메뉴 건너뛰기




Volumn 2, Issue 1, 2013, Pages

CP110 and its network of partners coordinately regulate cilia assembly

Author keywords

BBSome; Centrosomes; Cep290; Cilia; Ciliogenesis; CP110; IFT; Protein network

Indexed keywords

CELL PROTEIN; INTRAFLAGELLAR TRANSPORT PROTEIN; PROTEIN CEP290; PROTEIN CP110; UNCLASSIFIED DRUG;

EID: 84901940697     PISSN: None     EISSN: 20462530     Source Type: Journal    
DOI: 10.1186/2046-2530-2-9     Document Type: Review
Times cited : (65)

References (86)
  • 1
    • 84857691732 scopus 로고    scopus 로고
    • Deconstructing the centriole: structure and number control
    • 10.1016/j.ceb.2012.01.003, 22321829
    • Brito DA, Gouveia SM, Bettencourt-Dias M. Deconstructing the centriole: structure and number control. Curr Opin Cell Biol 2012, 24:4-13. 10.1016/j.ceb.2012.01.003, 22321829.
    • (2012) Curr Opin Cell Biol , vol.24 , pp. 4-13
    • Brito, D.A.1    Gouveia, S.M.2    Bettencourt-Dias, M.3
  • 2
    • 80053553994 scopus 로고    scopus 로고
    • The centrosome cycle: centriole biogenesis, duplication and inherent asymmetries
    • 10.1038/ncb2345, 21968988
    • Nigg EA, Stearns T. The centrosome cycle: centriole biogenesis, duplication and inherent asymmetries. Nat Cell Biol 2011, 13:1154-1160. 10.1038/ncb2345, 21968988.
    • (2011) Nat Cell Biol , vol.13 , pp. 1154-1160
    • Nigg, E.A.1    Stearns, T.2
  • 4
    • 70350771277 scopus 로고    scopus 로고
    • Centrioles, centrosomes, and cilia in health and disease
    • 10.1016/j.cell.2009.10.036, 19914163
    • Nigg EA, Raff JW. Centrioles, centrosomes, and cilia in health and disease. Cell 2009, 139:663-678. 10.1016/j.cell.2009.10.036, 19914163.
    • (2009) Cell , vol.139 , pp. 663-678
    • Nigg, E.A.1    Raff, J.W.2
  • 5
    • 79956193249 scopus 로고    scopus 로고
    • Regulating the transition from centriole to basal body
    • 10.1083/jcb.201101005, 3087006, 21536747
    • Kobayashi T, Dynlacht BD. Regulating the transition from centriole to basal body. J Cell Biol 2011, 193:435-444. 10.1083/jcb.201101005, 3087006, 21536747.
    • (2011) J Cell Biol , vol.193 , pp. 435-444
    • Kobayashi, T.1    Dynlacht, B.D.2
  • 6
    • 84856454196 scopus 로고    scopus 로고
    • A structural road map to unveil basal body composition and assembly
    • 10.1038/emboj.2011.474, 3273397, 22293831
    • Jana SC, Machado P, Bettencourt-Dias M. A structural road map to unveil basal body composition and assembly. EMBO J 2012, 31:519-521. 10.1038/emboj.2011.474, 3273397, 22293831.
    • (2012) EMBO J , vol.31 , pp. 519-521
    • Jana, S.C.1    Machado, P.2    Bettencourt-Dias, M.3
  • 8
    • 84875221634 scopus 로고    scopus 로고
    • Kif3a interacts with dynactin subunit p150 Glued to organize centriole sub-distal appendages
    • 10.1038/emboj.2013.3, 23386061
    • Kodani A, Salome Sirerol-Piquer M, Seol A, Garcia-Verdugo JM, Reiter JF. Kif3a interacts with dynactin subunit p150 Glued to organize centriole sub-distal appendages. EMBO J 2013, 32:597-607. 10.1038/emboj.2013.3, 23386061.
    • (2013) EMBO J , vol.32 , pp. 597-607
    • Kodani, A.1    Salome Sirerol-Piquer, M.2    Seol, A.3    Garcia-Verdugo, J.M.4    Reiter, J.F.5
  • 9
    • 84867878514 scopus 로고    scopus 로고
    • The centrosome regulates the Rab11-dependent recycling endosome pathway at appendages of the mother centriole
    • 10.1016/j.cub.2012.08.022, 22981775
    • Hehnly H, Chen CT, Powers CM, Liu HL, Doxsey S. The centrosome regulates the Rab11-dependent recycling endosome pathway at appendages of the mother centriole. Curr Biol 2012, 22:1944-1950. 10.1016/j.cub.2012.08.022, 22981775.
    • (2012) Curr Biol , vol.22 , pp. 1944-1950
    • Hehnly, H.1    Chen, C.T.2    Powers, C.M.3    Liu, H.L.4    Doxsey, S.5
  • 10
    • 84856360903 scopus 로고    scopus 로고
    • Stages of ciliogenesis and regulation of ciliary length
    • 10.1016/j.diff.2011.11.015, 3269565, 22178116
    • Avasthi P, Marshall WF. Stages of ciliogenesis and regulation of ciliary length. Differentiation 2012, 83:S30-S42. 10.1016/j.diff.2011.11.015, 3269565, 22178116.
    • (2012) Differentiation , vol.83
    • Avasthi, P.1    Marshall, W.F.2
  • 12
    • 84863327175 scopus 로고    scopus 로고
    • The base of the cilium: roles for transition fibers and the transition zone in ciliary formation, maintenance and compartmentalization
    • 10.1038/embor.2012.73, 3388784, 22653444
    • Reiter JF, Blacque OE, Leroux MR. The base of the cilium: roles for transition fibers and the transition zone in ciliary formation, maintenance and compartmentalization. EMBO Rep 2012, 13:608-618. 10.1038/embor.2012.73, 3388784, 22653444.
    • (2012) EMBO Rep , vol.13 , pp. 608-618
    • Reiter, J.F.1    Blacque, O.E.2    Leroux, M.R.3
  • 13
    • 77957682469 scopus 로고    scopus 로고
    • TULP3 bridges the IFT-A complex and membrane phosphoinositides to promote trafficking of G protein-coupled receptors into primary cilia
    • 10.1101/gad.1966210, 2947770, 20889716
    • Mukhopadhyay S, Wen X, Chih B, Nelson CD, Lane WS, Scales SJ, Jackson PK. TULP3 bridges the IFT-A complex and membrane phosphoinositides to promote trafficking of G protein-coupled receptors into primary cilia. Genes Dev 2010, 24:2180-2193. 10.1101/gad.1966210, 2947770, 20889716.
    • (2010) Genes Dev , vol.24 , pp. 2180-2193
    • Mukhopadhyay, S.1    Wen, X.2    Chih, B.3    Nelson, C.D.4    Lane, W.S.5    Scales, S.J.6    Jackson, P.K.7
  • 14
    • 84865803552 scopus 로고    scopus 로고
    • The BBSome controls IFT assembly and turnaround in cilia
    • 10.1038/ncb2560, 3434251, 22922713
    • Wei Q, Zhang Y, Li Y, Zhang Q, Ling K, Hu J. The BBSome controls IFT assembly and turnaround in cilia. Nat Cell Biol 2012, 14:950-957. 10.1038/ncb2560, 3434251, 22922713.
    • (2012) Nat Cell Biol , vol.14 , pp. 950-957
    • Wei, Q.1    Zhang, Y.2    Li, Y.3    Zhang, Q.4    Ling, K.5    Hu, J.6
  • 15
    • 84865772673 scopus 로고    scopus 로고
    • Regulating intraflagellar transport
    • 10.1038/ncb2569, 22945257
    • Pedersen LB, Christensen ST. Regulating intraflagellar transport. Nat Cell Biol 2012, 14:904-906. 10.1038/ncb2569, 22945257.
    • (2012) Nat Cell Biol , vol.14 , pp. 904-906
    • Pedersen, L.B.1    Christensen, S.T.2
  • 16
    • 84864021901 scopus 로고    scopus 로고
    • The IFT-A complex regulates Shh signaling through cilia structure and membrane protein trafficking
    • 10.1083/jcb.201110049, 3373400, 22689656
    • Liem KF, Ashe A, He M, Satir P, Moran J, Beier D, Wicking C, Anderson KV. The IFT-A complex regulates Shh signaling through cilia structure and membrane protein trafficking. J Cell Biol 2012, 197:789-800. 10.1083/jcb.201110049, 3373400, 22689656.
    • (2012) J Cell Biol , vol.197 , pp. 789-800
    • Liem, K.F.1    Ashe, A.2    He, M.3    Satir, P.4    Moran, J.5    Beier, D.6    Wicking, C.7    Anderson, K.V.8
  • 17
    • 79953032655 scopus 로고    scopus 로고
    • Ciliogenesis: building the cell's antenna
    • 10.1038/nrm3085, 21427764
    • Ishikawa H, Marshall WF. Ciliogenesis: building the cell's antenna. Nat Rev Mol Cell Biol 2011, 12:222-234. 10.1038/nrm3085, 21427764.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 222-234
    • Ishikawa, H.1    Marshall, W.F.2
  • 18
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • 10.1038/nature02166, 14654843
    • Andersen JS, Wilkinson CJ, Mayor T, Mortensen P, Nigg EA, Mann M. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 2003, 426:570-574. 10.1038/nature02166, 14654843.
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 20
    • 2342501364 scopus 로고    scopus 로고
    • Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene
    • 10.1016/S0092-8674(04)00450-7, 15137946
    • Li JB, Gerdes JM, Haycraft CJ, Fan Y, Teslovich TM, May-Simera H, Li H, Blacque OE, Li L, Leitch CC, et al. Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene. Cell 2004, 117:541-552. 10.1016/S0092-8674(04)00450-7, 15137946.
    • (2004) Cell , vol.117 , pp. 541-552
    • Li, J.B.1    Gerdes, J.M.2    Haycraft, C.J.3    Fan, Y.4    Teslovich, T.M.5    May-Simera, H.6    Li, H.7    Blacque, O.E.8    Li, L.9    Leitch, C.C.10
  • 21
    • 35548974826 scopus 로고    scopus 로고
    • Cep164, a novel centriole appendage protein required for primary cilium formation
    • 10.1083/jcb.200707181, 2064767, 17954613
    • Graser S, Stierhof YD, Lavoie SB, Gassner OS, Lamla S, Le Clech M, Nigg EA. Cep164, a novel centriole appendage protein required for primary cilium formation. J Cell Biol 2007, 179:321-330. 10.1083/jcb.200707181, 2064767, 17954613.
    • (2007) J Cell Biol , vol.179 , pp. 321-330
    • Graser, S.1    Stierhof, Y.D.2    Lavoie, S.B.3    Gassner, O.S.4    Lamla, S.5    Le Clech, M.6    Nigg, E.A.7
  • 22
    • 77951128108 scopus 로고    scopus 로고
    • Functional genomic screen for modulators of ciliogenesis and cilium length
    • 10.1038/nature08895, 2929961, 20393563
    • Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG. Functional genomic screen for modulators of ciliogenesis and cilium length. Nature 2010, 464:1048-1051. 10.1038/nature08895, 2929961, 20393563.
    • (2010) Nature , vol.464 , pp. 1048-1051
    • Kim, J.1    Lee, J.E.2    Heynen-Genel, S.3    Suyama, E.4    Ono, K.5    Lee, K.6    Ideker, T.7    Aza-Blanc, P.8    Gleeson, J.G.9
  • 23
    • 34547939469 scopus 로고    scopus 로고
    • Cep97 and CP110 suppress a cilia assembly program
    • 10.1016/j.cell.2007.06.027, 17719545
    • Spektor A, Tsang WY, Khoo D, Dynlacht BD. Cep97 and CP110 suppress a cilia assembly program. Cell 2007, 130:678-690. 10.1016/j.cell.2007.06.027, 17719545.
    • (2007) Cell , vol.130 , pp. 678-690
    • Spektor, A.1    Tsang, W.Y.2    Khoo, D.3    Dynlacht, B.D.4
  • 24
    • 82555165884 scopus 로고    scopus 로고
    • Inflammation-mediated upregulation of centrosomal protein 110, a negative modulator of ciliogenesis, in patients with chronic rhinosinusitis
    • e1201, 10.1016/j.jaci.2011.09.001, 21982113
    • Lai Y, Chen B, Shi J, Palmer JN, Kennedy DW, Cohen NA. Inflammation-mediated upregulation of centrosomal protein 110, a negative modulator of ciliogenesis, in patients with chronic rhinosinusitis. J Allergy Clin Immunol 2011, 128:1207-1215. e1201, 10.1016/j.jaci.2011.09.001, 21982113.
    • (2011) J Allergy Clin Immunol , vol.128 , pp. 1207-1215
    • Lai, Y.1    Chen, B.2    Shi, J.3    Palmer, J.N.4    Kennedy, D.W.5    Cohen, N.A.6
  • 25
    • 48549102438 scopus 로고    scopus 로고
    • CP110 suppresses primary cilia formation through its interaction with CEP290, a protein deficient in human ciliary disease
    • 10.1016/j.devcel.2008.07.004, 18694559
    • Tsang WY, Bossard C, Khanna H, Peranen J, Swaroop A, Malhotra V, Dynlacht BD. CP110 suppresses primary cilia formation through its interaction with CEP290, a protein deficient in human ciliary disease. Dev Cell 2008, 15:187-197. 10.1016/j.devcel.2008.07.004, 18694559.
    • (2008) Dev Cell , vol.15 , pp. 187-197
    • Tsang, W.Y.1    Bossard, C.2    Khanna, H.3    Peranen, J.4    Swaroop, A.5    Malhotra, V.6    Dynlacht, B.D.7
  • 26
    • 33746659376 scopus 로고    scopus 로고
    • CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability
    • 10.1091/mbc.E06-04-0371, 1525247, 16760425
    • Tsang WY, Spektor A, Luciano DJ, Indjeian VB, Chen Z, Salisbury JL, Sanchez I, Dynlacht BD. CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability. Mol Biol Cell 2006, 17:3423-3434. 10.1091/mbc.E06-04-0371, 1525247, 16760425.
    • (2006) Mol Biol Cell , vol.17 , pp. 3423-3434
    • Tsang, W.Y.1    Spektor, A.2    Luciano, D.J.3    Indjeian, V.B.4    Chen, Z.5    Salisbury, J.L.6    Sanchez, I.7    Dynlacht, B.D.8
  • 27
    • 65649100187 scopus 로고    scopus 로고
    • Cep76, a centrosomal protein that specifically restrains centriole reduplication
    • 10.1016/j.devcel.2009.03.004, 19460342
    • Tsang WY, Spektor A, Vijayakumar S, Bista BR, Li J, Sanchez I, Duensing S, Dynlacht BD. Cep76, a centrosomal protein that specifically restrains centriole reduplication. Dev Cell 2009, 16:649-660. 10.1016/j.devcel.2009.03.004, 19460342.
    • (2009) Dev Cell , vol.16 , pp. 649-660
    • Tsang, W.Y.1    Spektor, A.2    Vijayakumar, S.3    Bista, B.R.4    Li, J.5    Sanchez, I.6    Duensing, S.7    Dynlacht, B.D.8
  • 28
    • 79958250238 scopus 로고    scopus 로고
    • Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis
    • 10.1016/j.cell.2011.04.028, 21620453
    • Kobayashi T, Tsang WY, Li J, Lane W, Dynlacht BD. Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis. Cell 2011, 145:914-925. 10.1016/j.cell.2011.04.028, 21620453.
    • (2011) Cell , vol.145 , pp. 914-925
    • Kobayashi, T.1    Tsang, W.Y.2    Li, J.3    Lane, W.4    Dynlacht, B.D.5
  • 29
    • 0036745763 scopus 로고    scopus 로고
    • CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells
    • 10.1016/S1534-5807(02)00258-7, 12361598
    • Chen Z, Indjeian VB, McManus M, Wang L, Dynlacht BD. CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells. Dev Cell 2002, 3:339-350. 10.1016/S1534-5807(02)00258-7, 12361598.
    • (2002) Dev Cell , vol.3 , pp. 339-350
    • Chen, Z.1    Indjeian, V.B.2    McManus, M.3    Wang, L.4    Dynlacht, B.D.5
  • 30
    • 84862779190 scopus 로고    scopus 로고
    • Neurl4, a novel daughter centriole protein, prevents formation of ectopic microtubule organizing centers
    • 10.1038/embor.2012.40, 3367236, 22441691
    • Li J, Kim S, Kobayashi T, Liang FX, Korzeniewski N, Duensing S, Dynlacht BD. Neurl4, a novel daughter centriole protein, prevents formation of ectopic microtubule organizing centers. EMBO Rep 2012, 13:547-553. 10.1038/embor.2012.40, 3367236, 22441691.
    • (2012) EMBO Rep , vol.13 , pp. 547-553
    • Li, J.1    Kim, S.2    Kobayashi, T.3    Liang, F.X.4    Korzeniewski, N.5    Duensing, S.6    Dynlacht, B.D.7
  • 31
    • 84862321083 scopus 로고    scopus 로고
    • Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture
    • 3433907, 22261722
    • Al-Hakim AK, Bashkurov M, Gingras AC, Durocher D, Pelletier L. Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture. Mol Cell Proteomics 2012, 11:M111 014233. 3433907, 22261722.
    • (2012) Mol Cell Proteomics , vol.11
    • Al-Hakim, A.K.1    Bashkurov, M.2    Gingras, A.C.3    Durocher, D.4    Pelletier, L.5
  • 34
    • 67349228738 scopus 로고    scopus 로고
    • Overly long centrioles and defective cell division upon excess of the SAS-4-related protein CPAP
    • 10.1016/j.cub.2009.05.018, 2993638, 19481460
    • Kohlmaier G, Loncarek J, Meng X, McEwen BF, Mogensen MM, Spektor A, Dynlacht BD, Khodjakov A, Gonczy P. Overly long centrioles and defective cell division upon excess of the SAS-4-related protein CPAP. Curr Biol 2009, 19:1012-1018. 10.1016/j.cub.2009.05.018, 2993638, 19481460.
    • (2009) Curr Biol , vol.19 , pp. 1012-1018
    • Kohlmaier, G.1    Loncarek, J.2    Meng, X.3    McEwen, B.F.4    Mogensen, M.M.5    Spektor, A.6    Dynlacht, B.D.7    Khodjakov, A.8    Gonczy, P.9
  • 35
    • 67349279485 scopus 로고    scopus 로고
    • CPAP is a cell-cycle regulated protein that controls centriole length
    • 10.1038/ncb1889, 19503075
    • Tang CJ, Fu RH, Wu KS, Hsu WB, Tang TK. CPAP is a cell-cycle regulated protein that controls centriole length. Nat Cell Biol 2009, 11:825-831. 10.1038/ncb1889, 19503075.
    • (2009) Nat Cell Biol , vol.11 , pp. 825-831
    • Tang, C.J.1    Fu, R.H.2    Wu, K.S.3    Hsu, W.B.4    Tang, T.K.5
  • 36
    • 84858702711 scopus 로고    scopus 로고
    • Klp10A, a microtubule-depolymerizing kinesin-13, cooperates with CP110 to control Drosophila centriole length
    • 10.1016/j.cub.2012.01.046, 22365849
    • Delgehyr N, Rangone H, Fu J, Mao G, Tom B, Riparbelli MG, Callaini G, Glover DM. Klp10A, a microtubule-depolymerizing kinesin-13, cooperates with CP110 to control Drosophila centriole length. Curr Biol 2012, 22:502-509. 10.1016/j.cub.2012.01.046, 22365849.
    • (2012) Curr Biol , vol.22 , pp. 502-509
    • Delgehyr, N.1    Rangone, H.2    Fu, J.3    Mao, G.4    Tom, B.5    Riparbelli, M.G.6    Callaini, G.7    Glover, D.M.8
  • 37
    • 84874990849 scopus 로고    scopus 로고
    • USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110
    • 10.1038/nature11941, 23486064
    • Li J, D'Angiolella V, Seeley ES, Kim S, Kobayashi T, Fu W, Campos EI, Pagano M, Dynlacht BD. USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110. Nature 2013, 495:255-259. 10.1038/nature11941, 23486064.
    • (2013) Nature , vol.495 , pp. 255-259
    • Li, J.1    D'Angiolella, V.2    Seeley, E.S.3    Kim, S.4    Kobayashi, T.5    Fu, W.6    Campos, E.I.7    Pagano, M.8    Dynlacht, B.D.9
  • 38
    • 77954240714 scopus 로고    scopus 로고
    • SCF (Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation
    • 10.1038/nature09140, 2946399, 20596027
    • D'Angiolella V, Donato V, Vijayakumar S, Saraf A, Florens L, Washburn MP, Dynlacht B, Pagano M. SCF (Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. Nature 2010, 466:138-142. 10.1038/nature09140, 2946399, 20596027.
    • (2010) Nature , vol.466 , pp. 138-142
    • D'Angiolella, V.1    Donato, V.2    Vijayakumar, S.3    Saraf, A.4    Florens, L.5    Washburn, M.P.6    Dynlacht, B.7    Pagano, M.8
  • 39
    • 84863198374 scopus 로고    scopus 로고
    • MiR-129-3p controls cilia assembly by regulating CP110 and actin dynamics
    • 10.1038/ncb2512, 22684256
    • Cao J, Shen Y, Zhu L, Xu Y, Zhou Y, Wu Z, Li Y, Yan X, Zhu X. miR-129-3p controls cilia assembly by regulating CP110 and actin dynamics. Nat Cell Biol 2012, 14:697-706. 10.1038/ncb2512, 22684256.
    • (2012) Nat Cell Biol , vol.14 , pp. 697-706
    • Cao, J.1    Shen, Y.2    Zhu, L.3    Xu, Y.4    Zhou, Y.5    Wu, Z.6    Li, Y.7    Yan, X.8    Zhu, X.9
  • 40
    • 84869069719 scopus 로고    scopus 로고
    • The spinocerebellar ataxia-associated gene Tau tubulin kinase 2 controls the initiation of ciliogenesis
    • 10.1016/j.cell.2012.10.010, 23141541
    • Goetz SC, Liem KF, Anderson KV. The spinocerebellar ataxia-associated gene Tau tubulin kinase 2 controls the initiation of ciliogenesis. Cell 2012, 151:847-858. 10.1016/j.cell.2012.10.010, 23141541.
    • (2012) Cell , vol.151 , pp. 847-858
    • Goetz, S.C.1    Liem, K.F.2    Anderson, K.V.3
  • 43
    • 84874574400 scopus 로고    scopus 로고
    • Centriole distal appendages promote membrane docking, leading to cilia initiation
    • 10.1101/gad.207043.112, 3566309, 23348840
    • Tanos BE, Yang HJ, Soni R, Wang WJ, Macaluso FP, Asara JM, Tsou MF. Centriole distal appendages promote membrane docking, leading to cilia initiation. Genes Dev 2013, 27:163-168. 10.1101/gad.207043.112, 3566309, 23348840.
    • (2013) Genes Dev , vol.27 , pp. 163-168
    • Tanos, B.E.1    Yang, H.J.2    Soni, R.3    Wang, W.J.4    Macaluso, F.P.5    Asara, J.M.6    Tsou, M.F.7
  • 45
    • 84871986826 scopus 로고    scopus 로고
    • Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis
    • 10.1083/jcb.201202126, 3529528, 23253480
    • Schmidt KN, Kuhns S, Neuner A, Hub B, Zentgraf H, Pereira G. Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis. J Cell Biol 2012, 199:1083-1101. 10.1083/jcb.201202126, 3529528, 23253480.
    • (2012) J Cell Biol , vol.199 , pp. 1083-1101
    • Schmidt, K.N.1    Kuhns, S.2    Neuner, A.3    Hub, B.4    Zentgraf, H.5    Pereira, G.6
  • 46
    • 84874364274 scopus 로고    scopus 로고
    • The microtubule affinity regulating kinase MARK4 promotes axoneme extension during early ciliogenesis
    • 10.1083/jcb.201206013, 3575539, 23400999
    • Kuhns S, Schmidt KN, Reymann J, Gilbert DF, Neuner A, Hub B, Carvalho R, Wiedemann P, Zentgraf H, Erfle H, et al. The microtubule affinity regulating kinase MARK4 promotes axoneme extension during early ciliogenesis. J Cell Biol 2013, 200:505-522. 10.1083/jcb.201206013, 3575539, 23400999.
    • (2013) J Cell Biol , vol.200 , pp. 505-522
    • Kuhns, S.1    Schmidt, K.N.2    Reymann, J.3    Gilbert, D.F.4    Neuner, A.5    Hub, B.6    Carvalho, R.7    Wiedemann, P.8    Zentgraf, H.9    Erfle, H.10
  • 47
    • 34547590810 scopus 로고    scopus 로고
    • Functional dissection of Rab GTPases involved in primary cilium formation
    • 10.1083/jcb.200703047, 2064854, 17646400
    • Yoshimura S, Egerer J, Fuchs E, Haas AK, Barr FA. Functional dissection of Rab GTPases involved in primary cilium formation. J Cell Biol 2007, 178:363-369. 10.1083/jcb.200703047, 2064854, 17646400.
    • (2007) J Cell Biol , vol.178 , pp. 363-369
    • Yoshimura, S.1    Egerer, J.2    Fuchs, E.3    Haas, A.K.4    Barr, F.A.5
  • 49
    • 84964866213 scopus 로고    scopus 로고
    • 3D-structured illumination microscopy provides novel insight into architecture of human centrosomes
    • 10.1242/bio.20122337, 3507176, 23213374
    • Sonnen KF, Schermelleh L, Leonhardt H, Nigg EA. 3D-structured illumination microscopy provides novel insight into architecture of human centrosomes. Biol Open 2012, 1:965-976. 10.1242/bio.20122337, 3507176, 23213374.
    • (2012) Biol Open , vol.1 , pp. 965-976
    • Sonnen, K.F.1    Schermelleh, L.2    Leonhardt, H.3    Nigg, E.A.4
  • 50
    • 78149296423 scopus 로고    scopus 로고
    • CEP290, a gene with many faces: mutation overview and presentation of CEP290base
    • 10.1002/humu.21337, 20690115
    • Coppieters F, Lefever S, Leroy BP, De Baere E. CEP290, a gene with many faces: mutation overview and presentation of CEP290base. Hum Mutat 2010, 31:1097-1108. 10.1002/humu.21337, 20690115.
    • (2010) Hum Mutat , vol.31 , pp. 1097-1108
    • Coppieters, F.1    Lefever, S.2    Leroy, B.P.3    De Baere, E.4
  • 53
    • 56049117628 scopus 로고    scopus 로고
    • CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium
    • 10.1093/hmg/ddn277, 2722899, 18772192
    • Kim J, Krishnaswami SR, Gleeson JG. CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium. Hum Mol Genet 2008, 17:3796-3805. 10.1093/hmg/ddn277, 2722899, 18772192.
    • (2008) Hum Mol Genet , vol.17 , pp. 3796-3805
    • Kim, J.1    Krishnaswami, S.R.2    Gleeson, J.G.3
  • 54
    • 20144375842 scopus 로고    scopus 로고
    • Nephrocystin-5, a ciliary IQ domain protein, is mutated in Senior-Loken syndrome and interacts with RPGR and calmodulin
    • 10.1038/ng1520, 15723066
    • Otto EA, Loeys B, Khanna H, Hellemans J, Sudbrak R, Fan S, Muerb U, O'Toole JF, Helou J, Attanasio M, et al. Nephrocystin-5, a ciliary IQ domain protein, is mutated in Senior-Loken syndrome and interacts with RPGR and calmodulin. Nat Genet 2005, 37:282-288. 10.1038/ng1520, 15723066.
    • (2005) Nat Genet , vol.37 , pp. 282-288
    • Otto, E.A.1    Loeys, B.2    Khanna, H.3    Hellemans, J.4    Sudbrak, R.5    Fan, S.6    Muerb, U.7    O'Toole, J.F.8    Helou, J.9    Attanasio, M.10
  • 55
    • 84878478625 scopus 로고    scopus 로고
    • Pathogenic NPHP5 mutations impair protein interaction with Cep290, a prerequisite for ciliogenesis
    • 10.1093/hmg/ddt100, 23446637
    • Barbelanne M, Song J, Ahmadzai M, Tsang WY. Pathogenic NPHP5 mutations impair protein interaction with Cep290, a prerequisite for ciliogenesis. Hum Mol Genet 2013, 22:2482-2494. 10.1093/hmg/ddt100, 23446637.
    • (2013) Hum Mol Genet , vol.22 , pp. 2482-2494
    • Barbelanne, M.1    Song, J.2    Ahmadzai, M.3    Tsang, W.Y.4
  • 56
    • 79955808192 scopus 로고    scopus 로고
    • Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways
    • 10.1016/j.cell.2011.04.019, 3383065, 21565611
    • Sang L, Miller JJ, Corbit KC, Giles RH, Brauer MJ, Otto EA, Baye LM, Wen X, Scales SJ, Kwong M, et al. Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways. Cell 2011, 145:513-528. 10.1016/j.cell.2011.04.019, 3383065, 21565611.
    • (2011) Cell , vol.145 , pp. 513-528
    • Sang, L.1    Miller, J.J.2    Corbit, K.C.3    Giles, R.H.4    Brauer, M.J.5    Otto, E.A.6    Baye, L.M.7    Wen, X.8    Scales, S.J.9    Kwong, M.10
  • 58
    • 33744757686 scopus 로고    scopus 로고
    • In-frame deletion in a novel centrosomal/ciliary protein CEP290/NPHP6 perturbs its interaction with RPGR and results in early-onset retinal degeneration in the rd16 mouse
    • 10.1093/hmg/ddl107, 1592550, 16632484
    • Chang B, Khanna H, Hawes N, Jimeno D, He S, Lillo C, Parapuram SK, Cheng H, Scott A, Hurd RE, et al. In-frame deletion in a novel centrosomal/ciliary protein CEP290/NPHP6 perturbs its interaction with RPGR and results in early-onset retinal degeneration in the rd16 mouse. Hum Mol Genet 2006, 15:1847-1857. 10.1093/hmg/ddl107, 1592550, 16632484.
    • (2006) Hum Mol Genet , vol.15 , pp. 1847-1857
    • Chang, B.1    Khanna, H.2    Hawes, N.3    Jimeno, D.4    He, S.5    Lillo, C.6    Parapuram, S.K.7    Cheng, H.8    Scott, A.9    Hurd, R.E.10
  • 60
    • 77956388187 scopus 로고    scopus 로고
    • CEP290 tethers flagellar transition zone microtubules to the membrane and regulates flagellar protein content
    • 10.1083/jcb.201006105, 2935561, 20819941
    • Craige B, Tsao CC, Diener DR, Hou Y, Lechtreck KF, Rosenbaum JL, Witman GB. CEP290 tethers flagellar transition zone microtubules to the membrane and regulates flagellar protein content. J Cell Biol 2010, 190:927-940. 10.1083/jcb.201006105, 2935561, 20819941.
    • (2010) J Cell Biol , vol.190 , pp. 927-940
    • Craige, B.1    Tsao, C.C.2    Diener, D.R.3    Hou, Y.4    Lechtreck, K.F.5    Rosenbaum, J.L.6    Witman, G.B.7
  • 61
    • 84862780073 scopus 로고    scopus 로고
    • A size-exclusion permeability barrier and nucleoporins characterize a ciliary pore complex that regulates transport into cilia
    • 10.1038/ncb2450, 3319646, 22388888
    • Kee HL, Dishinger JF, Blasius TL, Liu CJ, Margolis B, Verhey KJ. A size-exclusion permeability barrier and nucleoporins characterize a ciliary pore complex that regulates transport into cilia. Nat Cell Biol 2012, 14:431-437. 10.1038/ncb2450, 3319646, 22388888.
    • (2012) Nat Cell Biol , vol.14 , pp. 431-437
    • Kee, H.L.1    Dishinger, J.F.2    Blasius, T.L.3    Liu, C.J.4    Margolis, B.5    Verhey, K.J.6
  • 66
    • 84862004139 scopus 로고    scopus 로고
    • Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable Bardet-Biedl syndrome protein complex, the BBSome
    • 10.1074/jbc.M112.341487, 3370246, 22500027
    • Zhang Q, Yu D, Seo S, Stone EM, Sheffield VC. Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable Bardet-Biedl syndrome protein complex, the BBSome. J Biol Chem 2012, 287:20625-20635. 10.1074/jbc.M112.341487, 3370246, 22500027.
    • (2012) J Biol Chem , vol.287 , pp. 20625-20635
    • Zhang, Q.1    Yu, D.2    Seo, S.3    Stone, E.M.4    Sheffield, V.C.5
  • 67
    • 76549121983 scopus 로고    scopus 로고
    • BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly
    • 10.1073/pnas.0910268107, 2824390, 20080638
    • Seo S, Baye LM, Schulz NP, Beck JS, Zhang Q, Slusarski DC, Sheffield VC. BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly. Proc Natl Acad Sci U S A 2010, 107:1488-1493. 10.1073/pnas.0910268107, 2824390, 20080638.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1488-1493
    • Seo, S.1    Baye, L.M.2    Schulz, N.P.3    Beck, J.S.4    Zhang, Q.5    Slusarski, D.C.6    Sheffield, V.C.7
  • 68
    • 84865709186 scopus 로고    scopus 로고
    • The centriolar satellite proteins Cep72 and Cep290 interact and are required for recruitment of BBS proteins to the cilium
    • 10.1091/mbc.E12-02-0134, 3431927, 22767577
    • Stowe TR, Wilkinson CJ, Iqbal A, Stearns T. The centriolar satellite proteins Cep72 and Cep290 interact and are required for recruitment of BBS proteins to the cilium. Mol Biol Cell 2012, 23:3322-3335. 10.1091/mbc.E12-02-0134, 3431927, 22767577.
    • (2012) Mol Biol Cell , vol.23 , pp. 3322-3335
    • Stowe, T.R.1    Wilkinson, C.J.2    Iqbal, A.3    Stearns, T.4
  • 70
    • 80054849116 scopus 로고    scopus 로고
    • Centriolar satellites: busy orbits around the centrosome
    • 10.1016/j.ejcb.2011.07.007, 21945726
    • Barenz F, Mayilo D, Gruss OJ. Centriolar satellites: busy orbits around the centrosome. Eur J Cell Biol 2011, 90:983-989. 10.1016/j.ejcb.2011.07.007, 21945726.
    • (2011) Eur J Cell Biol , vol.90 , pp. 983-989
    • Barenz, F.1    Mayilo, D.2    Gruss, O.J.3
  • 71
    • 0033615982 scopus 로고    scopus 로고
    • Centriolar satellites: molecular characterization, ATP-dependent movement toward centrioles and possible involvement in ciliogenesis
    • 10.1083/jcb.147.5.969, 2169353, 10579718
    • Kubo A, Sasaki H, Yuba-Kubo A, Tsukita S, Shiina N. Centriolar satellites: molecular characterization, ATP-dependent movement toward centrioles and possible involvement in ciliogenesis. J Cell Biol 1999, 147:969-980. 10.1083/jcb.147.5.969, 2169353, 10579718.
    • (1999) J Cell Biol , vol.147 , pp. 969-980
    • Kubo, A.1    Sasaki, H.2    Yuba-Kubo, A.3    Tsukita, S.4    Shiina, N.5
  • 72
    • 0037191046 scopus 로고    scopus 로고
    • Assembly of centrosomal proteins and microtubule organization depends on PCM-1
    • 10.1083/jcb.200204023, 2173044, 12403812
    • Dammermann A, Merdes A. Assembly of centrosomal proteins and microtubule organization depends on PCM-1. J Cell Biol 2002, 159:255-266. 10.1083/jcb.200204023, 2173044, 12403812.
    • (2002) J Cell Biol , vol.159 , pp. 255-266
    • Dammermann, A.1    Merdes, A.2
  • 73
    • 79951829447 scopus 로고    scopus 로고
    • Centriolar satellites are assembly points for proteins implicated in human ciliopathies, including oral-facial-digital syndrome 1
    • 10.1242/jcs.077156, 3031371, 21266464
    • Lopes CA, Prosser SL, Romio L, Hirst RA, O'Callaghan C, Woolf AS, Fry AM. Centriolar satellites are assembly points for proteins implicated in human ciliopathies, including oral-facial-digital syndrome 1. J Cell Sci 2011, 124:600-612. 10.1242/jcs.077156, 3031371, 21266464.
    • (2011) J Cell Sci , vol.124 , pp. 600-612
    • Lopes, C.A.1    Prosser, S.L.2    Romio, L.3    Hirst, R.A.4    O'Callaghan, C.5    Woolf, A.S.6    Fry, A.M.7
  • 75
    • 79551718744 scopus 로고    scopus 로고
    • The blind leading the obese: the molecular pathophysiology of a human obesity syndrome
    • discussion 181-172, 2917141, 20697559
    • Sheffield VC. The blind leading the obese: the molecular pathophysiology of a human obesity syndrome. Trans Am Clin Climatol Assoc 2010, 121:172-181. discussion 181-172, 2917141, 20697559.
    • (2010) Trans Am Clin Climatol Assoc , vol.121 , pp. 172-181
    • Sheffield, V.C.1
  • 77
    • 77953879123 scopus 로고    scopus 로고
    • The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia
    • 10.1016/j.cell.2010.05.015, 2898735, 20603001
    • Jin H, White SR, Shida T, Schulz S, Aguiar M, Gygi SP, Bazan JF, Nachury MV. The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to cilia. Cell 2010, 141:1208-1219. 10.1016/j.cell.2010.05.015, 2898735, 20603001.
    • (2010) Cell , vol.141 , pp. 1208-1219
    • Jin, H.1    White, S.R.2    Shida, T.3    Schulz, S.4    Aguiar, M.5    Gygi, S.P.6    Bazan, J.F.7    Nachury, M.V.8
  • 78
    • 44449106038 scopus 로고    scopus 로고
    • Identification of ciliary localization sequences within the third intracellular loop of G protein-coupled receptors
    • 10.1091/mbc.E07-09-0942, 2291422, 18256283
    • Berbari NF, Johnson AD, Lewis JS, Askwith CC, Mykytyn K. Identification of ciliary localization sequences within the third intracellular loop of G protein-coupled receptors. Mol Biol Cell 2008, 19:1540-1547. 10.1091/mbc.E07-09-0942, 2291422, 18256283.
    • (2008) Mol Biol Cell , vol.19 , pp. 1540-1547
    • Berbari, N.F.1    Johnson, A.D.2    Lewis, J.S.3    Askwith, C.C.4    Mykytyn, K.5
  • 79
    • 76149101303 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii BBSome is an IFT cargo required for export of specific signaling proteins from flagella
    • 10.1083/jcb.200909183, 2806276, 20038682
    • Lechtreck KF, Johnson EC, Sakai T, Cochran D, Ballif BA, Rush J, Pazour GJ, Ikebe M, Witman GB. The Chlamydomonas reinhardtii BBSome is an IFT cargo required for export of specific signaling proteins from flagella. J Cell Biol 2009, 187:1117-1132. 10.1083/jcb.200909183, 2806276, 20038682.
    • (2009) J Cell Biol , vol.187 , pp. 1117-1132
    • Lechtreck, K.F.1    Johnson, E.C.2    Sakai, T.3    Cochran, D.4    Ballif, B.A.5    Rush, J.6    Pazour, G.J.7    Ikebe, M.8    Witman, G.B.9
  • 80
    • 33144456230 scopus 로고    scopus 로고
    • Bardet-Biedl syndrome genes are important in retrograde intracellular trafficking and Kupffer's vesicle cilia function
    • 10.1093/hmg/ddi468, 16399798
    • Yen HJ, Tayeh MK, Mullins RF, Stone EM, Sheffield VC, Slusarski DC. Bardet-Biedl syndrome genes are important in retrograde intracellular trafficking and Kupffer's vesicle cilia function. Hum Mol Genet 2006, 15:667-677. 10.1093/hmg/ddi468, 16399798.
    • (2006) Hum Mol Genet , vol.15 , pp. 667-677
    • Yen, H.J.1    Tayeh, M.K.2    Mullins, R.F.3    Stone, E.M.4    Sheffield, V.C.5    Slusarski, D.C.6
  • 84
    • 9344261783 scopus 로고    scopus 로고
    • Bbs2-null mice have neurosensory deficits, a defect in social dominance, and retinopathy associated with mislocalization of rhodopsin
    • 10.1073/pnas.0405496101, 534519, 15539463
    • Nishimura DY, Fath M, Mullins RF, Searby C, Andrews M, Davis R, Andorf JL, Mykytyn K, Swiderski RE, Yang B, et al. Bbs2-null mice have neurosensory deficits, a defect in social dominance, and retinopathy associated with mislocalization of rhodopsin. Proc Natl Acad Sci USA 2004, 101:16588-16593. 10.1073/pnas.0405496101, 534519, 15539463.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16588-16593
    • Nishimura, D.Y.1    Fath, M.2    Mullins, R.F.3    Searby, C.4    Andrews, M.5    Davis, R.6    Andorf, J.L.7    Mykytyn, K.8    Swiderski, R.E.9    Yang, B.10
  • 85
    • 84859219770 scopus 로고    scopus 로고
    • BBS proteins interact genetically with the IFT pathway to influence SHH-related phenotypes
    • 10.1093/hmg/dds004, 3315203, 22228099
    • Zhang Q, Seo S, Bugge K, Stone EM, Sheffield VC. BBS proteins interact genetically with the IFT pathway to influence SHH-related phenotypes. Hum Mol Genet 2012, 21:1945-1953. 10.1093/hmg/dds004, 3315203, 22228099.
    • (2012) Hum Mol Genet , vol.21 , pp. 1945-1953
    • Zhang, Q.1    Seo, S.2    Bugge, K.3    Stone, E.M.4    Sheffield, V.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.