메뉴 건너뛰기




Volumn 44, Issue 4, 1999, Pages 274-283

Molecular chaperones in cilia and flagella: Implications for protein turnover

Author keywords

Heat shock protein (HSP); HSP70; HSP90; TCP 1; Tubulin

Indexed keywords

CELL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90;

EID: 0032740537     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(199912)44:4<274::AID-CM5>3.0.CO;2-O     Document Type: Article
Times cited : (35)

References (46)
  • 1
    • 0023959196 scopus 로고
    • A novel hsp70-like protein (P70) is present in mouse spermatogenic cells
    • Allen RL, O'Brien, DA, Eddy, EM. 1988. A novel hsp70-like protein (P70) is present in mouse spermatogenic cells. Mol Cell Biol 8:828-832.
    • (1988) Mol Cell Biol , vol.8 , pp. 828-832
    • Allen, R.L.1    O'Brien, D.A.2    Eddy, E.M.3
  • 2
    • 0015963535 scopus 로고
    • Isolation of ciliated or unciliated basal bodies from the rabbit oviduct
    • Anderson RGW. 1974. Isolation of ciliated or unciliated basal bodies from the rabbit oviduct. J Cell Biol 60:393-404.
    • (1974) J Cell Biol , vol.60 , pp. 393-404
    • Anderson, R.G.W.1
  • 3
    • 0028867374 scopus 로고
    • Identification of a molecular chaperone in the eukaryotic flagellum and its localization to the site of microtubule assembly
    • Bloch MA, Johnson KA. 1995. Identification of a molecular chaperone in the eukaryotic flagellum and its localization to the site of microtubule assembly. J Cell Sci 108:3541-3545.
    • (1995) J Cell Sci , vol.108 , pp. 3541-3545
    • Bloch, M.A.1    Johnson, K.A.2
  • 4
    • 0030025137 scopus 로고    scopus 로고
    • Molecular chaperones and the centrosome. A role for TCP-1 in microtubule nucleation
    • Brown CR, Doxsey SJ, Hong-Brown LQ, Martin RL, Welch WJ. 1996a. Molecular chaperones and the centrosome. A role for TCP-1 in microtubule nucleation. J Biol Chem 271:824-832.
    • (1996) J Biol Chem , vol.271 , pp. 824-832
    • Brown, C.R.1    Doxsey, S.J.2    Hong-Brown, L.Q.3    Martin, R.L.4    Welch, W.J.5
  • 5
    • 0029670788 scopus 로고    scopus 로고
    • Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment
    • Brown CR, Hong-Brown LQ, Doxsey SJ, Welch WJ. 1996b. Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment. J Biol Chem 271:833-840.
    • (1996) J Biol Chem , vol.271 , pp. 833-840
    • Brown, C.R.1    Hong-Brown, L.Q.2    Doxsey, S.J.3    Welch, W.J.4
  • 6
    • 0028905287 scopus 로고
    • Neuronal aspects of cytosolic chaperonin complexes: Structures implicated in the production of functional cytoskeletal proteins
    • Carden MJ, Roobol A. 1995. Neuronal aspects of cytosolic chaperonin complexes: structures implicated in the production of functional cytoskeletal proteins. Biochem Soc Trans 23:70-76.
    • (1995) Biochem Soc Trans , vol.23 , pp. 70-76
    • Carden, M.J.1    Roobol, A.2
  • 8
    • 0029924155 scopus 로고    scopus 로고
    • The Tetrahymena chaperonin subunit CCTη is coexpressed with CCTγ gene during cilia biogenesis and cell sexual reproduction
    • Cyrne L, Guerreiro P, Cardoso AC, Rodrigues-Pousada C, Soares H. 1996. The Tetrahymena chaperonin subunit CCTη is coexpressed with CCTγ gene during cilia biogenesis and cell sexual reproduction. FEBS Lett 383:277-283.
    • (1996) FEBS Lett , vol.383 , pp. 277-283
    • Cyrne, L.1    Guerreiro, P.2    Cardoso, A.C.3    Rodrigues-Pousada, C.4    Soares, H.5
  • 9
    • 0017757111 scopus 로고
    • Flagellar elongation and shortening in Chlamydomonas. III. Structures attached to the tips of flagellar microtubules and their relationship to the directionality of flagellar microtubule assembly
    • Dentler WL, Rosenbaum JL. 1977. Flagellar elongation and shortening in Chlamydomonas. III. Structures attached to the tips of flagellar microtubules and their relationship to the directionality of flagellar microtubule assembly. J Cell Biol 74:747-759.
    • (1977) J Cell Biol , vol.74 , pp. 747-759
    • Dentler, W.L.1    Rosenbaum, J.L.2
  • 10
    • 0022553775 scopus 로고
    • Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on western blots by monoclonal antibodies
    • Dunn SD. 1986. Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on western blots by monoclonal antibodies. Anal Biochem 157:144-153.
    • (1986) Anal Biochem , vol.157 , pp. 144-153
    • Dunn, S.D.1
  • 11
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major peptides of the human erythrocyte
    • Fairbanks GT, Steck, T, Wallach, DFH. 1971. Electrophoretic analysis of the major peptides of the human erythrocyte. Biochemistry 10:2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.T.1    Steck, T.2    Wallach, D.F.H.3
  • 12
    • 0031127727 scopus 로고    scopus 로고
    • Dynamic organisation of intermediate filaments and associated proteins during the cell cycle
    • Foisner R. 1997. Dynamic organisation of intermediate filaments and associated proteins during the cell cycle. BioEssays 19:297-305.
    • (1997) BioEssays , vol.19 , pp. 297-305
    • Foisner, R.1
  • 13
    • 0025769926 scopus 로고
    • The stress (heat shock) proteins
    • Itoh H, Tashima Y. 1990. The stress (heat shock) proteins. Int J Biochem 23:1185-1191.
    • (1990) Int J Biochem , vol.23 , pp. 1185-1191
    • Itoh, H.1    Tashima, Y.2
  • 14
    • 0027098030 scopus 로고
    • Polarity of flagellar assembly in Chlamydomonas
    • Johnson KA, Rosenbaum JL. 1992. Polarity of flagellar assembly in Chlamydomonas. J Cell Biol 119:1605-1611.
    • (1992) J Cell Biol , vol.119 , pp. 1605-1611
    • Johnson, K.A.1    Rosenbaum, J.L.2
  • 15
    • 0027536953 scopus 로고
    • Flagellar regeneration in Chlamydomonas: A model system for studying organelle assembly
    • Johnson KA, Rosenbaum JL. 1993. Flagellar regeneration in Chlamydomonas: a model system for studying organelle assembly. Trends Cell Biol 3:156-161.
    • (1993) Trends Cell Biol , vol.3 , pp. 156-161
    • Johnson, K.A.1    Rosenbaum, J.L.2
  • 17
    • 0029062216 scopus 로고
    • The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol
    • Kubota H, Hynes G, Willson K. 1995. The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Eur J Biochem 230:3-16.
    • (1995) Eur J Biochem , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willson, K.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of the structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of the structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0028110026 scopus 로고
    • Molecular characterixation of the 77-kDa echinoderm microtubule-associated protein. Homology to the beta-transducin family
    • Li Q, Suprenant KA. 1994. Molecular characterixation of the 77-kDa echinoderm microtubule-associated protein. Homology to the beta-transducin family. J Biol Chem 269:31777-31784.
    • (1994) J Biol Chem , vol.269 , pp. 31777-31784
    • Li, Q.1    Suprenant, K.A.2
  • 20
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang P, MacRae TH. 1997. Molecular chaperones and the cytoskeleton. J Cell Sci 110:1431-1440.
    • (1997) J Cell Sci , vol.110 , pp. 1431-1440
    • Liang, P.1    Macrae, T.H.2
  • 21
    • 0020335261 scopus 로고
    • Structure and chemical composition of insoluble filamentous components of sperm flagellar microtubules
    • Linck RW, Langevin GL. 1982. Structure and chemical composition of insoluble filamentous components of sperm flagellar microtubules. J Cell Sci 58:1-22.
    • (1982) J Cell Sci , vol.58 , pp. 1-22
    • Linck, R.W.1    Langevin, G.L.2
  • 22
    • 0345313338 scopus 로고
    • Evidence for tektins in the cilia of the ctenophore Mnemiopsis leidyi
    • Baccetti, B, editor. New York: Raven Press Ltd.
    • Linck RW, Stephens RE, Tamm SL. 1991. Evidence for tektins in the cilia of the ctenophore Mnemiopsis leidyi. In: Baccetti, B, editor. Comparative spermatology 20 years later. New York: Raven Press Ltd. p 392-395.
    • (1991) Comparative Spermatology 20 Years Later , pp. 392-395
    • Linck, R.W.1    Stephens, R.E.2    Tamm, S.L.3
  • 23
    • 0030922765 scopus 로고    scopus 로고
    • Heterotrimeric kinesin-II is requried for the assembly of motile 9+2 axonemes on sea urchin embryos
    • Morris, RL, Scholey, JM. 1997. Heterotrimeric kinesin-II is requried for the assembly of motile 9+2 axonemes on sea urchin embryos. J Cell Biol 138:1009-1022.
    • (1997) J Cell Biol , vol.138 , pp. 1009-1022
    • Morris, R.L.1    Scholey, J.M.2
  • 24
    • 0016839045 scopus 로고
    • Regulation of tubulin during ciliary regeneration in non-growing Tetrahymena
    • Nelson EM. 1975. Regulation of tubulin during ciliary regeneration in non-growing Tetrahymena. Exp Cell Res 94:152-158.
    • (1975) Exp Cell Res , vol.94 , pp. 152-158
    • Nelson, E.M.1
  • 25
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. 1975. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007-4021.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 26
    • 0030955070 scopus 로고    scopus 로고
    • Transport of a novel complex in the cytoplasmic matrix of Chlamydomonas flagella
    • Piperno G, Mead K. 1997. Transport of a novel complex in the cytoplasmic matrix of Chlamydomonas flagella. Proc Natl Acad Sci USA 94:4457-4462.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4457-4462
    • Piperno, G.1    Mead, K.2
  • 27
    • 0023095911 scopus 로고
    • Development of microtubule capping structure in ciliated epithelial cells
    • Portman RW, Dentler WL. 1987. Development of microtubule capping structure in ciliated epithelial cells. J Cell Sci 87:85-94.
    • (1987) J Cell Sci , vol.87 , pp. 85-94
    • Portman, R.W.1    Dentler, W.L.2
  • 28
    • 0028908136 scopus 로고
    • Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in suhunit composition within single cells
    • Roobol A, Holmes FE, Hayes NVL, Baines AJ, Carden MJ. 1995. Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in suhunit composition within single cells. J Cell Sci 108:1477-1488.
    • (1995) J Cell Sci , vol.108 , pp. 1477-1488
    • Roobol, A.1    Holmes, F.E.2    Hayes, N.V.L.3    Baines, A.J.4    Carden, M.J.5
  • 29
    • 0014104888 scopus 로고
    • Flagellar regeneration of protozoan flagellates
    • Rosenbaum JL, Child FM. 1967. Flagellar regeneration of protozoan flagellates. J Cell Biol 34:345-364.
    • (1967) J Cell Biol , vol.34 , pp. 345-364
    • Rosenbaum, J.L.1    Child, F.M.2
  • 31
    • 0028172234 scopus 로고
    • A Tetrahymena orthologue of the mouse chaperonin subunit CCTγ and its coexpression with tubulin during cilia recovery
    • Soares H, Penque D, Mouta C, Rodriques-Pousada C. 1994. A Tetrahymena orthologue of the mouse chaperonin subunit CCTγ and its coexpression with tubulin during cilia recovery. J Biol Chem 269:29299-29307.
    • (1994) J Biol Chem , vol.269 , pp. 29299-29307
    • Soares, H.1    Penque, D.2    Mouta, C.3    Rodriques-Pousada, C.4
  • 32
    • 0345115707 scopus 로고    scopus 로고
    • Turnover of flagellar proteins in Chlamydomonas
    • Song L, Dentler WL. 1998. Turnover of flagellar proteins in Chlamydomonas. Mol Biol Cell 61:398a.
    • (1998) Mol Biol Cell , vol.61
    • Song, L.1    Dentler, W.L.2
  • 33
    • 0014944479 scopus 로고
    • Thermal fractionation of outer doublet microtubules into A- and B-subfiber components: A- and B-tubulin
    • Stephens RE. 1970. Thermal fractionation of outer doublet microtubules into A- and B-subfiber components: A- and B-tubulin. J Mol Biol 47:353-363.
    • (1970) J Mol Biol , vol.47 , pp. 353-363
    • Stephens, R.E.1
  • 34
    • 0025943016 scopus 로고
    • Tubulin in sea urchin embryonic cilia: Characterization of the membrane-periaxonemal matrix
    • Stephens RE. 1991. Tubulin in sea urchin embryonic cilia: characterization of the membrane-periaxonemal matrix. J Cell Sci 100:521-531.
    • (1991) J Cell Sci , vol.100 , pp. 521-531
    • Stephens, R.E.1
  • 35
    • 0026538495 scopus 로고
    • Tubulin in sea urchin embryonic cilia: Post-translational modifications during regeneration
    • Stephens RE. 1992. Tubulin in sea urchin embryonic cilia: post-translational modifications during regeneration. J Cell Sci 101:837-845.
    • (1992) J Cell Sci , vol.101 , pp. 837-845
    • Stephens, R.E.1
  • 36
    • 0028288745 scopus 로고
    • Tubulin and tektin in sea urchin embryonic cilia: Pathways of protein incorporation during turnover and regeneration
    • Stephens RE. 1994. Tubulin and tektin in sea urchin embryonic cilia: pathways of protein incorporation during turnover and regeneration. J Cell Sci 107:683-692.
    • (1994) J Cell Sci , vol.107 , pp. 683-692
    • Stephens, R.E.1
  • 37
    • 0029278729 scopus 로고
    • Ciliogenesis in sea urchin embryos: A subroutine in the program of development
    • Stephens RE. 1995a. Ciliogenesis in sea urchin embryos: a subroutine in the program of development. BioEssays 17:331-340.
    • (1995) BioEssays , vol.17 , pp. 331-340
    • Stephens, R.E.1
  • 38
    • 0029187089 scopus 로고
    • Isolation of molluscan gill cilia, sperm flagella, and axonemes
    • Stephens RE. 1995b. Isolation of molluscan gill cilia, sperm flagella, and axonemes. Meth Cell Biol 47:37-42.
    • (1995) Meth Cell Biol , vol.47 , pp. 37-42
    • Stephens, R.E.1
  • 39
    • 0030117331 scopus 로고    scopus 로고
    • Selective incorporation of architectural proteins into terminally differentiated molluscan gill cilia
    • Stephens RE. 1996. Selective incorporation of architectural proteins into terminally differentiated molluscan gill cilia. J Exp Zool 274:300-309.
    • (1996) J Exp Zool , vol.274 , pp. 300-309
    • Stephens, R.E.1
  • 40
    • 0030730983 scopus 로고    scopus 로고
    • Synthesis and turnover of embryonic sea urchin ciliary proteins during selective inhibition of tubulin synthesis and assembly
    • Stephens RE. 1997. Synthesis and turnover of embryonic sea urchin ciliary proteins during selective inhibition of tubulin synthesis and assembly. Mol Biol Cell 8:2187-2198.
    • (1997) Mol Biol Cell , vol.8 , pp. 2187-2198
    • Stephens, R.E.1
  • 41
    • 0032754579 scopus 로고    scopus 로고
    • Turnover of tubulin in ciliary outer doublet microtubules
    • in press
    • Stephens RE. 1999. Turnover of tubulin in ciliary outer doublet microtubules. Cell Struct Funct (in press).
    • (1999) Cell Struct Funct
    • Stephens, R.E.1
  • 42
    • 0031950455 scopus 로고    scopus 로고
    • Tektins as structural determinants in basal bodies
    • Stephens RE, Lemieux NA. 1998. Tektins as structural determinants in basal bodies. Cell Motil Cytoskeleton 40:379-392.
    • (1998) Cell Motil Cytoskeleton , vol.40 , pp. 379-392
    • Stephens, R.E.1    Lemieux, N.A.2
  • 43
    • 0024623686 scopus 로고
    • Retention of ciliary ninefold structure after removal of microtubules
    • Stephens RE, Oleszko S, Linck RW. 1989. Retention of ciliary ninefold structure after removal of microtubules. J Cell Sci 92:391-402.
    • (1989) J Cell Sci , vol.92 , pp. 391-402
    • Stephens, R.E.1    Oleszko, S.2    Linck, R.W.3
  • 44
    • 0023285114 scopus 로고
    • Temperature and pH govern the self assembly of microtubules from unfertilized sea-urchin eggs
    • Suprenant KA, Marsh JC. 1987. Temperature and pH govern the self assembly of microtubules from unfertilized sea-urchin eggs. J Cell Sci 87:71-84.
    • (1987) J Cell Sci , vol.87 , pp. 71-84
    • Suprenant, K.A.1    Marsh, J.C.2
  • 45
    • 0030793697 scopus 로고    scopus 로고
    • HSP70 and HSP90 homologs are associated with tubulin in hetero-oligomeric complexes, cilia and the cortex of Tetrahymena
    • Williams NE, Nelsen EM. 1997. HSP70 and HSP90 homologs are associated with tubulin in hetero-oligomeric complexes, cilia and the cortex of Tetrahymena. J Cell Sci 110:1665-1672.
    • (1997) J Cell Sci , vol.110 , pp. 1665-1672
    • Williams, N.E.1    Nelsen, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.