메뉴 건너뛰기




Volumn 118, Issue 5, 2005, Pages 1007-1020

MKKS/BBS6, a divergent chaperonin-like protein linked to the obesity disorder Bardet-Biedl syndrome, is a novel centrosomal component required for cytokinesis

Author keywords

Bardet Biedl syndrome; BBS6; Centrosome; Chaperonin; Cytokinesis; MKKS

Indexed keywords

CHAPERONE; CHAPERONIN; PROTEIN BBS6; PROTEIN MKKS; RNA INDUCED SILENCING COMPLEX; UNCLASSIFIED DRUG;

EID: 20144386878     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01676     Document Type: Article
Times cited : (141)

References (45)
  • 2
    • 0033598189 scopus 로고    scopus 로고
    • Recurrent paralogy in the evolution of archaeal chaperonins
    • Archibald, J. M., Logsdon, J. M. and Doolittle, W. F. (1999). Recurrent paralogy in the evolution of archaeal chaperonins. Curr. Biol. 9, 1053-1056.
    • (1999) Curr. Biol. , vol.9 , pp. 1053-1056
    • Archibald, J.M.1    Logsdon, J.M.2    Doolittle, W.F.3
  • 3
    • 0033800261 scopus 로고    scopus 로고
    • Origin and evolution of eukaryotic chaperonins: Phylogenetic evidence for ancient duplications in CCT genes
    • Archibald, J. M., Logsdon, J. M., Jr and Doolittle, W. F. (2000). Origin and evolution of eukaryotic chaperonins: phylogenetic evidence for ancient duplications in CCT genes. Mol. Biol. Evol. 17, 1456-1466.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 1456-1466
    • Archibald, J.M.1    Logsdon Jr., J.M.2    Doolittle, W.F.3
  • 4
    • 0037371508 scopus 로고    scopus 로고
    • Identification of a novel Bardet-Biedl syndrome protein, BBS7, that shares structural features with BBS1 and BBS2
    • Badano, J. L., Ansley, S. J., Leitch, C. C., Lewis, R. A., Lupski, J. R. and Katsanis, N. (2003). Identification of a novel Bardet-Biedl syndrome protein, BBS7, that shares structural features with BBS1 and BBS2. Am. J. Hum. Genet. 72, 650-658.
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 650-658
    • Badano, J.L.1    Ansley, S.J.2    Leitch, C.C.3    Lewis, R.A.4    Lupski, J.R.5    Katsanis, N.6
  • 5
    • 0033062278 scopus 로고    scopus 로고
    • New criteria for improved diagnosis of Bardet-Biedl syndrome: Results of a population survey
    • Beales, P. L., Elcioglu, N., Woolf, A. S., Parker, D. and Hinter, F. A. (1999). New criteria for improved diagnosis of Bardet-Biedl syndrome: results of a population survey. J. Med. Genet. 36, 437-446.
    • (1999) J. Med. Genet. , vol.36 , pp. 437-446
    • Beales, P.L.1    Elcioglu, N.2    Woolf, A.S.3    Parker, D.4    Hinter, F.A.5
  • 7
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • Brummelkamp, T. R., Bernards, R. and Agami, R. (2002). A system for stable expression of short interfering RNAs in mammalian cells. Science 296, 550-553.
    • (2002) Science , vol.296 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 8
    • 0035239206 scopus 로고    scopus 로고
    • Structural comparison of prokaryotic and eukaryotic chaperonins
    • Carrascosa, J. L., Llorca, O. and Valpuesta, J. M. (2001). Structural comparison of prokaryotic and eukaryotic chaperonins. Micron 32, 43-50.
    • (2001) Micron. , vol.32 , pp. 43-50
    • Carrascosa, J.L.1    Llorca, O.2    Valpuesta, J.M.3
  • 10
    • 0037191046 scopus 로고    scopus 로고
    • Assembly of centrosomal proteins and microtubule organization depends on PCM-1
    • Dammermann, A. and Merdes, A. (2002). Assembly of centrosomal proteins and microtubule organization depends on PCM-1. J. Cell Biol. 159, 255-266.
    • (2002) J. Cell Biol. , vol.159 , pp. 255-266
    • Dammermann, A.1    Merdes, A.2
  • 11
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel, L., Lowe, J., Stock, D., Steller, K. O., Huber, H., Huber, R. and Steinbacher, S. (1998). Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Steller, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 13
    • 0030807655 scopus 로고    scopus 로고
    • BIONJ: An improved version of the NJ algorithm based on a simple model of sequence data
    • Gascuel, O. (1997). BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. Mol. Biol. Evol. 14, 685-695.
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 685-695
    • Gascuel, O.1
  • 14
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
    • Gutsche, I., Essen, L. O. and Baumeister, W. (1999). Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. J. Mol. Biol. 293, 295-312.
    • (1999) J. Mol. Biol. , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.O.2    Baumeister, W.3
  • 15
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U. and Hayer-Hartl, M. (2002). Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 16
    • 0027925641 scopus 로고
    • Protein folding in the cell: Functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
    • discussion 325-316
    • Horwich, A. L. and Willison, K. R. (1993). Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. Philos. Trans R Soc. Lond. B Biol. Sci. 339, 313-325; discussion 325-316.
    • (1993) Philos. Trans. R Soc. Lond. B Biol. Sci. , vol.339 , pp. 313-325
    • Horwich, A.L.1    Willison, K.R.2
  • 17
    • 0028895618 scopus 로고
    • Antibody characterisation of two distinct conformations of the chaperonin-containing TCP-1 from mouse testis
    • Hynes, G., Kubota, H. and Willison, K. R. (1995). Antibody characterisation of two distinct conformations of the chaperonin-containing TCP-1 from mouse testis. FEBS Lett. 358 129-132.
    • (1995) FEBS Lett. , vol.358 , pp. 129-132
    • Hynes, G.1    Kubota, H.2    Willison, K.R.3
  • 18
    • 1842579395 scopus 로고    scopus 로고
    • The oligogenic properties of Bardet-Biedl syndrome
    • Spec. No. 1
    • Katsanis, N. (2004). The oligogenic properties of Bardet-Biedl syndrome. Hum. Mol. Genet. 13, Spec. No. 1, R65-71.
    • (2004) Hum. Mol. Genet. , vol.13
    • Katsanis, N.1
  • 20
    • 20244381625 scopus 로고    scopus 로고
    • The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression
    • Kim, J. C., Badano, J. L., Sibold, S., Esmail, M. A., Hill, J., Hoskins, B. E., Leitch, C. C., Venner, K., Ansley, S. J., Ross, A. J. et al. (2004). The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression. Nat. Genet. 36, 462-470.
    • (2004) Nat. Genet. , vol.36 , pp. 462-470
    • Kim, J.C.1    Badano, J.L.2    Sibold, S.3    Esmail, M.A.4    Hill, J.5    Hoskins, B.E.6    Leitch, C.C.7    Venner, K.8    Ansley, S.J.9    Ross, A.J.10
  • 21
    • 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. and Willison, 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    Willison, K.3
  • 23
    • 0034611628 scopus 로고    scopus 로고
    • Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT
    • Leroux, M. R. and Hartl, F. U. (2000). Protein folding: versatility of the cytosolic chaperonin TRiC/CCT. Curr. Biol. 10 R260-264.
    • (2000) Curr. Biol. , vol.10
    • Leroux, M.R.1    Hartl, F.U.2
  • 25
    • 0031930213 scopus 로고    scopus 로고
    • Autoantibodies to a group of centrosomal proteins in human autoimmune sera reactive with the centrosome
    • Mack, G. J., Rees, J., Sandblom, O., Balczon, R., Fritzler, M. J. and Rattner, J. B. (1998). Autoantibodies to a group of centrosomal proteins in human autoimmune sera reactive with the centrosome. Arthritis Rheum. 41, 551-558.
    • (1998) Arthritis Rheum. , vol.41 , pp. 551-558
    • Mack, G.J.1    Rees, J.2    Sandblom, O.3    Balczon, R.4    Fritzler, M.J.5    Rattner, J.B.6
  • 26
    • 0038737003 scopus 로고    scopus 로고
    • Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    • Meyer, A. S., Gillespie, J. R., Walther, D., Millet, I. S., Doniach, S. and Frydman, J. (2003). Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113, 369-381.
    • (2003) Cell , vol.113 , pp. 369-381
    • Meyer, A.S.1    Gillespie, J.R.2    Walther, D.3    Millet, I.S.4    Doniach, S.5    Frydman, J.6
  • 31
    • 0034575968 scopus 로고    scopus 로고
    • Membrane traffic and cytokinesis
    • O'Halloran, T. J. (2000). Membrane traffic and cytokinesis. Traffic 1, 921-926.
    • (2000) Traffic , vol.1 , pp. 921-926
    • O'Halloran, T.J.1
  • 32
    • 0033799252 scopus 로고    scopus 로고
    • A subset of centrosomal proteins are arranged in a tubular conformation that is reproduced during centrosome duplication
    • Ou, Y. Y. and Rattner, J. B. (2000). A subset of centrosomal proteins are arranged in a tubular conformation that is reproduced during centrosome duplication. Cell Motil. Cytoskeleton 47, 13-24.
    • (2000) Cell Motil. Cytoskeleton , vol.47 , pp. 13-24
    • Ou, Y.Y.1    Rattner, J.B.2
  • 34
    • 0035983515 scopus 로고    scopus 로고
    • Crystal structure of the CCTγ apical domain: Implications for substrate binding to the eukaryotic cytosolic chaperonin
    • Pappenberger, G., Wilsher, J. A., Roe, S. M., Counsell, D. J., Willison, K. R. and Pearl, L. H. (2002). Crystal structure of the CCTγ apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. J. Mol. Biol. 318, 1367-1379.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1367-1379
    • Pappenberger, G.1    Wilsher, J.A.2    Roe, S.M.3    Counsell, D.J.4    Willison, K.R.5    Pearl, L.H.6
  • 35
    • 0035936920 scopus 로고    scopus 로고
    • Centrosome-dependent exit of cytokinesis in animal cells
    • Piel, M., Nordberg, J., Euteneuer, U. and Bornens, M. (2001). Centrosome-dependent exit of cytokinesis in animal cells. Science 291, 1550-1553.
    • (2001) Science , vol.291 , pp. 1550-1553
    • Piel, M.1    Nordberg, J.2    Euteneuer, U.3    Bornens, M.4
  • 36
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
    • Siegers, K., Waldmann, T., Leroux, M. R., Grein, K., Shevchenko, A., Schiebel, E. and Hartl, F. U. (1999). Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18, 75-84.
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5    Schiebel, E.6    Hartl, F.U.7
  • 37
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert, R., Leroux, M. R., Scheufler, C., Hartl, F. U. and Moarefi, I. (2000). Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621-632.
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 40
    • 0029836454 scopus 로고    scopus 로고
    • Quartet puzzling: A quartet maximum-likelihood method for reconstructing tree topologies
    • Strimmer, K. and von Haeseler, A. (1996). Quartet puzzling: a quartet maximum-likelihood method for reconstructing tree topologies. Mol. Biol. Evol. 13, 964-969.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 964-969
    • Strimmer, K.1    von Haeseler, A.2
  • 41
    • 0037424258 scopus 로고    scopus 로고
    • Polo-like kinase 1 and Chk2 interact and co-localize to centrosomes and the midbody
    • Tsvetkov, L., Xu, X., Li, J. and Stern, D. F. (2003). Polo-like kinase 1 and Chk2 interact and co-localize to centrosomes and the midbody. J. Biol. Chem. 278, 8468-8475.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8468-8475
    • Tsvetkov, L.1    Xu, X.2    Li, J.3    Stern, D.F.4
  • 43
  • 44
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
    • Vaughan, K. T. and Vallee, R. B. (1995). Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. J. Cell Biol. 131, 1507-1516.
    • (1995) J. Cell Biol. , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 45
    • 0031791650 scopus 로고    scopus 로고
    • The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding
    • Weber, F., Keppel, F., Georgopoulos, C., Hayer-Hartl, M. K. and Hartl, F. U. (1998). The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding. Nat. Struct. Biol. 5, 977-985.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 977-985
    • Weber, F.1    Keppel, F.2    Georgopoulos, C.3    Hayer-Hartl, M.K.4    Hartl, F.U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.