메뉴 건너뛰기




Volumn 179, Issue 3, 2007, Pages 515-526

A conserved CaM- and radial spoke-associated complex mediates regulation of flagellar dynein activity

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALMODULIN; CELL PROTEIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE; FLAGELLAR ASSOCIATED PROTEIN 91; UNCLASSIFIED DRUG;

EID: 35948992977     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200703107     Document Type: Article
Times cited : (111)

References (48)
  • 1
    • 0019050328 scopus 로고
    • Calcium control of wave-form in isolated flagellar axonemes of Chlamydomonas
    • Bessen, M., R.B. Fay, and G.B. Witman. 1980. Calcium control of wave-form in isolated flagellar axonemes of Chlamydomonas. J. Cell Biol. 86:446-455.
    • (1980) J. Cell Biol , vol.86 , pp. 446-455
    • Bessen, M.1    Fay, R.B.2    Witman, G.B.3
  • 2
    • 0018584031 scopus 로고
    • Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella
    • Brokaw, C.J. 1979. Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella. J. Cell Biol. 82:401-411.
    • (1979) J. Cell Biol , vol.82 , pp. 401-411
    • Brokaw, C.J.1
  • 3
    • 0016247865 scopus 로고
    • Calcium ion regulation of flagellar beat symmetry in reactivated sea urchin spermatozoa
    • Brokaw, C.J., R. Josslin, and L. Bobrow. 1974. Calcium ion regulation of flagellar beat symmetry in reactivated sea urchin spermatozoa. Biochem. Biophys. Res. Commun. 58:795-800.
    • (1974) Biochem. Biophys. Res. Commun , vol.58 , pp. 795-800
    • Brokaw, C.J.1    Josslin, R.2    Bobrow, L.3
  • 4
    • 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., L.H. Ang, and J.L. Rosenbaum. 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
  • 5
    • 0035897417 scopus 로고    scopus 로고
    • Flagellar radial spoke protein 3 is an A-kinase anchoring protein (AKAP)
    • Gaillard, A.R., D.R. Diener, J.L. Rosenbaum, and W.S. Sale. 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
  • 6
    • 33744728042 scopus 로고    scopus 로고
    • 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
    • Gaillard, A.R., L.A. Fox, J.M. Rhea, B. Craige, and W.S. Sale. 2006. 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. Mol. Biol. Cell. 17:2626-2635.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2626-2635
    • Gaillard, A.R.1    Fox, L.A.2    Rhea, J.M.3    Craige, B.4    Sale, W.S.5
  • 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., E. O'Toole, C.A. Perrone, T. Giddings, and M.E. Porter. 1994. 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. 127:1311-1325.
    • (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
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: Their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii
    • Gorman, D.S., and R.P. Levine. 1965. Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA. 54:1665-1669.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 9
    • 0029165838 scopus 로고
    • Regulation of dynein-driven microtubule sliding by an axonemal kinase and phosphatase in Chlamydomonas flagella
    • Habermacher, G., and W.S. Sale. 1995. Regulation of dynein-driven microtubule sliding by an axonemal kinase and phosphatase in Chlamydomonas flagella. Cell Motil. Cytoskeleton. 32:106-109.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 106-109
    • Habermacher, G.1    Sale, W.S.2
  • 10
    • 0029890059 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by an axonemal type-1 phosphatase in Chlamydomonas
    • Habermacher, G., and W.S. Sale. 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
  • 11
    • 0031022258 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by phosphorylation of a 138-kD inner arm dynein intermediate chain
    • Habermacher, G., and W.S. Sale. 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
  • 12
  • 13
    • 0028007426 scopus 로고
    • Regulation of Chlamydomonas flagellar dynein by an axonemal protein kinase
    • Howard, D.R., G. Habermacher, D.B. Glass, E.F. Smith, and W.S. Sale. 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
  • 14
    • 0019372102 scopus 로고
    • Radial spokes of Chlamydomonas flagella: Genetic analysis of assembly and function
    • Huang, B., G. Piperno, Z. Ramanis, and D.J. Luck. 1981. Radial spokes of Chlamydomonas flagella: genetic analysis of assembly and function. J. Cell Biol. 88:80-88.
    • (1981) J. Cell Biol , vol.88 , pp. 80-88
    • Huang, B.1    Piperno, G.2    Ramanis, Z.3    Luck, D.J.4
  • 15
    • 0020082250 scopus 로고
    • Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function
    • Huang, B., Z. Ramanis, and D.J. Luck. 1982. Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function. Cell. 28:115-124.
    • (1982) Cell , vol.28 , pp. 115-124
    • Huang, B.1    Ramanis, Z.2    Luck, D.J.3
  • 16
    • 0021861320 scopus 로고
    • Tetrahymena cell model exhibiting Ca-dependant behavior
    • Izumi, A., and T. Miki-Noumura. 1985. Tetrahymena cell model exhibiting Ca-dependant behavior. Cell Motil. 5:323-331.
    • (1985) Cell Motil , vol.5 , pp. 323-331
    • Izumi, A.1    Miki-Noumura, T.2
  • 17
    • 0027097082 scopus 로고
    • Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein
    • Kagami, O., and R. Kamiya. 1992. Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein. J. Cell Sci. 103:653-664.
    • (1992) J. Cell Sci , vol.103 , pp. 653-664
    • Kagami, O.1    Kamiya, R.2
  • 18
    • 0021335092 scopus 로고
    • Submicromolar levels of calcium control the balance of beating between the two flagella in demembranated models of Chlamydomonas
    • Kamiya, R., and G.B. Witman. 1984. Submicromolar levels of calcium control the balance of beating between the two flagella in demembranated models of Chlamydomonas. J. Cell Biol. 98:97-107.
    • (1984) J. Cell Biol , vol.98 , pp. 97-107
    • Kamiya, R.1    Witman, G.B.2
  • 19
    • 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 S.K. Dutcher. 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
  • 21
    • 0015494798 scopus 로고
    • Reactivated triton-extracted models of paramecium: Modification of ciliary movement by calcium ions
    • Naitoh, Y., and H. Kaneko. 1972. Reactivated triton-extracted models of paramecium: modification of ciliary movement by calcium ions. Science. 176:523-524.
    • (1972) Science , vol.176 , pp. 523-524
    • Naitoh, Y.1    Kaneko, H.2
  • 22
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E.J., C.J. Schmidt, R. Nambudripad, and T.F. Smith. 1994. The ancient regulatory-protein family of WD-repeat proteins. Nature. 371:297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 24
    • 0023009146 scopus 로고
    • Microtubule sliding in mutant Chlamydomonas axonemes devoid of outer or inner dynein arms
    • Okagaki, T., and R. Kamiya. 1986. Microtubule sliding in mutant Chlamydomonas axonemes devoid of outer or inner dynein arms. J. Cell Biol. 103:1895-1902.
    • (1986) J. Cell Biol , vol.103 , pp. 1895-1902
    • Okagaki, T.1    Kamiya, R.2
  • 25
    • 14644388135 scopus 로고    scopus 로고
    • Phototactic activity in Chlamydomonas 'non-phototactic' mutants deficient in Ca2+-dependent control of flagellar dominance or in inner-arm dynein
    • Okita, N., N. Isogai, M. Hirono, R. Kamiya, and K. Yoshimura. 2005. Phototactic activity in Chlamydomonas 'non-phototactic' mutants deficient in Ca2+-dependent control of flagellar dominance or in inner-arm dynein. J. Cell Sci. 118:529-537.
    • (2005) J. Cell Sci , vol.118 , pp. 529-537
    • Okita, N.1    Isogai, N.2    Hirono, M.3    Kamiya, R.4    Yoshimura, K.5
  • 27
    • 0019365126 scopus 로고
    • Radial spokes of Chlamydomonas flagella: Polypeptide composition and phosphorylation of stalk components
    • Piperno, G., B. Huang, Z. Ramanis, and D.J. Luck. 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
  • 28
    • 0025019981 scopus 로고
    • Three distinct inner dynein arms in Chlamydomonas flagella: Molecular composition and location in the axoneme
    • Piperno, G., Z. Ramanis, E.F. Smith, and W.S. Sale. 1990. Three distinct inner dynein arms in Chlamydomonas flagella: molecular composition and location in the axoneme. J. Cell Biol. 110:379-389.
    • (1990) J. Cell Biol , vol.110 , pp. 379-389
    • Piperno, G.1    Ramanis, Z.2    Smith, E.F.3    Sale, W.S.4
  • 29
    • 0026673055 scopus 로고    scopus 로고
    • Piperno, G., K. Mead, and W. Shestak. 1992. The inner dynein arms I2 interact with a dynein regulatory complex in Chlamydomonas flagella. J. Cell Biol. 118:1455-1463.
    • Piperno, G., K. Mead, and W. Shestak. 1992. The inner dynein arms I2 interact with a "dynein regulatory complex" in Chlamydomonas flagella. J. Cell Biol. 118:1455-1463.
  • 30
    • 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 W.S. Sale. 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-F42.
    • (2000) J. Cell Biol , vol.151
    • Porter, M.E.1    Sale, W.S.2
  • 31
    • 0026674076 scopus 로고
    • Extragenic suppressors of paralyzed flagellar mutations in Chlamydomonas reinhardtii identify loci that alter the inner dynein arms
    • Porter, M.E., J. Power, and S.K. Dutcher. 1992. Extragenic suppressors of paralyzed flagellar mutations in Chlamydomonas reinhardtii identify loci that alter the inner dynein arms. J. Cell Biol. 118:1163-1176.
    • (1992) J. Cell Biol , vol.118 , pp. 1163-1176
    • Porter, M.E.1    Power, J.2    Dutcher, S.K.3
  • 32
    • 0037810853 scopus 로고    scopus 로고
    • A subunit of the dynein regulatory complex in Chlamydomonas is a homologue of a growth arrest-specific gene product
    • Rupp, G., and M.E. Porter. 2003. A subunit of the dynein regulatory complex in Chlamydomonas is a homologue of a growth arrest-specific gene product. J. Cell Biol. 162:47-57.
    • (2003) J. Cell Biol , vol.162 , pp. 47-57
    • Rupp, G.1    Porter, M.E.2
  • 33
    • 0001894974 scopus 로고
    • Switching mechanisms in the control of ciliary motility
    • Alan R. Liss, Inc, New York
    • Satir, P. 1985. Switching mechanisms in the control of ciliary motility. In Modern Cell Biology. Alan R. Liss, Inc., New York. 1-46.
    • (1985) Modern Cell Biology , pp. 1-46
    • Satir, P.1
  • 34
    • 0036732941 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase
    • Smith, E.F. 2002a. Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase. Mol. Biol. Cell. 13:3303-3313.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3303-3313
    • Smith, E.F.1
  • 35
    • 0036245322 scopus 로고    scopus 로고
    • Regulation of flagellar dynein by the axonemal central apparatus
    • Smith, E.F. 2002b. 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
  • 36
    • 0346732099 scopus 로고    scopus 로고
    • The radial spokes and central apparatus: Mechano-chemical transducers that regulate flagellar motility
    • Smith, E.F., and P. Yang. 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
  • 37
    • 0018908499 scopus 로고
    • Ca2+-dependent hormonal stimulation of ciliary activity
    • Verdugo, P. 1980. Ca2+-dependent hormonal stimulation of ciliary activity. Nature. 283:764-765.
    • (1980) Nature , vol.283 , pp. 764-765
    • Verdugo, P.1
  • 38
    • 33747403852 scopus 로고    scopus 로고
    • Modulation of Chlamydomonas reinhardtii flagellar motility by redox poise
    • Wakabayashi, K., and S.M. King. 2006. Modulation of Chlamydomonas reinhardtii flagellar motility by redox poise. J. Cell Biol. 173:743-754.
    • (2006) J. Cell Biol , vol.173 , pp. 743-754
    • Wakabayashi, K.1    King, S.M.2
  • 39
    • 0037422637 scopus 로고    scopus 로고
    • Asymmetry of the central apparatus defines the location of active microtubule sliding in Chlamydomonas flagella
    • Wargo, M.J., and E.F. Smith. 2003. Asymmetry of the central apparatus defines the location of active microtubule sliding in Chlamydomonas flagella. Proc. Natl. Acad. Sci. USA. 100:137-142.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 137-142
    • Wargo, M.J.1    Smith, E.F.2
  • 40
    • 3042730953 scopus 로고    scopus 로고
    • Analysis of microtubule sliding patterns in Chlamydomonas flagellar axonemes reveals dynein activity on specific doublet microtubules
    • Wargo, M.J., M.A. McPeek, and E.F. Smith. 2004. Analysis of microtubule sliding patterns in Chlamydomonas flagellar axonemes reveals dynein activity on specific doublet microtubules. J. Cell Sci. 117:2533-2544.
    • (2004) J. Cell Sci , vol.117 , pp. 2533-2544
    • Wargo, M.J.1    McPeek, M.A.2    Smith, E.F.3
  • 41
    • 27844496997 scopus 로고    scopus 로고
    • Calmodulin and PF6 are components of a complex that localizes to the C1 microtubule of the flagellar central apparatus
    • Wargo, M.J., E.E. Dymek, and E.F. Smith. 2005. Calmodulin and PF6 are components of a complex that localizes to the C1 microtubule of the flagellar central apparatus. J. Cell Sci. 118:4655-4665.
    • (2005) J. Cell Sci , vol.118 , pp. 4655-4665
    • Wargo, M.J.1    Dymek, E.E.2    Smith, E.F.3
  • 42
    • 0028205103 scopus 로고
    • Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein
    • Wilkerson, C.G., S.M. King, and G.B. Witman. 1994. Molecular analysis of the gamma heavy chain of Chlamydomonas flagellar outer-arm dynein. J. Cell Sci. 107:497-506.
    • (1994) J. Cell Sci , vol.107 , pp. 497-506
    • Wilkerson, C.G.1    King, S.M.2    Witman, G.B.3
  • 43
    • 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
  • 44
    • 0034705378 scopus 로고    scopus 로고
    • Casein kinase I is anchored on axonemal doublet microtubules and regulates flagellar dynein phosphorylation and activity
    • Yang, P., and W.S. Sale. 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
  • 45
    • 0035844885 scopus 로고    scopus 로고
    • Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes
    • Yang, P., D.R. Diener, J.L. Rosenbaum, and W.S. Sale. 2001. Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes. J. Cell Biol. 153:1315-1326.
    • (2001) J. Cell Biol , vol.153 , pp. 1315-1326
    • Yang, P.1    Diener, D.R.2    Rosenbaum, J.L.3    Sale, W.S.4
  • 47
    • 0037160085 scopus 로고    scopus 로고
    • AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase
    • Yukitake, H., M. Furusawa, T. Taira, S.M. Iguchi-Ariga, and H. Ariga. 2002. AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase. J. Biol. Chem. 277:45480-45492.
    • (2002) J. Biol. Chem , vol.277 , pp. 45480-45492
    • Yukitake, H.1    Furusawa, M.2    Taira, T.3    Iguchi-Ariga, S.M.4    Ariga, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.