Johnson, K.A.2
  • 32
    • 12844266000 scopus 로고    scopus 로고
    • High speed sliding of axonemal microtubules produced by outer arm dynein
    • R.N. Seetharam, and P. Satir High speed sliding of axonemal microtubules produced by outer arm dynein Cell Motil. Cytoskeleton 60 2005 96 103
    • (2005) Cell Motil. Cytoskeleton , vol.60 , pp. 96-103
    • Seetharam, R.N.1    Satir, P.2
  • 33
    • 0035799299 scopus 로고    scopus 로고
    • Axoneme-specific β-tubulin specialization: A conserved C-terminal motif specifies the central pair
    • M.G. Nielsen, and F.R. Turner E.C. Raff Axoneme-specific β-tubulin specialization: a conserved C-terminal motif specifies the central pair Curr. Biol. 11 2001 529 533
    • (2001) Curr. Biol. , vol.11 , pp. 529-533
    • Nielsen, M.G.1    Turner, F.R.2    Raff, E.C.3
  • 34
    • 0024306241 scopus 로고
    • Interaction of brain cytoplasmic dynein and MAP2 with a common sequence at the C terminus of tubulin
    • B.M. Paschal, R.A. Obar, and R.B. Vallee Interaction of brain cytoplasmic dynein and MAP2 with a common sequence at the C terminus of tubulin Nature 342 1989 569 572
    • (1989) Nature , vol.342 , pp. 569-572
    • Paschal, B.M.1    Obar, R.A.2    Vallee, R.B.3
  • 35
    • 82455219434 scopus 로고    scopus 로고
    • Electrostatically biased binding of kinesin to microtubules
    • B.J. Grant, and D.M. Gheorghe R.A. Cross Electrostatically biased binding of kinesin to microtubules PLoS Biol. 9 2011 e1001207
    • (2011) PLoS Biol. , vol.9 , pp. 1001207
    • Grant, B.J.1    Gheorghe, D.M.2    Cross, R.A.3
  • 36
    • 77649098302 scopus 로고    scopus 로고
    • Tubulin polyglutamylation regulates axonemal motility by modulating activities of inner-arm dyneins
    • T. Kubo, and H.A. Yanagisawa R. Kamiya Tubulin polyglutamylation regulates axonemal motility by modulating activities of inner-arm dyneins Curr. Biol. 20 2010 441 445
    • (2010) Curr. Biol. , vol.20 , pp. 441-445
    • Kubo, T.1    Yanagisawa, H.A.2    Kamiya, R.3
  • 37
    • 84871172900 scopus 로고    scopus 로고
    • Tubulin polyglutamylation regulates flagellar motility by controlling a specific inner-arm dynein that interacts with the dynein regulatory complex
    • T. Kubo, T. Yagi, and R. Kamiya Tubulin polyglutamylation regulates flagellar motility by controlling a specific inner-arm dynein that interacts with the dynein regulatory complex Cytoskeleton (Hoboken) 69 2012 1059 1068
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 1059-1068
    • Kubo, T.1    Yagi, T.2    Kamiya, R.3
  • 38
    • 77649172810 scopus 로고    scopus 로고
    • Tubulin glutamylation regulates ciliary motility by altering inner dynein arm activity
    • S. Suryavanshi, and B. Eddé J. Gaertig Tubulin glutamylation regulates ciliary motility by altering inner dynein arm activity Curr. Biol. 20 2010 435 440
    • (2010) Curr. Biol. , vol.20 , pp. 435-440
    • Suryavanshi, S.1    Eddé, B.2    Gaertig, J.3
  • 39
    • 0031905985 scopus 로고    scopus 로고
    • The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content
    • K.A. Johnson The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content J. Cell Sci. 111 1998 313 320
    • (1998) J. Cell Sci. , vol.111 , pp. 313-320
    • Johnson, K.A.1
  • 40
    • 73349125122 scopus 로고    scopus 로고
    • Tug-of-war between dissimilar teams of microtubule motors regulates transport and fission of endosomes
    • V. Soppina, and A.K. Rai R. Mallik Tug-of-war between dissimilar teams of microtubule motors regulates transport and fission of endosomes Proc. Natl. Acad. Sci. USA 106 2009 19381 19386
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19381-19386
    • Soppina, V.1    Rai, A.K.2    Mallik, R.3
  • 41
    • 84863740946 scopus 로고    scopus 로고
    • Lis1 is an initiation factor for dynein-driven organelle transport
    • M.J. Egan, K. Tan, and S.L. Reck-Peterson Lis1 is an initiation factor for dynein-driven organelle transport J. Cell Biol. 197 2012 971 982
    • (2012) J. Cell Biol. , vol.197 , pp. 971-982
    • Egan, M.J.1    Tan, K.2    Reck-Peterson, S.L.3
  • 42
    • 84859933274 scopus 로고    scopus 로고
    • Molecular crowding creates traffic jams of kinesin motors on microtubules
    • C. Leduc, and K. Padberg-Gehle J. Howard Molecular crowding creates traffic jams of kinesin motors on microtubules Proc. Natl. Acad. Sci. USA 109 2012 6100 6105
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6100-6105
    • Leduc, C.1    Padberg-Gehle, K.2    Howard, J.3
  • 43
    • 51549097934 scopus 로고    scopus 로고
    • Intramolecular strain coordinates kinesin stepping behavior along microtubules
    • A. Yildiz, and M. Tomishige R.D. Vale Intramolecular strain coordinates kinesin stepping behavior along microtubules Cell 134 2008 1030 1041
    • (2008) Cell , vol.134 , pp. 1030-1041
    • Yildiz, A.1    Tomishige, M.2    Vale, R.D.3
  • 44
    • 34147206187 scopus 로고    scopus 로고
    • Backtracking determines the force sensitivity of RNAP II in a factor-dependent manner
    • E.A. Galburt, and S.W. Grill C. Bustamante Backtracking determines the force sensitivity of RNAP II in a factor-dependent manner Nature 446 2007 820 823
    • (2007) Nature , vol.446 , pp. 820-823
    • Galburt, E.A.1    Grill, S.W.2    Bustamante, C.3
  • 45
    • 0345047725 scopus 로고    scopus 로고
    • Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking
    • K.C. Neuman, and E.A. Abbondanzieri S.M. Block Ubiquitous transcriptional pausing is independent of RNA polymerase backtracking Cell 115 2003 437 447
    • (2003) Cell , vol.115 , pp. 437-447
    • Neuman, K.C.1    Abbondanzieri, E.A.2    Block, S.M.3
  • 46
    • 79952670230 scopus 로고    scopus 로고
    • Analysis and modelling of swimming behaviour in Oxyrrhis marina
    • D.E. Boakes, and E.A. Codling M. Steinke Analysis and modelling of swimming behaviour in Oxyrrhis marina J. Plankton Res. 33 2011 641 649
    • (2011) J. Plankton Res. , vol.33 , pp. 641-649
    • Boakes, D.E.1    Codling, E.A.2    Steinke, M.3
  • 47
    • 0033771415 scopus 로고    scopus 로고
    • Effects of light on gravitaxis and velocity in Chlamydomonas reinhardtii
    • O. Sineshchekov, M. Lebert, and D.-P. Häder Effects of light on gravitaxis and velocity in Chlamydomonas reinhardtii J. Plant Physiol. 157 2000 247 254
    • (2000) J. Plant Physiol. , vol.157 , pp. 247-254
    • Sineshchekov, O.1    Lebert, M.2    Häder, D.-P.3
  • 48
    • 59349109969 scopus 로고    scopus 로고
    • How to track protists in three dimensions
    • 014301-014307
    • K. Drescher, K.C. Leptos, and R.E. Goldstein How to track protists in three dimensions Rev. Sci. Instrum. 80 2009 014301 014301-014307
    • (2009) Rev. Sci. Instrum. , vol.80 , pp. 014301
    • Drescher, K.1    Leptos, K.C.2    Goldstein, R.E.3
  • 49
    • 84862643429 scopus 로고    scopus 로고
    • Mismatch in mechanical and adhesive properties induces pulsating cancer cell migration in epithelial monolayer
    • M.-H. Lee, and P.-H. Wu D. Wirtz Mismatch in mechanical and adhesive properties induces pulsating cancer cell migration in epithelial monolayer Biophys. J. 102 2012 2731 2741
    • (2012) Biophys. J. , vol.102 , pp. 2731-2741
    • Lee, M.-H.1    Wu, P.-H.2    Wirtz, D.3
  • 50
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • A. Shevchenko, and H. Tomas M. Mann In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat. Protoc. 1 2006 2856 2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Mann, M.3
  • 51
    • 53049085543 scopus 로고    scopus 로고
    • Separating the wheat from the chaff: Unbiased filtering of background tandem mass spectra improves protein identification
    • M. Junqueira, and V. Spirin A. Shevchenko Separating the wheat from the chaff: unbiased filtering of background tandem mass spectra improves protein identification J. Proteome Res. 7 2008 3382 3395
    • (2008) J. Proteome Res. , vol.7 , pp. 3382-3395
    • Junqueira, M.1    Spirin, V.2    Shevchenko, A.3
  • 52
    • 0028005499 scopus 로고
    • ATP-induced sliding of microtubules on tracks of 22S dynein molecules aligned with the same polarity
    • Y. Mimori, and T. Miki-Nomura ATP-induced sliding of microtubules on tracks of 22S dynein molecules aligned with the same polarity Cell Motil. Cytoskeleton 27 1994 180 191
    • (1994) Cell Motil. Cytoskeleton , vol.27 , pp. 180-191
    • Mimori, Y.1    Miki-Nomura, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.