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Volumn 17, Issue 2, 2007, Pages 253-259

Structural insights into microtubule doublet interactions in axonemes

Author keywords

[No Author keywords available]

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 34147096000     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.03.013     Document Type: Review
Times cited : (27)

References (43)
  • 1
    • 0019781934 scopus 로고
    • Cilia and flagella of eukaryotes
    • Gibbons I.R. Cilia and flagella of eukaryotes. J Cell Biol 91 (1981) 107s-124s
    • (1981) J Cell Biol , vol.91
    • Gibbons, I.R.1
  • 2
    • 0033849936 scopus 로고    scopus 로고
    • Chlamydomonas flagella
    • Mitchell D.R. Chlamydomonas flagella. J Phycol 36 (2000) 261-273
    • (2000) J Phycol , vol.36 , pp. 261-273
    • Mitchell, D.R.1
  • 3
    • 0034722338 scopus 로고    scopus 로고
    • The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility
    • Porter M.E., and Sale W.S. The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility. J Cell Biol 151 (2000) F37-F42
    • (2000) J Cell Biol , vol.151
    • Porter, M.E.1    Sale, W.S.2
  • 4
    • 0347604867 scopus 로고    scopus 로고
    • Molecular architecture of the sperm flagella: molecules for motility and signaling
    • Inaba K. Molecular architecture of the sperm flagella: molecules for motility and signaling. Zoolog Sci 20 (2003) 1043-1056
    • (2003) Zoolog Sci , vol.20 , pp. 1043-1056
    • Inaba, K.1
  • 5
    • 0026673055 scopus 로고
    • The inner dynein arms I2 interact with a "dynein regulatory complex" in Chlamydomonas flagella
    • Piperno G., Mead K., and Shestak W. The inner dynein arms I2 interact with a "dynein regulatory complex" in Chlamydomonas flagella. J Cell Biol 118 (1992) 1455-1463
    • (1992) J Cell Biol , vol.118 , pp. 1455-1463
    • Piperno, G.1    Mead, K.2    Shestak, W.3
  • 6
    • 0028176103 scopus 로고
    • Mutations in the "dynein regulatory complex" alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes
    • Piperno G., Mead K., LeDizet M., and Moscatelli A. Mutations in the "dynein regulatory complex" alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes. J Cell Biol 125 (1994) 1109-1117
    • (1994) J Cell Biol , vol.125 , pp. 1109-1117
    • Piperno, G.1    Mead, K.2    LeDizet, M.3    Moscatelli, A.4
  • 7
    • 0028170976 scopus 로고
    • Components of a "dynein regulatory complex" are located at the junction between the radial spokes and the dynein arms in Chlamydomonas flagella
    • Gardner L.C., O'Toole E., Perrone C.A., Giddings T., and Porter M.E. Components of a "dynein regulatory complex" are located at the junction between the radial spokes and the dynein arms in Chlamydomonas flagella. J Cell Biol 127 (1994) 1311-1325
    • (1994) J Cell Biol , vol.127 , pp. 1311-1325
    • Gardner, L.C.1    O'Toole, E.2    Perrone, C.A.3    Giddings, T.4    Porter, M.E.5
  • 8
    • 0031018910 scopus 로고    scopus 로고
    • Studies on the eel sperm flagellum. I. The structure of the inner dynein arm complex
    • Woolley D.M. Studies on the eel sperm flagellum. I. The structure of the inner dynein arm complex. J Cell Sci 110 (1997) 85-94
    • (1997) J Cell Sci , vol.110 , pp. 85-94
    • Woolley, D.M.1
  • 9
    • 0346732099 scopus 로고    scopus 로고
    • The radial spokes and central apparatus: mechano-chemical transducers that regulate flagellar motility
    • Smith E.F., and Yang P. The radial spokes and central apparatus: mechano-chemical transducers that regulate flagellar motility. Cell Motil Cytoskeleton 57 (2004) 8-17
    • (2004) Cell Motil Cytoskeleton , vol.57 , pp. 8-17
    • Smith, E.F.1    Yang, P.2
  • 10
    • 4444224020 scopus 로고    scopus 로고
    • Bend propagation drives central pair rotation in Chlamydomonas reinhardtii flagella
    • Mitchell D.R., and Nakatsugawa M. Bend propagation drives central pair rotation in Chlamydomonas reinhardtii flagella. J Cell Biol 166 (2004) 709-715
    • (2004) J Cell Biol , vol.166 , pp. 709-715
    • Mitchell, D.R.1    Nakatsugawa, M.2
  • 11
    • 33746092106 scopus 로고    scopus 로고
    • Basal body and flagellum mutants reveal a rotational constraint of the central pair microtubules in the axonemes of trypanosomes
    • Gadelha C., Wickstead B., McKean P.G., and Gull K. Basal body and flagellum mutants reveal a rotational constraint of the central pair microtubules in the axonemes of trypanosomes. J Cell Sci 119 (2006) 2405-2413
    • (2006) J Cell Sci , vol.119 , pp. 2405-2413
    • Gadelha, C.1    Wickstead, B.2    McKean, P.G.3    Gull, K.4
  • 12
    • 0021779571 scopus 로고
    • Live and reactivated motility in the 9+0 flagellum of Anguilla sperm
    • Gibbons B.H., Baccetti B., and Gibbons I.R. Live and reactivated motility in the 9+0 flagellum of Anguilla sperm. Cell Motil 5 (1985) 333-350
    • (1985) Cell Motil , vol.5 , pp. 333-350
    • Gibbons, B.H.1    Baccetti, B.2    Gibbons, I.R.3
  • 13
    • 0031881230 scopus 로고    scopus 로고
    • Studies on the eel sperm flagellum. 2. The kinematics of normal motility
    • Woolley D.M. Studies on the eel sperm flagellum. 2. The kinematics of normal motility. Cell Motil Cytoskeleton 39 (1998) 233-245
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 233-245
    • Woolley, D.M.1
  • 14
    • 0031905571 scopus 로고    scopus 로고
    • Studies on the eel sperm flagellum. 3. Vibratile motility and rotatory bending
    • Woolley D.M. Studies on the eel sperm flagellum. 3. Vibratile motility and rotatory bending. Cell Motil Cytoskeleton 39 (1998) 246-255
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 246-255
    • Woolley, D.M.1
  • 15
    • 0015840312 scopus 로고
    • The effect of partial extraction of dynein arms on the movement of reactivated sea-urchin sperm
    • Gibbons B.H., and Gibbons I.R. The effect of partial extraction of dynein arms on the movement of reactivated sea-urchin sperm. J Cell Sci 13 (1973) 337-357
    • (1973) J Cell Sci , vol.13 , pp. 337-357
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 16
    • 0023083510 scopus 로고
    • Bending patterns of Chlamydomonas flagella: IV. Mutants with defects in inner and outer dynein arms indicate differences in dynein arm function
    • Brokaw C.J., and Kamiya R. Bending patterns of Chlamydomonas flagella: IV. Mutants with defects in inner and outer dynein arms indicate differences in dynein arm function. Cell Motil Cytoskeleton 8 (1987) 68-75
    • (1987) Cell Motil Cytoskeleton , vol.8 , pp. 68-75
    • Brokaw, C.J.1    Kamiya, R.2
  • 17
    • 27644477833 scopus 로고    scopus 로고
    • 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography
    • The authors present the first cryo-tomographic work on the structure of the axoneme from sea urchin.
    • Nicastro D., McIntosh J.R., and Baumeister W. 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography. Proc Natl Acad Sci USA 102 (2005) 15889-15894. The authors present the first cryo-tomographic work on the structure of the axoneme from sea urchin.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15889-15894
    • Nicastro, D.1    McIntosh, J.R.2    Baumeister, W.3
  • 18
    • 33747598723 scopus 로고    scopus 로고
    • The molecular architecture of axonemes revealed by cryoelectron tomography
    • This excellent cryo-electron tomographic work on the intact axoneme structure reveals many new features of dynein shapes and interactions. The averaged tomograms also show some densities inside microtubule doublets.
    • Nicastro D., Schwartz C., Pierson J., Gaudette R., Porter M.E., and McIntosh J.R. The molecular architecture of axonemes revealed by cryoelectron tomography. Science 313 (2006) 944-948. This excellent cryo-electron tomographic work on the intact axoneme structure reveals many new features of dynein shapes and interactions. The averaged tomograms also show some densities inside microtubule doublets.
    • (2006) Science , vol.313 , pp. 944-948
    • Nicastro, D.1    Schwartz, C.2    Pierson, J.3    Gaudette, R.4    Porter, M.E.5    McIntosh, J.R.6
  • 19
    • 33747088253 scopus 로고    scopus 로고
    • Molecular architecture of axonemal microtubule doublets revealed by cryo-electron tomography
    • The authors reported the molecular architecture of microtubule doublets. The density map and further analysis that reached better than 3 nm resolution provided important insight into the structure and function of the doublet.
    • Sui H., and Downing K.H. Molecular architecture of axonemal microtubule doublets revealed by cryo-electron tomography. Nature 442 (2006) 475-478. The authors reported the molecular architecture of microtubule doublets. The density map and further analysis that reached better than 3 nm resolution provided important insight into the structure and function of the doublet.
    • (2006) Nature , vol.442 , pp. 475-478
    • Sui, H.1    Downing, K.H.2
  • 20
    • 0017285608 scopus 로고
    • Flagellar doublet microtubules: fractionation of minor components and alpha-tubulin from specific regions of the A-tubule
    • Linck R.W. Flagellar doublet microtubules: fractionation of minor components and alpha-tubulin from specific regions of the A-tubule. J Cell Sci 20 (1976) 405-439
    • (1976) J Cell Sci , vol.20 , pp. 405-439
    • Linck, R.W.1
  • 21
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 Å resolution
    • Lowe J., Li H., Downing K.H., and Nogales E. Refined structure of alpha beta-tubulin at 3.5 Å resolution. J Mol Biol 313 (2001) 1045-1057
    • (2001) J Mol Biol , vol.313 , pp. 1045-1057
    • Lowe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 25
    • 0037413708 scopus 로고    scopus 로고
    • Repeat motifs of tau bind to the insides of microtubules in the absence of taxol
    • Kar S., Fan J., Smith M.J., Goedert M., and Amos L.A. Repeat motifs of tau bind to the insides of microtubules in the absence of taxol. EMBO J 22 (2003) 70-77
    • (2003) EMBO J , vol.22 , pp. 70-77
    • Kar, S.1    Fan, J.2    Smith, M.J.3    Goedert, M.4    Amos, L.A.5
  • 26
    • 0015400926 scopus 로고
    • Chlamydomonas flagella. I. Isolation and electrophoretic analysis of microtubules, matrix, membranes, and mastigonemes
    • Witman G.B., Carlson K., Berliner J., and Rosenbaum J.L. Chlamydomonas flagella. I. Isolation and electrophoretic analysis of microtubules, matrix, membranes, and mastigonemes. J Cell Biol 54 (1972) 507-539
    • (1972) J Cell Biol , vol.54 , pp. 507-539
    • Witman, G.B.1    Carlson, K.2    Berliner, J.3    Rosenbaum, J.L.4
  • 27
    • 33747343902 scopus 로고    scopus 로고
    • Tektin interactions and a model for molecular functions
    • A detailed model of the tektin filament structure as it might be incorporated as one of the microtubule protofilaments is presented.
    • Setter P.W., Malvey-Dorn E., Steffen W., Stephens R.E., and Linck R.W. Tektin interactions and a model for molecular functions. Exp Cell Res 312 (2006) 2880-2896. A detailed model of the tektin filament structure as it might be incorporated as one of the microtubule protofilaments is presented.
    • (2006) Exp Cell Res , vol.312 , pp. 2880-2896
    • Setter, P.W.1    Malvey-Dorn, E.2    Steffen, W.3    Stephens, R.E.4    Linck, R.W.5
  • 28
    • 0020335261 scopus 로고
    • Structure and chemical composition of insoluble filamentous components of sperm flagellar microtubules
    • Linck R.W., and Langevin G.L. Structure and chemical composition of insoluble filamentous components of sperm flagellar microtubules. J Cell Sci 58 (1982) 1-22
    • (1982) J Cell Sci , vol.58 , pp. 1-22
    • Linck, R.W.1    Langevin, G.L.2
  • 29
    • 0023225061 scopus 로고
    • Cross-reactivity of antibodies specific for flagellar tektin and intermediate filament subunits
    • Chang X.J., and Piperno G. Cross-reactivity of antibodies specific for flagellar tektin and intermediate filament subunits. J Cell Biol 104 (1987) 1563-1568
    • (1987) J Cell Biol , vol.104 , pp. 1563-1568
    • Chang, X.J.1    Piperno, G.2
  • 30
    • 0024388980 scopus 로고
    • Relationship between tektins and intermediate filament proteins: an immunological study
    • Steffen W., and Linck R.W. Relationship between tektins and intermediate filament proteins: an immunological study. Cell Motil Cytoskeleton 14 (1989) 359-371
    • (1989) Cell Motil Cytoskeleton , vol.14 , pp. 359-371
    • Steffen, W.1    Linck, R.W.2
  • 31
    • 0026701930 scopus 로고
    • Primary structure of tektin A1: comparison with intermediate-filament proteins and a model for its association with tubulin
    • Norrander J.M., Amos L.A., and Linck R.W. Primary structure of tektin A1: comparison with intermediate-filament proteins and a model for its association with tubulin. Proc Natl Acad Sci USA 89 (1992) 8567-8571
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8567-8571
    • Norrander, J.M.1    Amos, L.A.2    Linck, R.W.3
  • 32
    • 0027504663 scopus 로고
    • Tektin B1 from ciliary microtubules: primary structure as deduced from the cDNA sequence and comparison with tektin A1
    • Chen R., Perrone C.A., Amos L.A., and Linck R.W. Tektin B1 from ciliary microtubules: primary structure as deduced from the cDNA sequence and comparison with tektin A1. J Cell Sci 106 (1993) 909-918
    • (1993) J Cell Sci , vol.106 , pp. 909-918
    • Chen, R.1    Perrone, C.A.2    Amos, L.A.3    Linck, R.W.4
  • 33
    • 0029240498 scopus 로고
    • At least one of the protofilaments in flagellar microtubules is not composed of tubulin
    • Nojima D., Linck R.W., and Egelman E.H. At least one of the protofilaments in flagellar microtubules is not composed of tubulin. Curr Biol 5 (1995) 158-167
    • (1995) Curr Biol , vol.5 , pp. 158-167
    • Nojima, D.1    Linck, R.W.2    Egelman, E.H.3
  • 34
    • 0031913583 scopus 로고    scopus 로고
    • Two proteins isolated from sea urchin sperm flagella: structural components common to the stable microtubules of axonemes and centrioles
    • Hinchcliffe E.H., and Linck R.W. Two proteins isolated from sea urchin sperm flagella: structural components common to the stable microtubules of axonemes and centrioles. J Cell Sci 111 (1998) 585-595
    • (1998) J Cell Sci , vol.111 , pp. 585-595
    • Hinchcliffe, E.H.1    Linck, R.W.2
  • 35
    • 0242540472 scopus 로고    scopus 로고
    • Protofilament ribbon compartments of ciliary and flagellar microtubules
    • Linck R.W., and Norrander J.M. Protofilament ribbon compartments of ciliary and flagellar microtubules. Protist 154 (2003) 299-311
    • (2003) Protist , vol.154 , pp. 299-311
    • Linck, R.W.1    Norrander, J.M.2
  • 36
    • 0037470084 scopus 로고    scopus 로고
    • Rib72, a conserved protein associated with the ribbon compartment of flagellar A-microtubules and potentially involved in the linkage between outer doublet microtubules
    • Ikeda K., Brown J.A., Yagi T., Norrander J.M., Hirono M., Eccleston E., Kamiya R., and Linck R.W. Rib72, a conserved protein associated with the ribbon compartment of flagellar A-microtubules and potentially involved in the linkage between outer doublet microtubules. J Biol Chem 278 (2003) 7725-7734
    • (2003) J Biol Chem , vol.278 , pp. 7725-7734
    • Ikeda, K.1    Brown, J.A.2    Yagi, T.3    Norrander, J.M.4    Hirono, M.5    Eccleston, E.6    Kamiya, R.7    Linck, R.W.8
  • 37
    • 0037072484 scopus 로고    scopus 로고
    • 2+-regulated nucleoside-diphosphate kinase system within the Chlamydomonas flagellum. The regulatory subunit p72
    • 2+-regulated nucleoside-diphosphate kinase system within the Chlamydomonas flagellum. The regulatory subunit p72. J Biol Chem 277 (2002) 34271-34279
    • (2002) J Biol Chem , vol.277 , pp. 34271-34279
    • Patel-King, R.S.1    Benashski, S.E.2    King, S.M.3
  • 38
    • 0024623686 scopus 로고
    • Retention of ciliary ninefold structure after removal of microtubules
    • Stephens R.E., Oleszko-Szuts S., and Linck R.W. Retention of ciliary ninefold structure after removal of microtubules. J Cell Sci 92 (1989) 391-402
    • (1989) J Cell Sci , vol.92 , pp. 391-402
    • Stephens, R.E.1    Oleszko-Szuts, S.2    Linck, R.W.3
  • 39
    • 0014342870 scopus 로고
    • Studies on cilia. 3. Further studies on the cilium tip and a "sliding filament" model of ciliary motility
    • Satir P. Studies on cilia. 3. Further studies on the cilium tip and a "sliding filament" model of ciliary motility. J Cell Biol 39 (1968) 77-94
    • (1968) J Cell Biol , vol.39 , pp. 77-94
    • Satir, P.1
  • 40
    • 0029162615 scopus 로고
    • Novel mode of hyper-oscillation in the paralyzed axoneme of a Chlamydomonas mutant lacking the central-pair microtubules
    • Yagi T., and Kamiya R. Novel mode of hyper-oscillation in the paralyzed axoneme of a Chlamydomonas mutant lacking the central-pair microtubules. Cell Motil Cytoskeleton 31 (1995) 207-214
    • (1995) Cell Motil Cytoskeleton , vol.31 , pp. 207-214
    • Yagi, T.1    Kamiya, R.2
  • 41
    • 0030058586 scopus 로고    scopus 로고
    • Flexural rigidity of microtubules measured with the use of optical tweezers
    • Felgner H., Frank R., and Schliwa M. Flexural rigidity of microtubules measured with the use of optical tweezers. J Cell Sci 109 (1996) 509-516
    • (1996) J Cell Sci , vol.109 , pp. 509-516
    • Felgner, H.1    Frank, R.2    Schliwa, M.3
  • 43
    • 33746784797 scopus 로고    scopus 로고
    • Elastic response, buckling, and instability of microtubules under radial indentation
    • The authors studied the mechanical response of the microtubule to direct indentation by atomic force microscopy.
    • Schaap I.A., Carrasco C., de Pablo P.J., MacKintosh F.C., and Schmidt C.F. Elastic response, buckling, and instability of microtubules under radial indentation. Biophys J 91 (2006) 1521-1531. The authors studied the mechanical response of the microtubule to direct indentation by atomic force microscopy.
    • (2006) Biophys J , vol.91 , pp. 1521-1531
    • Schaap, I.A.1    Carrasco, C.2    de Pablo, P.J.3    MacKintosh, F.C.4    Schmidt, C.F.5


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