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Volumn 100, Issue 11, 2009, Pages 2115-2125

BRCA2 interacts with the cytoskeletal linker protein plectin to form a complex controlling centrosome localization

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; BRCA2 PROTEIN; CYCLIN B; CYCLIN DEPENDENT KINASE 1; CYTOSKELETON PROTEIN; DNA; GAMMA TUBULIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; PLECTIN; SMALL INTERFERING RNA; VIMENTIN;

EID: 71049185569     PISSN: 13479032     EISSN: 13497006     Source Type: Journal    
DOI: 10.1111/j.1349-7006.2009.01282.x     Document Type: Article
Times cited : (35)

References (38)
  • 1
    • 0006713602 scopus 로고
    • Identification of the breast cancer susceptibility gene BRCA2
    • Wooster R, Bignell G, Lancaster J. Identification of the breast cancer susceptibility gene BRCA2. Nature 1995, 378:789-92.
    • (1995) Nature , vol.378 , pp. 789-792
    • Wooster, R.1    Bignell, G.2    Lancaster, J.3
  • 2
    • 0037169354 scopus 로고    scopus 로고
    • Cancer susceptibility and the functions of BRCA1 and BRCA2
    • Venkitaraman A. Cancer susceptibility and the functions of BRCA1 and BRCA2. Cell 2002, 108:171-82.
    • (2002) Cell , vol.108 , pp. 171-182
    • Venkitaraman, A.1
  • 3
    • 3242749855 scopus 로고    scopus 로고
    • Emerging functions of BRCA2 in DNA recombination
    • Pellegrini L, Venkitaraman A. Emerging functions of BRCA2 in DNA recombination. Trends Biochem Sci 2004, 29:310-6.
    • (2004) Trends Biochem Sci , vol.29 , pp. 310-316
    • Pellegrini, L.1    Venkitaraman, A.2
  • 4
    • 15844373362 scopus 로고    scopus 로고
    • CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair
    • Esashi F, Christ N, Gannon J. CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair. Nature 2005, 434:598-604.
    • (2005) Nature , vol.434 , pp. 598-604
    • Esashi, F.1    Christ, N.2    Gannon, J.3
  • 5
    • 0031466027 scopus 로고    scopus 로고
    • RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2
    • Wong A, Pero R, Ormonde P, Tavtigian S, Bartel P. RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2. J Biol Chem 1997, 272:31941-4.
    • (1997) J Biol Chem , vol.272 , pp. 31941-31944
    • Wong, A.1    Pero, R.2    Ormonde, P.3    Tavtigian, S.4    Bartel, P.5
  • 6
    • 14144253224 scopus 로고    scopus 로고
    • The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction
    • Yang H, Li Q, Fan J, Holloman W, Pavletich N. The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction. Nature 2005, 433:653-7.
    • (2005) Nature , vol.433 , pp. 653-657
    • Yang, H.1    Li, Q.2    Fan, J.3    Holloman, W.4    Pavletich, N.5
  • 7
    • 0033533731 scopus 로고    scopus 로고
    • Absence of Brca2 causes genome instability by chromosome breakage and loss associated with centrosome amplification
    • Tutt A, Gabriel A, Bertwistle D. Absence of Brca2 causes genome instability by chromosome breakage and loss associated with centrosome amplification. Curr Biol 1999, 9:1107-10.
    • (1999) Curr Biol , vol.9 , pp. 1107-1110
    • Tutt, A.1    Gabriel, A.2    Bertwistle, D.3
  • 8
    • 7444222440 scopus 로고    scopus 로고
    • Abnormal cytokinesis in cells deficient in the breast cancer susceptibility protein BRCA2
    • Daniels M, Wang Y, Lee M, Venkitaraman A. Abnormal cytokinesis in cells deficient in the breast cancer susceptibility protein BRCA2. Science 2004, 306:876-9.
    • (2004) Science , vol.306 , pp. 876-879
    • Daniels, M.1    Wang, Y.2    Lee, M.3    Venkitaraman, A.4
  • 9
    • 43449099740 scopus 로고    scopus 로고
    • A CRM1-mediated nuclear export signal governs cytoplasmic localization of BRCA2 and is essential for centrosomal localization of BRCA2
    • Han X, Saito H, Miki Y, Nakanishi A. A CRM1-mediated nuclear export signal governs cytoplasmic localization of BRCA2 and is essential for centrosomal localization of BRCA2. Oncogene 2008, 27:2969-77.
    • (2008) Oncogene , vol.27 , pp. 2969-2977
    • Han, X.1    Saito, H.2    Miki, Y.3    Nakanishi, A.4
  • 10
    • 33847050182 scopus 로고    scopus 로고
    • Interference with BRCA2, which localizes to the centrosome during S and early M phase, leads to abnormal nuclear division
    • Nakanishi A, Han X, Saito H. Interference with BRCA2, which localizes to the centrosome during S and early M phase, leads to abnormal nuclear division. Biochem Biophys Res Commun 2007, 355:34-40.
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 34-40
    • Nakanishi, A.1    Han, X.2    Saito, H.3
  • 11
    • 0029620499 scopus 로고
    • Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression
    • Foisner R, Bohn W, Mannweiler K, Wiche G. Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression. J Struct Biol 1995, 115:304-17.
    • (1995) J Struct Biol , vol.115 , pp. 304-317
    • Foisner, R.1    Bohn, W.2    Mannweiler, K.3    Wiche, G.4
  • 12
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • Foisner R, Wiche G. Structure and hydrodynamic properties of plectin molecules. J Mol Biol 1987, 198:515-31.
    • (1987) J Mol Biol , vol.198 , pp. 515-531
    • Foisner, R.1    Wiche, G.2
  • 13
    • 33845987032 scopus 로고    scopus 로고
    • Plectin defects in epidermolysis bullosa simplex with muscular dystrophy
    • McMillan J, Akiyama M, Rouan F. Plectin defects in epidermolysis bullosa simplex with muscular dystrophy. Muscle Nerve 2007, 35:24-35.
    • (2007) Muscle Nerve , vol.35 , pp. 24-35
    • McMillan, J.1    Akiyama, M.2    Rouan, F.3
  • 14
    • 41049090068 scopus 로고    scopus 로고
    • The influence of plectin deficiency on stability of cytokeratin18 in hepatocellular carcinoma
    • Cheng C, Liu Y, Ho C. The influence of plectin deficiency on stability of cytokeratin18 in hepatocellular carcinoma. J Mol Histol 2008, 39:209-16.
    • (2008) J Mol Histol , vol.39 , pp. 209-216
    • Cheng, C.1    Liu, Y.2    Ho, C.3
  • 15
    • 43249086840 scopus 로고    scopus 로고
    • Targeted nanoparticles for imaging incipient pancreatic ductal adenocarcinoma
    • Kelly K, Bardeesy N, Anbazhagan R. Targeted nanoparticles for imaging incipient pancreatic ductal adenocarcinoma. PLoS Med 2008, 5:e85.
    • (2008) PLoS Med , vol.5
    • Kelly, K.1    Bardeesy, N.2    Anbazhagan, R.3
  • 16
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • Svitkina T, Verkhovsky A, Borisy G. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J Cell Biol 1996, 135:991-1007.
    • (1996) J Cell Biol , vol.135 , pp. 991-1007
    • Svitkina, T.1    Verkhovsky, A.2    Borisy, G.3
  • 17
    • 0032213892 scopus 로고    scopus 로고
    • Not just scaffolding: plectin regulates actin dynamics in cultured cells
    • Andrä K, Nikolic B, Stöcher M, Drenckhahn D, Wiche G. Not just scaffolding: plectin regulates actin dynamics in cultured cells. Genes Dev 1998, 12:3442-51.
    • (1998) Genes Dev , vol.12 , pp. 3442-3451
    • Andrä, K.1    Nikolic, B.2    Stöcher, M.3    Drenckhahn, D.4    Wiche, G.5
  • 18
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions
    • Nikolic B, Mac Nulty E, Mir B, Wiche G. Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J Cell Biol 1996, 134:1455-67.
    • (1996) J Cell Biol , vol.134 , pp. 1455-1467
    • Nikolic, B.1    Mac Nulty, E.2    Mir, B.3    Wiche, G.4
  • 19
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche G. Role of plectin in cytoskeleton organization and dynamics. J Cell Sci 1998, 111(Pt 17):2477-86.
    • (1998) J Cell Sci , vol.111 , Issue.PT 17 , pp. 2477-2486
    • Wiche, G.1
  • 20
    • 34548601698 scopus 로고    scopus 로고
    • Cytolinker cross-talk: periplakin N-terminus interacts with plectin to regulate keratin organisation and epithelial migration
    • Boczonadi V, McInroy L, Määttä A. Cytolinker cross-talk: periplakin N-terminus interacts with plectin to regulate keratin organisation and epithelial migration. Exp Cell Res 2007, 313:3579-91.
    • (2007) Exp Cell Res , vol.313 , pp. 3579-3591
    • Boczonadi, V.1    McInroy, L.2    Määttä, A.3
  • 21
    • 84954358370 scopus 로고    scopus 로고
    • Plectin deficiency affects precursor formation and dynamics of vimentin networks
    • Spurny R, Gregor M, Castañón M, Wiche G. Plectin deficiency affects precursor formation and dynamics of vimentin networks. Exp Cell Res 2008, 314:3570-80.
    • (2008) Exp Cell Res , vol.314 , pp. 3570-3580
    • Spurny, R.1    Gregor, M.2    Castañón, M.3    Wiche, G.4
  • 22
    • 0030020359 scopus 로고    scopus 로고
    • M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase
    • Foisner R, Malecz N, Dressel N, Stadler C, Wiche G. M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase. Mol Biol Cell 1996, 7:273-88.
    • (1996) Mol Biol Cell , vol.7 , pp. 273-288
    • Foisner, R.1    Malecz, N.2    Dressel, N.3    Stadler, C.4    Wiche, G.5
  • 23
    • 0025797361 scopus 로고
    • Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • Foisner R, Traub P, Wiche G. Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc Natl Acad Sci U S A 1991, 88:3812-6.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 24
    • 28544437813 scopus 로고    scopus 로고
    • Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin
    • Wilhelmsen K, Litjens S, Kuikman I. Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J Cell Biol 2005, 171:799-810.
    • (2005) J Cell Biol , vol.171 , pp. 799-810
    • Wilhelmsen, K.1    Litjens, S.2    Kuikman, I.3
  • 25
    • 0029873478 scopus 로고    scopus 로고
    • Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site
    • Malecz N, Foisner R, Stadler C, Wiche G. Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site. J Biol Chem 1996, 271:8203-8.
    • (1996) J Biol Chem , vol.271 , pp. 8203-8208
    • Malecz, N.1    Foisner, R.2    Stadler, C.3    Wiche, G.4
  • 26
    • 0035197616 scopus 로고    scopus 로고
    • Plectin repeats and modules: strategic cysteines and their presumed impact on cytolinker functions
    • Janda L, Damborský J, Rezniczek G, Wiche G. Plectin repeats and modules: strategic cysteines and their presumed impact on cytolinker functions. BioEssays 2001, 23:1064-9.
    • (2001) BioEssays , vol.23 , pp. 1064-1069
    • Janda, L.1    Damborský, J.2    Rezniczek, G.3    Wiche, G.4
  • 27
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi L, Cammett T, Desrosiers D, Peng Z. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci 2004, 13:1435-48.
    • (2004) Protein Sci , vol.13 , pp. 1435-1448
    • Mosavi, L.1    Cammett, T.2    Desrosiers, D.3    Peng, Z.4
  • 28
    • 20444418092 scopus 로고    scopus 로고
    • How dynein helps the cell find its center: a servomechanical model
    • Vallee R, Stehman S. How dynein helps the cell find its center: a servomechanical model. Trends Cell Biol 2005, 15:288-94.
    • (2005) Trends Cell Biol , vol.15 , pp. 288-294
    • Vallee, R.1    Stehman, S.2
  • 30
    • 0026032167 scopus 로고
    • Monoclonal antibody mapping of structural and functional plectin epitopes
    • Foisner R, Feldman B, Sander L, Wiche G. Monoclonal antibody mapping of structural and functional plectin epitopes. J Cell Biol 1991, 112:397-405.
    • (1991) J Cell Biol , vol.112 , pp. 397-405
    • Foisner, R.1    Feldman, B.2    Sander, L.3    Wiche, G.4
  • 31
    • 0346094458 scopus 로고    scopus 로고
    • The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus
    • Malone C, Misner L, Le Bot N. The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus. Cell 2003, 115:825-36.
    • (2003) Cell , vol.115 , pp. 825-836
    • Malone, C.1    Misner, L.2    Le Bot, N.3
  • 32
    • 1842715906 scopus 로고    scopus 로고
    • Centrosomes: hooked on the nucleus
    • Gönczy P. Centrosomes: hooked on the nucleus. Curr Biol 2004, 14:R268-70.
    • (2004) Curr Biol , vol.14
    • Gönczy, P.1
  • 33
    • 34548818532 scopus 로고    scopus 로고
    • A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane
    • Salpingidou G, Smertenko A, Hausmanowa-Petrucewicz I, Hussey P, Hutchison C. A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane. J Cell Biol 2007, 178:897-904.
    • (2007) J Cell Biol , vol.178 , pp. 897-904
    • Salpingidou, G.1    Smertenko, A.2    Hausmanowa-Petrucewicz, I.3    Hussey, P.4    Hutchison, C.5
  • 34
    • 44649117902 scopus 로고    scopus 로고
    • Centrosome amplification can initiate tumorigenesis in flies
    • Basto R, Brunk K, Vinadogrova T. Centrosome amplification can initiate tumorigenesis in flies. Cell 2008, 133:1032-42.
    • (2008) Cell , vol.133 , pp. 1032-1042
    • Basto, R.1    Brunk, K.2    Vinadogrova, T.3
  • 35
    • 49649092093 scopus 로고    scopus 로고
    • Centrosome dysfunction in drosophila neural stem cells causes tumors that are not due to genome instability
    • Castellanos E, Dominguez P, Gonzalez C. Centrosome dysfunction in drosophila neural stem cells causes tumors that are not due to genome instability. Curr Biol 2008, 18:1209-14.
    • (2008) Curr Biol , vol.18 , pp. 1209-1214
    • Castellanos, E.1    Dominguez, P.2    Gonzalez, C.3
  • 36
    • 0037133211 scopus 로고    scopus 로고
    • Centrosome amplification drives chromosomal instability in breast tumor development
    • Lingle W, Barrett S, Negron V. Centrosome amplification drives chromosomal instability in breast tumor development. Proc Natl Acad Sci U S A 2002, 99:1978-83.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 1978-1983
    • Lingle, W.1    Barrett, S.2    Negron, V.3
  • 37
    • 0037112246 scopus 로고    scopus 로고
    • Chromosomal biomarkers of genomic instability relevant to cancer
    • Fenech M. Chromosomal biomarkers of genomic instability relevant to cancer. Drug Discov Today 2002, 7:1128-37.
    • (2002) Drug Discov Today , vol.7 , pp. 1128-1137
    • Fenech, M.1
  • 38
    • 34047154552 scopus 로고    scopus 로고
    • An increased micronucleus frequency in peripheral blood lymphocytes predicts the risk of cancer in humans
    • Bonassi S, Znaor A, Ceppi M. An increased micronucleus frequency in peripheral blood lymphocytes predicts the risk of cancer in humans. Carcinogenesis 2007, 28:625-31.
    • (2007) Carcinogenesis , vol.28 , pp. 625-631
    • Bonassi, S.1    Znaor, A.2    Ceppi, M.3


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