메뉴 건너뛰기




Volumn 12, Issue 5, 2013, Pages 849-858

VDAC3 and Mps1 negatively regulate ciliogenesis

Author keywords

Basal body; Centrosome; Ciliogenesis; Mps1; Primary cilia; Quiescence; VDAC

Indexed keywords

TELOMERASE;

EID: 84874627577     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.23824     Document Type: Article
Times cited : (43)

References (50)
  • 1
    • 0034678396 scopus 로고    scopus 로고
    • The respective contributions of the mother and daughter centrioles to centrosome activity and behavior in vertebrate cells
    • PMID:10769025
    • Piel M, Meyer P, Khodjakov A, Rieder CL, Bornens M. The respective contributions of the mother and daughter centrioles to centrosome activity and behavior in vertebrate cells. J Cell Biol 2000; 149:317-30; PMID:10769025; http://dx.doi.org/10.1083/jcb.149.2.317
    • (2000) J Cell Biol , vol.149 , pp. 317-330
    • Piel, M.1    Meyer, P.2    Khodjakov, A.3    Rieder, C.L.4    Bornens, M.5
  • 2
    • 79956193249 scopus 로고    scopus 로고
    • Regulating the transition from centriole to basal body
    • PMID:21536747
    • Kobayashi T, Dynlacht BD. Regulating the transition from centriole to basal body. J Cell Biol 2011; 193:435-44; PMID:21536747; http://dx.doi.org/10. 1083/jcb.201101005
    • (2011) J Cell Biol , vol.193 , pp. 435-444
    • Kobayashi, T.1    Dynlacht, B.D.2
  • 3
    • 0034566978 scopus 로고    scopus 로고
    • Ciliary structure in health and disease
    • PMID:11082764
    • Afzelius BA. Ciliary structure in health and disease. Acta Otorhinolaryngol Belg 2000; 54:287-91; PMID:11082764
    • (2000) Acta Otorhinolaryngol Belg , vol.54 , pp. 287-291
    • Afzelius, B.A.1
  • 4
    • 84856360903 scopus 로고    scopus 로고
    • Stages of ciliogenesis and regulation of ciliary length
    • PMID:22178116
    • Avasthi P, Marshall WF. Stages of ciliogenesis and regulation of ciliary length. Differentiation 2012; 83:S30-42; PMID:22178116
    • (2012) Differentiation , vol.83
    • Avasthi, P.1    Marshall, W.F.2
  • 5
    • 7944223873 scopus 로고    scopus 로고
    • Cilia-related diseases
    • PMID:15495266
    • Afzelius BA. Cilia-related diseases. J Pathol 2004; 204:470-7; PMID:15495266; http://dx.doi. org/10.1002/path.1652
    • (2004) J Pathol , vol.204 , pp. 470-477
    • Afzelius, B.A.1
  • 6
    • 76649103368 scopus 로고    scopus 로고
    • The perennial organelle: Assembly and disassembly of the primary cilium
    • PMID:20144999
    • Seeley ES, Nachury MV. The perennial organelle: assembly and disassembly of the primary cilium. J Cell Sci 2010; 123:511-8; PMID:20144999; http://dx.doi. org/10.1242/jcs.061093
    • (2010) J Cell Sci , vol.123 , pp. 511-518
    • Seeley, E.S.1    Nachury, M.V.2
  • 7
    • 0036844195 scopus 로고    scopus 로고
    • Intraflagellar transport
    • PMID:12415299
    • Rosenbaum JL, Witman GB. Intraflagellar transport. Nat Rev Mol Cell Biol 2002; 3:813-25; PMID:12415299; http://dx.doi.org/10.1038/nrm952
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 813-825
    • Rosenbaum, J.L.1    Witman, G.B.2
  • 8
    • 79958250238 scopus 로고    scopus 로고
    • Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis
    • PMID: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; 145:914-25; PMID:21620453; http://dx.doi. org/10.1016/j.cell.2011.04. 028
    • (2011) Cell , vol.145 , pp. 914-925
    • Kobayashi, T.1    Tsang, W.Y.2    Li, J.3    Lane, W.4    Dynlacht, B.D.5
  • 9
    • 84862589652 scopus 로고    scopus 로고
    • Trichoplein and Aurora A block aberrant primary cilia assembly in proliferating cells
    • PMID:22529102
    • Inoko A, Matsuyama M, Goto H, Ohmuro-Matsuyama Y, Hayashi Y, Enomoto M, et al. Trichoplein and Aurora A block aberrant primary cilia assembly in proliferating cells. J Cell Biol 2012; 197:391-405; PMID:22529102; http://dx.doi.org/10.1083/jcb.201106101
    • (2012) J Cell Biol , vol.197 , pp. 391-405
    • Inoko, A.1    Matsuyama, M.2    Goto, H.3    Ohmuro-Matsuyama, Y.4    Hayashi, Y.5    Enomoto, M.6
  • 10
    • 84863934244 scopus 로고    scopus 로고
    • Calmodulin activation of Aurora-A kinase (AURKA) is required during ciliary disassembly and in mitosis
    • PMID:22621899
    • Plotnikova OV, Nikonova AS, Loskutov YV, Kozyulina PY, Pugacheva EN, Golemis EA. Calmodulin activation of Aurora-A kinase (AURKA) is required during ciliary disassembly and in mitosis. Mol Biol Cell 2012; 23:2658-70; PMID:22621899; http://dx.doi. org/10.1091/mbc.E11-12-1056
    • (2012) Mol Biol Cell , vol.23 , pp. 2658-2670
    • Plotnikova, O.V.1    Nikonova, A.S.2    Loskutov, Y.V.3    Kozyulina, P.Y.4    Pugacheva, E.N.5    Golemis, E.A.6
  • 11
    • 34250758641 scopus 로고    scopus 로고
    • HEF1-dependent Aurora A activation induces disassembly of the primary cilium
    • PMID:17604723
    • Pugacheva EN, Jablonski SA, Hartman TR, Henske EP, Golemis EA. HEF1-dependent Aurora A activation induces disassembly of the primary cilium. Cell 2007; 129:1351-63; PMID:17604723; http://dx.doi. org/10.1016/j.cell.2007. 04.035
    • (2007) Cell , vol.129 , pp. 1351-1363
    • Pugacheva, E.N.1    Jablonski, S.A.2    Hartman, T.R.3    Henske, E.P.4    Golemis, E.A.5
  • 12
    • 34547939469 scopus 로고    scopus 로고
    • Cep97 and CP110 suppress a cilia assembly program
    • PMID:17719545
    • Spektor A, Tsang WY, Khoo D, Dynlacht BD. Cep97 and CP110 suppress a cilia assembly program. Cell 2007; 130:678-90; PMID:17719545; http://dx.doi. org/10.1016/j.cell.2007.06.027
    • (2007) Cell , vol.130 , pp. 678-690
    • Spektor, A.1    Tsang, W.Y.2    Khoo, D.3    Dynlacht, B.D.4
  • 13
    • 84856352817 scopus 로고    scopus 로고
    • Primary cilia as biomechanical sensors in regulating endothelial function
    • PMID:22169885
    • Egorova AD, van der Heiden K, Poelmann RE, Hierck BP. Primary cilia as biomechanical sensors in regulating endothelial function. Differentiation 2012; 83:S56-61; PMID:22169885
    • (2012) Differentiation , vol.83
    • Egorova, A.D.1    Van Der Heiden, K.2    Poelmann, R.E.3    Hierck, B.P.4
  • 14
    • 79955808192 scopus 로고    scopus 로고
    • Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways
    • PMID:21565611
    • Sang L, Miller JJ, Corbit KC, Giles RH, Brauer MJ, Otto EA, et al. Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways. Cell 2011; 145:513-28; PMID:21565611; http://dx.doi.org/10.1016/j. cell.2011.04.019
    • (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
  • 15
    • 84867275965 scopus 로고    scopus 로고
    • VDAC3 regulates centriole assembly by targeting Mps1 to centrosomes
    • PMID:22935710
    • Majumder S, Slabodnick M, Pike A, Marquardt J, Fisk HA. VDAC3 regulates centriole assembly by targeting Mps1 to centrosomes. Cell Cycle 2012; 11:3666-78; PMID:22935710; http://dx.doi.org/10.4161/cc.21927
    • (2012) Cell Cycle , vol.11 , pp. 3666-3678
    • Majumder, S.1    Slabodnick, M.2    Pike, A.3    Marquardt, J.4    Fisk, H.A.5
  • 16
    • 38049129203 scopus 로고    scopus 로고
    • Autophosphorylation-dependent activation of human Mps1 is required for the spindle checkpoint
    • PMID:18083840
    • Kang J, Chen Y, Zhao Y, Yu H. Autophosphorylation-dependent activation of human Mps1 is required for the spindle checkpoint. Proc Natl Acad Sci USA 2007; 104:20232-7; PMID:18083840; http://dx.doi. org/10.1073/pnas.0710519105
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20232-20237
    • Kang, J.1    Chen, Y.2    Zhao, Y.3    Yu, H.4
  • 17
    • 0345166853 scopus 로고    scopus 로고
    • Human Mps1 protein kinase is required for centrosome duplication and normal mitotic progression
    • PMID:14657364
    • Fisk HA, Mattison CP, Winey M. Human Mps1 protein kinase is required for centrosome duplication and normal mitotic progression. Proc Natl Acad Sci USA 2003; 100:14875-80; PMID:14657364; http://dx.doi. org/10.1073/pnas.2434156100
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14875-14880
    • Fisk, H.A.1    Mattison, C.P.2    Winey, M.3
  • 18
    • 78649648081 scopus 로고    scopus 로고
    • Antizyme restrains centrosome amplification by regulating the accumulation of Mps1 at centrosomes
    • PMID:20861309
    • Kasbek C, Yang CH, Fisk HA. Antizyme restrains centrosome amplification by regulating the accumulation of Mps1 at centrosomes. Mol Biol Cell 2010; 21:3878-89; PMID:20861309; http://dx.doi.org/10.1091/mbc. E10-04-0281
    • (2010) Mol Biol Cell , vol.21 , pp. 3878-3889
    • Kasbek, C.1    Yang, C.H.2    Fisk, H.A.3
  • 19
    • 0035854383 scopus 로고    scopus 로고
    • The mouse Mps1p-like kinase regulates centrosome duplication
    • PMID:11461705
    • Fisk HA, Winey M. The mouse Mps1p-like kinase regulates centrosome duplication. Cell 2001; 106:95-104; PMID:11461705; http://dx.doi.org/10.1016/ S0092-8674(01)00411-1
    • (2001) Cell , vol.106 , pp. 95-104
    • Fisk, H.A.1    Winey, M.2
  • 20
    • 79953867887 scopus 로고    scopus 로고
    • Centriole assembly and the role of Mps1: Defensible or dispensable?
    • PMID:21492451
    • Pike AN, Fisk HA. Centriole assembly and the role of Mps1: defensible or dispensable? Cell Div 2011; 6:9; PMID:21492451; http://dx.doi.org/10.1186/1747- 1028-6-9
    • (2011) Cell Div , vol.6 , pp. 9
    • Pike, A.N.1    Fisk, H.A.2
  • 21
    • 78649641932 scopus 로고    scopus 로고
    • Mps1 phosphorylation sites regulate the function of centrin 2 in centriole assembly
    • PMID:20980622
    • Yang CH, Kasbek C, Majumder S, Yusof AM, Fisk HA. Mps1 phosphorylation sites regulate the function of centrin 2 in centriole assembly. Mol Biol Cell 2010; 21:4361-72; PMID:20980622; http://dx.doi. org/10.1091/mbc.E10-04-0298
    • (2010) Mol Biol Cell , vol.21 , pp. 4361-4372
    • Yang, C.H.1    Kasbek, C.2    Majumder, S.3    Yusof, A.M.4    Fisk, H.A.5
  • 22
    • 70349914036 scopus 로고    scopus 로고
    • Mps1 as a link between centrosomes and genomic instability
    • PMID:19274768
    • Kasbek C, Yang CH, Fisk HA. Mps1 as a link between centrosomes and genomic instability. Environ Mol Mutagen 2009; 50:654-65; PMID:19274768; http://dx.doi.org/10.1002/em.20476
    • (2009) Environ Mol Mutagen , vol.50 , pp. 654-665
    • Kasbek, C.1    Yang, C.H.2    Fisk, H.A.3
  • 23
    • 35848944115 scopus 로고    scopus 로고
    • Preventing the degradation of mps1 at centrosomes is sufficient to cause centrosome reduplication in human cells
    • PMID:17804818
    • Kasbek C, Yang CH, Yusof AM, Chapman HM, Winey M, Fisk HA. Preventing the degradation of mps1 at centrosomes is sufficient to cause centrosome reduplication in human cells. Mol Biol Cell 2007; 18:4457-69; PMID:17804818; http://dx.doi. org/10.1091/mbc.E07-03-0283
    • (2007) Mol Biol Cell , vol.18 , pp. 4457-4469
    • Kasbek, C.1    Yang, C.H.2    Yusof, A.M.3    Chapman, H.M.4    Winey, M.5    Fisk, H.A.6
  • 24
    • 84873732622 scopus 로고    scopus 로고
    • Phosphorylation of Mps1 by BRAF(V600E) prevents Mps1 degradation and contributes to chromosome instability in melanoma
    • PMID:22430208
    • Liu J, Cheng X, Zhang Y, Li S, Cui H, Zhang L, et al. Phosphorylation of Mps1 by BRAF(V600E) prevents Mps1 degradation and contributes to chromosome instability in melanoma. Oncogene 2012; PMID:22430208
    • (2012) Oncogene
    • Liu, J.1    Cheng, X.2    Zhang, Y.3    Li, S.4    Cui, H.5    Zhang, L.6
  • 25
    • 79953305554 scopus 로고    scopus 로고
    • Ciliary transition zone activation of phosphorylated Tctex-1 controls ciliary resorption, S-phase entry and fate of neural progenitors
    • PMID:21394082
    • Li A, Saito M, Chuang JZ, Tseng YY, Dedesma C, Tomizawa K, et al. Ciliary transition zone activation of phosphorylated Tctex-1 controls ciliary resorption, S-phase entry and fate of neural progenitors. Nat Cell Biol 2011; 13:402-11; PMID:21394082; http://dx.doi.org/10.1038/ncb2218
    • (2011) Nat Cell Biol , vol.13 , pp. 402-411
    • Li, A.1    Saito, M.2    Chuang, J.Z.3    Tseng, Y.Y.4    Dedesma, C.5    Tomizawa, K.6
  • 26
    • 79953331186 scopus 로고    scopus 로고
    • Nde1-mediated inhibition of ciliogenesis affects cell cycle re-entry
    • PMID:21394081
    • Kim S, Zaghloul NA, Bubenshchikova E, Oh EC, Rankin S, Katsanis N, et al. Nde1-mediated inhibition of ciliogenesis affects cell cycle re-entry. Nat Cell Biol 2011; 13:351-60; PMID:21394081; http://dx.doi. org/10.1038/ncb2183
    • (2011) Nat Cell Biol , vol.13 , pp. 351-360
    • Kim, S.1    Zaghloul, N.A.2    Bubenshchikova, E.3    Oh, E.C.4    Rankin, S.5    Katsanis, N.6
  • 27
    • 79953316640 scopus 로고    scopus 로고
    • Do cilia put brakes on the cell cycle?
    • PMID:21460803
    • Jackson PK. Do cilia put brakes on the cell cycle? Nat Cell Biol 2011; 13:340-2; PMID:21460803; http://dx.doi.org/10.1038/ncb0411-340
    • (2011) Nat Cell Biol , vol.13 , pp. 340-342
    • Jackson, P.K.1
  • 28
    • 80052410146 scopus 로고    scopus 로고
    • Ciliary resorption modulates G1 length and cell cycle progression
    • PMID:21964298
    • Sung CH, Li A. Ciliary resorption modulates G1 length and cell cycle progression. Cell Cycle 2011; 10:2825-6; PMID:21964298; http://dx.doi.org/10. 4161/cc.10.17.16943
    • (2011) Cell Cycle , vol.10 , pp. 2825-2826
    • Sung, C.H.1    Li, A.2
  • 29
    • 77951128108 scopus 로고    scopus 로고
    • Functional genomic screen for modulators of ciliogenesis and cilium length
    • PMID:20393563
    • Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, et al. Functional genomic screen for modulators of ciliogenesis and cilium length. Nature 2010; 464:1048-51; PMID:20393563; http://dx.doi. org/10.1038/nature08895
    • (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
  • 30
    • 82655189981 scopus 로고    scopus 로고
    • Arl13b regulates ciliogenesis and the dynamic localization of Shh signaling proteins
    • PMID:21976698
    • Larkins CE, Aviles GD, East MP, Kahn RA, Caspary T. Arl13b regulates ciliogenesis and the dynamic localization of Shh signaling proteins. Mol Biol Cell 2011; 22:4694-703; PMID:21976698; http://dx.doi. org/10.1091/mbc.E10-12- 0994
    • (2011) Mol Biol Cell , vol.22 , pp. 4694-4703
    • Larkins, C.E.1    Aviles, G.D.2    East, M.P.3    Kahn, R.A.4    Caspary, T.5
  • 31
    • 34250372956 scopus 로고    scopus 로고
    • RAS-RAF-MEK dependent oxidative cell death involving voltagedependent anion channels
    • PMID:17568748
    • Yagoda N, von Rechenberg M, Zaganjor E, Bauer AJ, Yang WS, Fridman DJ, et al. RAS-RAF-MEK dependent oxidative cell death involving voltagedependent anion channels. Nature 2007; 447:864-8; PMID:17568748; http://dx.doi.org/10.1038/ nature05859
    • (2007) Nature , vol.447 , pp. 864-868
    • Yagoda, N.1    Von Rechenberg, M.2    Zaganjor, E.3    Bauer, A.J.4    Yang, W.S.5    Fridman, D.J.6
  • 32
    • 40849085503 scopus 로고    scopus 로고
    • Synthetic lethal screening identifies compounds activating iron-dependent, nonapoptotic cell death in oncogenic-RAS-harboring cancer cells
    • PMID:18355723
    • Yang WS, Stockwell BR. Synthetic lethal screening identifies compounds activating iron-dependent, nonapoptotic cell death in oncogenic-RAS-harboring cancer cells. Chem Biol 2008; 15:234-45; PMID:18355723; http://dx.doi.org/10. 1016/j.chembiol. 2008.02.010
    • (2008) Chem Biol , vol.15 , pp. 234-245
    • Yang, W.S.1    Stockwell, B.R.2
  • 33
    • 48549102438 scopus 로고    scopus 로고
    • CP110 suppresses primary cilia formation through its interaction with CEP290, a protein deficient in human ciliary disease
    • PMID:18694559
    • Tsang WY, Bossard C, Khanna H, Peränen J, Swaroop A, Malhotra V, et al. CP110 suppresses primary cilia formation through its interaction with CEP290, a protein deficient in human ciliary disease. Dev Cell 2008; 15:187-97; PMID:18694559; http://dx.doi. org/10.1016/j.devcel.2008.07.004
    • (2008) Dev Cell , vol.15 , pp. 187-197
    • Tsang, W.Y.1    Bossard, C.2    Khanna, H.3    Peränen, J.4    Swaroop, A.5    Malhotra, V.6
  • 34
    • 0026638016 scopus 로고
    • Expression of TTK, a novel human protein kinase, is associated with cell proliferation
    • PMID:1639825
    • Mills GB, Schmandt R, McGill M, Amendola A, Hill M, Jacobs K, et al. Expression of TTK, a novel human protein kinase, is associated with cell proliferation. J Biol Chem 1992; 267:16000-6; PMID:1639825
    • (1992) J Biol Chem , vol.267 , pp. 16000-16006
    • Mills, G.B.1    Schmandt, R.2    McGill, M.3    Amendola, A.4    Hill, M.5    Jacobs, K.6
  • 35
  • 36
    • 0036861418 scopus 로고    scopus 로고
    • Mps1 defines a proximal blastemal proliferative compartment essential for zebrafish fin regeneration
    • PMID:12399306
    • Poss KD, Nechiporuk A, Hillam AM, Johnson SL, Keating MT. Mps1 defines a proximal blastemal proliferative compartment essential for zebrafish fin regeneration. Development 2002; 129:5141-9; PMID:12399306
    • (2002) Development , vol.129 , pp. 5141-5149
    • Poss, K.D.1    Nechiporuk, A.2    Hillam, A.M.3    Johnson, S.L.4    Keating, M.T.5
  • 37
    • 67249088610 scopus 로고    scopus 로고
    • Genetic evidence for shared mechanisms of epimorphic regeneration in zebrafish
    • PMID:19474300
    • Qin Z, Barthel LK, Raymond PA. Genetic evidence for shared mechanisms of epimorphic regeneration in zebrafish. Proc Natl Acad Sci USA 2009; 106:9310-5; PMID:19474300; http://dx.doi.org/10.1073/pnas.0811186106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9310-9315
    • Qin, Z.1    Barthel, L.K.2    Raymond, P.A.3
  • 38
    • 0034574615 scopus 로고    scopus 로고
    • The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin
    • PMID:11263498
    • Gillingham AK, Munro S. The PACT domain, a conserved centrosomal targeting motif in the coiled-coil proteins AKAP450 and pericentrin. EMBO Rep 2000; 1:524-9; PMID:11263498
    • (2000) EMBO Rep , vol.1 , pp. 524-529
    • Gillingham, A.K.1    Munro, S.2
  • 39
    • 84863198374 scopus 로고    scopus 로고
    • MiR-129-3p controls cilia assembly by regulating CP110 and actin dynamics
    • PMID:22684256
    • Cao J, Shen Y, Zhu L, Xu Y, Zhou Y, Wu Z, et al. miR-129-3p controls cilia assembly by regulating CP110 and actin dynamics. Nat Cell Biol 2012; 14:697-706; PMID:22684256; http://dx.doi.org/10.1038/ncb2512
    • (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
  • 40
    • 79960900387 scopus 로고    scopus 로고
    • A transition zone complex regulates mammalian ciliogenesis and ciliary membrane composition
    • PMID:21725307
    • Garcia-Gonzalo FR, Corbit KC, Sirerol-Piquer MS, Ramaswami G, Otto EA, Noriega TR, et al. A transition zone complex regulates mammalian ciliogenesis and ciliary membrane composition. Nat Genet 2011; 43:776-84; PMID:21725307; http://dx.doi. org/10.1038/ng.891
    • (2011) Nat Genet , vol.43 , pp. 776-784
    • Garcia-Gonzalo, F.R.1    Corbit, K.C.2    Sirerol-Piquer, M.S.3    Ramaswami, G.4    Otto, E.A.5    Noriega, T.R.6
  • 41
    • 79955513961 scopus 로고    scopus 로고
    • MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis
    • PMID:21422230
    • Williams CL, Li C, Kida K, Inglis PN, Mohan S, Semenec L, et al. MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis. J Cell Biol 2011; 192:1023-41; PMID:21422230; http://dx.doi.org/10.1083/jcb.201012116
    • (2011) J Cell Biol , vol.192 , pp. 1023-1041
    • Williams, C.L.1    Li, C.2    Kida, K.3    Inglis, P.N.4    Mohan, S.5    Semenec, L.6
  • 43
    • 2442468057 scopus 로고    scopus 로고
    • Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum
    • PMID:14739283
    • Hinsch KD, De Pinto V, Aires VA, Schneider X, Messina A, Hinsch E. Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum. J Biol Chem 2004; 279:15281-8; PMID:14739283; http://dx.doi. org/10.1074/jbc.M313433200
    • (2004) J Biol Chem , vol.279 , pp. 15281-15288
    • Hinsch, K.D.1    De Pinto, V.2    Aires, V.A.3    Schneider, X.4    Messina, A.5    Hinsch, E.6
  • 44
    • 0036257364 scopus 로고    scopus 로고
    • Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74
    • PMID:12009301
    • Schwarzer C, Barnikol-Watanabe S, Thinnes FP, Hilschmann N. Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex1 and the heat-shock protein PBP74. Int J Biochem Cell Biol 2002; 34:1059-70; PMID:12009301; http://dx.doi.org/10.1016/S1357-2725(02)00026-2
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 1059-1070
    • Schwarzer, C.1    Barnikol-Watanabe, S.2    Thinnes, F.P.3    Hilschmann, N.4
  • 45
    • 16844380974 scopus 로고    scopus 로고
    • Identification of trichoplein, a novel keratin filament-binding protein
    • PMID:15731013
    • Nishizawa M, Izawa I, Inoko A, Hayashi Y, Nagata K, Yokoyama T, et al. Identification of trichoplein, a novel keratin filament-binding protein. J Cell Sci 2005; 118:1081-90; PMID:15731013; http://dx.doi. org/10.1242/jcs.01667
    • (2005) J Cell Sci , vol.118 , pp. 1081-1090
    • Nishizawa, M.1    Izawa, I.2    Inoko, A.3    Hayashi, Y.4    Nagata, K.5    Yokoyama, T.6
  • 46
    • 78049342172 scopus 로고    scopus 로고
    • Trichoplein/mitostatin regulates endoplasmic reticulum-mitochondria juxtaposition
    • PMID:20930847
    • Cerqua C, Anesti V, Pyakurel A, Liu D, Naon D, Wiche G, et al. Trichoplein/mitostatin regulates endoplasmic reticulum-mitochondria juxtaposition. EMBO Rep 2010; 11:854-60; PMID:20930847; http://dx.doi. org/10.1038/embor.2010.151
    • (2010) EMBO Rep , vol.11 , pp. 854-860
    • Cerqua, C.1    Anesti, V.2    Pyakurel, A.3    Liu, D.4    Naon, D.5    Wiche, G.6
  • 47
    • 79952790040 scopus 로고    scopus 로고
    • Trichoplein controls microtubule anchoring at the centrosome by binding to Odf2 and ninein
    • PMID:21325031
    • Ibi M, Zou P, Inoko A, Shiromizu T, Matsuyama M, Hayashi Y, et al. Trichoplein controls microtubule anchoring at the centrosome by binding to Odf2 and ninein. J Cell Sci 2011; 124:857-64; PMID:21325031; http://dx.doi.org/10. 1242/jcs.075705
    • (2011) J Cell Sci , vol.124 , pp. 857-864
    • Ibi, M.1    Zou, P.2    Inoko, A.3    Shiromizu, T.4    Matsuyama, M.5    Hayashi, Y.6
  • 48
    • 0035914399 scopus 로고    scopus 로고
    • Immotile sperm and infertility in mice lacking mitochondrial voltage-dependent anion channel type 3
    • PMID:11507092
    • Sampson MJ, Decker WK, Beaudet AL, Ruitenbeek W, Armstrong D, Hicks MJ, et al. Immotile sperm and infertility in mice lacking mitochondrial voltage-dependent anion channel type 3. J Biol Chem 2001; 276:39206-12; PMID:11507092; http://dx.doi. org/10.1074/jbc.M104724200
    • (2001) J Biol Chem , vol.276 , pp. 39206-39212
    • Sampson, M.J.1    Decker, W.K.2    Beaudet, A.L.3    Ruitenbeek, W.4    Armstrong, D.5    Hicks, M.J.6
  • 49
    • 77949865316 scopus 로고    scopus 로고
    • Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy
    • PMID:20179356
    • O'Toole JF, Liu Y, Davis EE, Westlake CJ, Attanasio M, Otto EA, et al. Individuals with mutations in XPNPEP3, which encodes a mitochondrial protein, develop a nephronophthisis-like nephropathy. J Clin Invest 2010; 120:791-802; PMID:20179356; http://dx.doi.org/10.1172/JCI40076
    • (2010) J Clin Invest , vol.120 , pp. 791-802
    • O'Toole, J.F.1    Liu, Y.2    Davis, E.E.3    Westlake, C.J.4    Attanasio, M.5    Otto, E.A.6
  • 50
    • 69949118412 scopus 로고    scopus 로고
    • Polo kinase and separase regulate the mitotic licensing of centriole duplication in human cells
    • PMID:19758559
    • Tsou MF, Wang WJ, George KA, Uryu K, Stearns T, Jallepalli PV. Polo kinase and separase regulate the mitotic licensing of centriole duplication in human cells. Dev Cell 2009; 17:344-54; PMID:19758559; http://dx.doi.org/10.1016/ j.devcel.2009.07.015
    • (2009) Dev Cell , vol.17 , pp. 344-354
    • Tsou, M.F.1    Wang, W.J.2    George, K.A.3    Uryu, K.4    Stearns, T.5    Jallepalli, P.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.