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Volumn 17, Issue 6, 2006, Pages 2626-2635

Disruption of the A-kinase anchoring domain in flagellar radial spoke protein 3 results in unregulated axonemal cAMP-dependent protein kinase activity and abnormal flagellar motility

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; RADIAL SPOKE PROTEIN 3; UNCLASSIFIED DRUG;

EID: 33744728042     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-02-0095     Document Type: Article
Times cited : (49)

References (58)
  • 1
    • 7944223873 scopus 로고    scopus 로고
    • Cilia-related diseases
    • Afzelius, B. A. (2004). Cilia-related diseases. J. Pathol. 204, 470-477.
    • (2004) J. Pathol. , vol.204 , pp. 470-477
    • Afzelius, B.A.1
  • 2
    • 27744522623 scopus 로고    scopus 로고
    • Cyclical interactions between two outer doublet microtubules in split flagellar axonemes
    • Aoyama, S., and Kamiya, R. (2005). Cyclical interactions between two outer doublet microtubules in split flagellar axonemes. Biophys. J. 89, 3261-3268.
    • (2005) Biophys. J. , vol.89 , pp. 3261-3268
    • Aoyama, S.1    Kamiya, R.2
  • 3
    • 2342657884 scopus 로고    scopus 로고
    • Decoding cilia function: Denning specialized genes required for compartmentalized cilia biogenesis
    • Avidor-Reiss, T., Maer, A. M., Koundakjian, E., Polyanovsky, A., Keil, T., Subramaniam, S., and Zuker, C. S. (2004). Decoding cilia function: denning specialized genes required for compartmentalized cilia biogenesis. Cell 117, 527-539.
    • (2004) Cell , vol.117 , pp. 527-539
    • Avidor-Reiss, T.1    Maer, A.M.2    Koundakjian, E.3    Polyanovsky, A.4    Keil, T.5    Subramaniam, S.6    Zuker, C.S.7
  • 4
    • 0023440964 scopus 로고
    • Regulation of sperm flagellar motility by calcium and cAMF-dependent phosphorylation
    • Brokaw, C. J. (1987). Regulation of sperm flagellar motility by calcium and cAMF-dependent phosphorylation. J. Cell. Biochem. 35, 175-184.
    • (1987) J. Cell. Biochem. , vol.35 , pp. 175-184
    • Brokaw, C.J.1
  • 5
    • 0025949481 scopus 로고
    • Microtubule sliding in swimming sperm flagella: Direct and indirect measurements on sea urchin and tunicate spermatozoa
    • Brokaw, C. J. (1991). Microtubule sliding in swimming sperm flagella: direct and indirect measurements on sea urchin and tunicate spermatozoa. J. Cell Biol. 114, 1201-1215.
    • (1991) J. Cell Biol. , vol.114 , pp. 1201-1215
    • Brokaw, C.J.1
  • 6
    • 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. (1987). 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, 68-75.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 68-75
    • Brokaw, C.J.1    Kamiya, R.2
  • 7
    • 0020047275 scopus 로고
    • Analysis of the movement of Chlamydomonas flagella: The function of the radial-spoke system is revealed by comparison of wild-type and mutant flagella
    • Brokaw, C. J., Luck, D. J., and Huang, B. (1982). Analysis of the movement of Chlamydomonas flagella: the function of the radial-spoke system is revealed by comparison of wild-type and mutant flagella. J. Cell Biol. 92, 722-732.
    • (1982) J. Cell Biol. , vol.92 , pp. 722-732
    • Brokaw, C.J.1    Luck, D.J.2    Huang, B.3
  • 8
    • 0027511865 scopus 로고
    • Flagellar radial spoke: A model molecular genetic system for studying organelle assembly
    • Curry, A. M., and Rosenbaum, J. L. (1993). Flagellar radial spoke: a model molecular genetic system for studying organelle assembly. Cell Motil. Cytoskeleton 24, 224-232.
    • (1993) Cell Motil. Cytoskeleton , vol.24 , pp. 224-232
    • Curry, A.M.1    Rosenbaum, J.L.2
  • 9
    • 0027436318 scopus 로고
    • Assembly of flagellar radial spoke proteins in Chlamydomonas: Identification of the axoneme binding domain of radial spoke protein 3
    • Diener, D. R., Ang, L. H., and Rosenbaum, J. L. (1993). Assembly of flagellar radial spoke proteins in Chlamydomonas: identification of the axoneme binding domain of radial spoke protein 3. J. Cell Biol. 123, 183-190.
    • (1993) J. Cell Biol. , vol.123 , pp. 183-190
    • Diener, D.R.1    Ang, L.H.2    Rosenbaum, J.L.3
  • 10
    • 0344838614 scopus 로고    scopus 로고
    • Lateralization defects and ciliary dyskinesia: Lessons from algae
    • El Zein, L., Omran, H., and Bouvagnet, P. (2003). Lateralization defects and ciliary dyskinesia: lessons from algae. Trends Genet 19, 162-167.
    • (2003) Trends Genet , vol.19 , pp. 162-167
    • El Zein, L.1    Omran, H.2    Bouvagnet, P.3
  • 12
    • 0035897417 scopus 로고    scopus 로고
    • Flagellar radial spoke protein 3 is an A-kinase anchoring protein (AKAP)
    • Gaillard, A. R., Diener, D. R., Rosenbaum, J. L., and Sale, W. S. (2001). Flagellar radial spoke protein 3 is an A-kinase anchoring protein (AKAP). J. Cell Biol. 153, 443-448.
    • (2001) J. Cell Biol. , vol.153 , pp. 443-448
    • Gaillard, A.R.1    Diener, D.R.2    Rosenbaum, J.L.3    Sale, W.S.4
  • 13
    • 0029890059 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by an axonemal type-1 phosphatase in Chlamydomonas
    • Habermacher, G., and Sale, W. S. (1996). Regulation of flagellar dynein by an axonemal type-1 phosphatase in Chlamydomonas. J. Cell Sci. 109, 1899-1907.
    • (1996) J. Cell Sci. , vol.109 , pp. 1899-1907
    • Habermacher, G.1    Sale, W.S.2
  • 14
    • 0031022258 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by phosphorylation of a 138-kD inner arm dynein intermediate chain
    • Habermacher, G., and Sale, W. S. (1997). Regulation of flagellar dynein by phosphorylation of a 138-kD inner arm dynein intermediate chain. J. Cell Biol. 136, 167-176.
    • (1997) J. Cell Biol. , vol.136 , pp. 167-176
    • Habermacher, G.1    Sale, W.S.2
  • 15
    • 0025881253 scopus 로고
    • cAMP-stimulated phosphorylation of an axonemal polypeptide that copurifies with the 22S dynein arm regulates microtubule translocation velocity and swimming speed in Paramecium
    • Hamasaki, T., Barkalow, K., Richmond, J., and Satir, P. (1991). cAMP-stimulated phosphorylation of an axonemal polypeptide that copurifies with the 22S dynein arm regulates microtubule translocation velocity and swimming speed in Paramecium. Proc. Natl. Acad. Sci. USA 88, 7918-7922.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7918-7922
    • Hamasaki, T.1    Barkalow, K.2    Richmond, J.3    Satir, P.4
  • 17
    • 0023460829 scopus 로고
    • Stimulation of in vitro motility of Chlamydomonas axonemes by inhibition of cAMP-dependent phosphorylation
    • Hasegawa, E., Hayashi, H., Asakura, S., and Kamiya, R. (1987). Stimulation of in vitro motility of Chlamydomonas axonemes by inhibition of cAMP-dependent phosphorylation. Cell Motil. Cytoskeleton 8, 302-311.
    • (1987) Cell Motil. Cytoskeleton , vol.8 , pp. 302-311
    • Hasegawa, E.1    Hayashi, H.2    Asakura, S.3    Kamiya, R.4
  • 18
    • 9444222732 scopus 로고    scopus 로고
    • IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending
    • Hendrickson, T. W., Perrone, C. A., Griffin, P., Wuichet, K., Mueller, J., Yang, P., Porter, M. E., and Sale, W. S. (2004). IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending. Mol. Biol. Cell 12, 5431-5442.
    • (2004) Mol. Biol. Cell , vol.12 , pp. 5431-5442
    • Hendrickson, T.W.1    Perrone, C.A.2    Griffin, P.3    Wuichet, K.4    Mueller, J.5    Yang, P.6    Porter, M.E.7    Sale, W.S.8
  • 19
    • 0028007426 scopus 로고
    • Regulation of Chlamydomonas flagellar dynein by an axonemal protein kinase
    • Howard, D. R., Habermacher, G., Glass, D. B., Smith, E. F., and Sale, W. S. (1994). Regulation of Chlamydomonas flagellar dynein by an axonemal protein kinase. J. Cell Biol. 127, 1683-1692.
    • (1994) J. Cell Biol. , vol.127 , pp. 1683-1692
    • Howard, D.R.1    Habermacher, G.2    Glass, D.B.3    Smith, E.F.4    Sale, W.S.5
  • 20
    • 0035995284 scopus 로고    scopus 로고
    • Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants
    • Kamiya, R. (2002). Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants. Int. Rev. Cytol. 219, 115-155.
    • (2002) Int. Rev. Cytol. , vol.219 , pp. 115-155
    • Kamiya, R.1
  • 21
    • 0025117612 scopus 로고
    • High-frequency nuclear transformation of Chlamydomonas reinhardtii
    • Kindle, K. L. (1990). High-frequency nuclear transformation of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 87, 1228-1232.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1228-1232
    • Kindle, K.L.1
  • 22
    • 0031012517 scopus 로고    scopus 로고
    • Phosphoregulation of an inner dynein arm complex in Chlamydomonas reinhardtii is altered in phototactic mutant strains
    • King, S. J., and Dutcher, S. K. (1997). Phosphoregulation of an inner dynein arm complex in Chlamydomonas reinhardtii is altered in phototactic mutant strains. J. Cell Biol. 136, 177-191.
    • (1997) J. Cell Biol. , vol.136 , pp. 177-191
    • King, S.J.1    Dutcher, S.K.2
  • 24
    • 1842854486 scopus 로고    scopus 로고
    • Characterization of an A-kinase anchoring protein in human ciliary axonemes
    • Kultgen, P. L., Byrd, S. K., Ostrowski, L. E., and Milgram, S. L. (2002). Characterization of an A-kinase anchoring protein in human ciliary axonemes. Mol. Biol. Cell 13, 4156-4166.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4156-4166
    • Kultgen, P.L.1    Byrd, S.K.2    Ostrowski, L.E.3    Milgram, S.L.4
  • 25
    • 0038168237 scopus 로고    scopus 로고
    • Phosphorylation of phosphatase inhibitor-2 at centrosomes during mitosis
    • Leach, C., Shenolikar, S., and Brautigan, D. L. (2003). Phosphorylation of phosphatase inhibitor-2 at centrosomes during mitosis. J. Biol. Chem. 278, 26015-26020.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26015-26020
    • Leach, C.1    Shenolikar, S.2    Brautigan, D.L.3
  • 27
    • 2342501364 scopus 로고    scopus 로고
    • Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene
    • Li, J. B., et al. (2004). Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene. Cell 117, 541-552.
    • (2004) Cell , vol.117 , pp. 541-552
    • Li, J.B.1
  • 28
    • 33744721514 scopus 로고    scopus 로고
    • Phosphorylation of the Pro-X-Thr-Pro site in phosphatase inhibitor-2 by cyclin-dependent protein kinase during M-phase of the cell cycle
    • in press
    • Li, M., Stefansson, B., Wang, W., Schaefer, E. M., and Brautigan, D. L. (2005). Phosphorylation of the Pro-X-Thr-Pro site in phosphatase inhibitor-2 by cyclin-dependent protein kinase during M-phase of the cell cycle. Cell Signal (in press).
    • (2005) Cell Signal
    • Li, M.1    Stefansson, B.2    Wang, W.3    Schaefer, E.M.4    Brautigan, D.L.5
  • 29
    • 13444262384 scopus 로고    scopus 로고
    • CDD: A conserved domain database for protein classification
    • Marchler-Bauer, A., et al. (2005). CDD: a conserved domain database for protein classification. Nucleic Acids Res. 33, D192-D196.
    • (2005) Nucleic Acids Res. , vol.33
    • Marchler-Bauer, A.1
  • 30
    • 0041845296 scopus 로고    scopus 로고
    • Cilia are at the heart of vertebrate left-right asymmetry
    • McGrath, J., and Brueckner, M. (2003). Cilia are at the heart of vertebrate left-right asymmetry. Curr. Opin. Genet Dev. 13, 385-392.
    • (2003) Curr. Opin. Genet Dev. , vol.13 , pp. 385-392
    • McGrath, J.1    Brueckner, M.2
  • 31
    • 0019437867 scopus 로고
    • A rapid sensitive silver stain for polypeptides in polyacrylamide gels
    • Merril, C. R., Dunau, M. L., and Goldman, D. (1981). A rapid sensitive silver stain for polypeptides in polyacrylamide gels. Anal. Biochem. 110, 201-207.
    • (1981) Anal. Biochem. , vol.110 , pp. 201-207
    • Merril, C.R.1    Dunau, M.L.2    Goldman, D.3
  • 32
    • 0033601735 scopus 로고    scopus 로고
    • Characterization of a Chlamydomonas insertional mutant that disrupts flagellar central pair microtubule-associated structures
    • Mitchell, D. R., and Sale, W. S. (1999). Characterization of a Chlamydomonas insertional mutant that disrupts flagellar central pair microtubule-associated structures. J. Cell Biol. 144, 293-304.
    • (1999) J. Cell Biol. , vol.144 , pp. 293-304
    • Mitchell, D.R.1    Sale, W.S.2
  • 33
    • 0037326173 scopus 로고    scopus 로고
    • Identification of a novel leucine-rich repeat protein as a component of flagellar radial spoke in the ascidian Ciona intestinalis
    • Padma, P., Satouh, Y., Wakabayashi, K., Hozumi, A., Ushimaru, Y., Kamiya, R., and Inaba, K. (2003). Identification of a novel leucine-rich repeat protein as a component of flagellar radial spoke in the ascidian Ciona intestinalis. Mol. Biol. Cell 14, 774-785.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 774-785
    • Padma, P.1    Satouh, Y.2    Wakabayashi, K.3    Hozumi, A.4    Ushimaru, Y.5    Kamiya, R.6    Inaba, K.7
  • 34
    • 17144377111 scopus 로고    scopus 로고
    • Cilium-generated signaling and cilia-related disorders
    • Pan, J., Wang, Q., and Snell, W. J. (2005). Cilium-generated signaling and cilia-related disorders. Lab. Investig. 85, 452-463.
    • (2005) Lab. Investig. , vol.85 , pp. 452-463
    • Pan, J.1    Wang, Q.2    Snell, W.J.3
  • 35
  • 36
    • 0019365126 scopus 로고
    • Radial spokes of Chlamydomonas flagella: Polypeptide composition and phosphorylation of stalk components
    • Piperno, G., Huang, B., Ramanis, Z., and Luck, D. J. (1981). Radial spokes of Chlamydomonas flagella: polypeptide composition and phosphorylation of stalk components. J. Cell Biol. 88, 73-79.
    • (1981) J. Cell Biol. , vol.88 , pp. 73-79
    • Piperno, G.1    Huang, B.2    Ramanis, Z.3    Luck, D.J.4
  • 37
    • 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. (2000). The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility. J. Cell Biol. 151, F37-42.
    • (2000) J. Cell Biol. , vol.151
    • Porter, M.E.1    Sale, W.S.2
  • 38
    • 22344445826 scopus 로고    scopus 로고
    • Cilia and the cell cycle?
    • Quarmby, L. M., and Parker, J. D. (2005). Cilia and the cell cycle? J. Cell Biol. 169, 707-710.
    • (2005) J. Cell Biol. , vol.169 , pp. 707-710
    • Quarmby, L.M.1    Parker, J.D.2
  • 39
    • 0032544711 scopus 로고    scopus 로고
    • The catalytic subunit of the cAMP-dependent protein kinase of ovine sperm flagella has a unique amino-terminal sequence
    • San Agustin, J. T., Leszyk, J. D., Nuwaysir, L. M., and Witman, G. B. (1998). The catalytic subunit of the cAMP-dependent protein kinase of ovine sperm flagella has a unique amino-terminal sequence. J. Biol. Chem. 273, 24874-24883.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24874-24883
    • San Agustin, J.T.1    Leszyk, J.D.2    Nuwaysir, L.M.3    Witman, G.B.4
  • 40
    • 0014342870 scopus 로고
    • Studies on cilia. 3. Further studies on the cilium tip and a "sliding filament" model of ciliary motility
    • Satir, P. (1968). Studies on cilia. 3. Further studies on the cilium tip and a "sliding filament" model of ciliary motility. J. Cell Biol. 39, 77-94.
    • (1968) J. Cell Biol. , vol.39 , pp. 77-94
    • Satir, P.1
  • 41
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P., and Ponting, C. P. (1998). SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA 95, 5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 42
    • 0017575980 scopus 로고
    • Local reactivation of Triton-extracted flagella by iontophoretic application of ATP
    • Shingyoji, C., Murakami, A., and Takahashi, K. (1977). Local reactivation of Triton-extracted flagella by iontophoretic application of ATP. Nature 265, 269-270.
    • (1977) Nature , vol.265 , pp. 269-270
    • Shingyoji, C.1    Murakami, A.2    Takahashi, K.3
  • 43
    • 85047681474 scopus 로고    scopus 로고
    • Assembly and motility of eukaryotic cilia and flagella. Lessons from Chlamydomonas reinhardtii
    • Silflow, C. D., and Lefebvre, P. A. (2001). Assembly and motility of eukaryotic cilia and flagella. Lessons from Chlamydomonas reinhardtii. Plant Physiol. 127, 1500-1507.
    • (2001) Plant Physiol. , vol.127 , pp. 1500-1507
    • Silflow, C.D.1    Lefebvre, P.A.2
  • 44
    • 0036245322 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by the axonemal central apparatus
    • Smith, E. F. (2002). Regulation of flagellar dynein by the axonemal central apparatus. Cell Motil. Cytoskeleton 52, 33-42.
    • (2002) Cell Motil. Cytoskeleton , vol.52 , pp. 33-42
    • Smith, E.F.1
  • 45
    • 0026768745 scopus 로고
    • Regulation of dynein-driven microtubule sliding by the radial spokes in flagella
    • Smith, E. F., and Sale, W. S. (1992). Regulation of dynein-driven microtubule sliding by the radial spokes in flagella. Science 257, 1557-1559.
    • (1992) Science , vol.257 , pp. 1557-1559
    • Smith, E.F.1    Sale, W.S.2
  • 46
    • 0346732099 scopus 로고    scopus 로고
    • The radial spokes and central apparatus: Mechano-chemical transducers that regulate flagellar motility
    • Smith, E. F., and Yang, P. (2004). The radial spokes and central apparatus: mechano-chemical transducers that regulate flagellar motility. Cell Motil. Cytoskeleton 57, 8-17.
    • (2004) Cell Motil. Cytoskeleton , vol.57 , pp. 8-17
    • Smith, E.F.1    Yang, P.2
  • 47
    • 2942521612 scopus 로고    scopus 로고
    • Cilia and flagella revealed: From flagellar assembly in Chlamydomonas to human obesity disorders
    • Snell, W. J., Pan, J., and Wang, Q. (2004). Cilia and flagella revealed: from flagellar assembly in Chlamydomonas to human obesity disorders. Cell 117, 693-697.
    • (2004) Cell , vol.117 , pp. 693-697
    • Snell, W.J.1    Pan, J.2    Wang, Q.3
  • 48
    • 0015188644 scopus 로고
    • Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm
    • Summers, K. E., and Gibbons, I. R. (1971). Adenosine triphosphate-induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm. Proc. Natl. Acad. Sci. USA 68, 3092-3096.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 3092-3096
    • Summers, K.E.1    Gibbons, I.R.2
  • 49
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken, K., and Aandahl, E. M. (2004). Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol. Rev. 84, 137-167.
    • (2004) Physiol. Rev. , vol.84 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 50
    • 17644385919 scopus 로고    scopus 로고
    • Two anti-radial spoke monoclonal antibodies inhibit Chlamydomonas axonemal motility by different mechanisms
    • White, D., Aghigh, S., Magder, I., Cosson, J., Huitorel, P., and Gagnon, C. (2005). Two anti-radial spoke monoclonal antibodies inhibit Chlamydomonas axonemal motility by different mechanisms. J. Biol. Chem. 280, 14803-14810.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14803-14810
    • White, D.1    Aghigh, S.2    Magder, I.3    Cosson, J.4    Huitorel, P.5    Gagnon, C.6
  • 51
    • 0022962478 scopus 로고
    • Isolation of Chlamydomonas flagella and flagellar axonemes
    • Witman, G. B. (1986). Isolation of Chlamydomonas flagella and flagellar axonemes. Methods Enzymol. 134, 280-290.
    • (1986) Methods Enzymol. , vol.134 , pp. 280-290
    • Witman, G.B.1
  • 52
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • Wong, W., and Scott, J. D. (2004). AKAP signalling complexes: focal points in space and time. Nat. Rev. Mol. Cell. Biol. 5, 959-970.
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 53
    • 13644257563 scopus 로고    scopus 로고
    • Both cAMP and cGMP are required for maximal ciliary beat stimulation in a cell-free model of bovine ciliary axonemes
    • Wyatt, T. A., Forget, M. A., Adams, J. M., and Sisson, J. H. (2005). Both cAMP and cGMP are required for maximal ciliary beat stimulation in a cell-free model of bovine ciliary axonemes. Am. J. Physiol. 288, L546-L551.
    • (2005) Am. J. Physiol. , vol.288
    • Wyatt, T.A.1    Forget, M.A.2    Adams, J.M.3    Sisson, J.H.4
  • 54
    • 30044437241 scopus 로고    scopus 로고
    • The flagellar motility of Chlamydomonas pf25 mutant lacking an AKAP-binding protein is overtly sensitive to medium conditions
    • Yang, C., and Yang, P. (2006). The flagellar motility of Chlamydomonas pf25 mutant lacking an AKAP-binding protein is overtly sensitive to medium conditions. Mol. Biol. Cell 17, 227-238.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 227-238
    • Yang, C.1    Yang, P.2
  • 55
    • 0033967129 scopus 로고    scopus 로고
    • Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme
    • Yang, P., Fox, L., Colbran, R. J., and Sale, W. S. (2000). Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme. J. Cell Sci. 113, 91-102.
    • (2000) J. Cell Sci. , vol.113 , pp. 91-102
    • Yang, P.1    Fox, L.2    Colbran, R.J.3    Sale, W.S.4
  • 56
    • 33645744387 scopus 로고    scopus 로고
    • Radial spoke proteins of Chlamydomonas flagella
    • Yang, P., et al. (2006). Radial spoke proteins of Chlamydomonas flagella. J. Cell Sci. 119, 1165-1174.
    • (2006) J. Cell Sci. , vol.119 , pp. 1165-1174
    • Yang, P.1
  • 57
    • 0034705378 scopus 로고    scopus 로고
    • Casein kinase I is anchored on axonemal doublet microtubules and regulates flagellar dynein phosphorylation and activity
    • Yang, P., and Sale, W. S. (2000). Casein kinase I is anchored on axonemal doublet microtubules and regulates flagellar dynein phosphorylation and activity. J. Biol. Chem. 275, 18905-18912.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18905-18912
    • Yang, P.1    Sale, W.S.2
  • 58
    • 1242345201 scopus 로고    scopus 로고
    • Flagellar radial spoke protein 2 is a calmodulin binding protein required for motility in Chlamydomonas reinhardtii. Eukaryot
    • Yang, P., Yang, C., and Sale, W. S. (2004). Flagellar radial spoke protein 2 is a calmodulin binding protein required for motility in Chlamydomonas reinhardtii. Eukaryot. Cell 3, 72-81.
    • (2004) Cell , vol.3 , pp. 72-81
    • Yang, P.1    Yang, C.2    Sale, W.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.