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Volumn 22, Issue 9, 2015, Pages 1540-1550

Nesprin-2-dependent ERK1/2 compartmentalisation regulates the DNA damage response in vascular smooth muscle cell ageing

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; CELL PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 3; NESPRIN 2; PROMYELOCYTIC LEUKEMIA PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; LAMIN A; MITOGEN ACTIVATED PROTEIN KINASE 1; NERVE PROTEIN; NUCLEAR PROTEIN; PRELAMIN A; SYNE2 PROTEIN, HUMAN;

EID: 84938966173     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2015.12     Document Type: Article
Times cited : (31)

References (36)
  • 1
    • 80051800674 scopus 로고    scopus 로고
    • Role of DNA damage in atherosclerosis-bystander or participant?
    • Gray K, Bennett M. Role of DNA damage in atherosclerosis-bystander or participant? Biochem Pharmacol 2011; 82: 693-700.
    • (2011) Biochem Pharmacol , vol.82 , pp. 693-700
    • Gray, K.1    Bennett, M.2
  • 2
    • 77953023624 scopus 로고    scopus 로고
    • Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging
    • Ragnauth CD, Warren DT, Liu Y, McNair R, Tajsic T, Figg N et al. Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging. Circulation 2010; 121: 2200-2210.
    • (2010) Circulation , vol.121 , pp. 2200-2210
    • Ragnauth, C.D.1    Warren, D.T.2    Liu, Y.3    McNair, R.4    Tajsic, T.5    Figg, N.6
  • 3
    • 84879808450 scopus 로고    scopus 로고
    • Prelamin A accelerates vascular calcification via activation of the DNA damage response and senescence-associated secretory phenotype in vascular smooth muscle cells
    • Liu Y, Drozdov I, Shroff R, Beltran LE, Shanahan CM. Prelamin A accelerates vascular calcification via activation of the DNA damage response and senescence-associated secretory phenotype in vascular smooth muscle cells. Circ Res 2013; 112: e99-109.
    • (2013) Circ Res , vol.112 , pp. e99-109
    • Liu, Y.1    Drozdov, I.2    Shroff, R.3    Beltran, L.E.4    Shanahan, C.M.5
  • 4
    • 84871501642 scopus 로고    scopus 로고
    • The nuclear lamins: Flexibility in function
    • Burke B, Stewart CL. The nuclear lamins: flexibility in function. Nat Rev Mol Cell Biol 2013; 14: 13-24.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 13-24
    • Burke, B.1    Stewart, C.L.2
  • 5
    • 78549252392 scopus 로고    scopus 로고
    • Identification of differential protein interactors of lamin A and progerin
    • Kubben N, Voncken JW, Demmers J, Calis C, van Almen G, Pinto Y et al. Identification of differential protein interactors of lamin A and progerin. Nucleus 2010; 1: 513-525.
    • (2010) Nucleus , vol.1 , pp. 513-525
    • Kubben, N.1    Voncken, J.W.2    Demmers, J.3    Calis, C.4    Van Almen, G.5    Pinto, Y.6
  • 6
    • 84877071045 scopus 로고    scopus 로고
    • A-type lamins maintain the positional stability of DNA damage repair foci in mammalian nuclei
    • Mahen R, Hattori H, Lee M, Sharma P, Jeyasekharan AD, Venkitaraman AR. A-type lamins maintain the positional stability of DNA damage repair foci in mammalian nuclei. PLoS One 2013; 8: e61893.
    • (2013) PLoS One , vol.8 , pp. e61893
    • Mahen, R.1    Hattori, H.2    Lee, M.3    Sharma, P.4    Jeyasekharan, A.D.5    Venkitaraman, A.R.6
  • 7
    • 22544466685 scopus 로고    scopus 로고
    • Genomic instability in laminopathy-based premature aging
    • Liu B, Wang J, Chan KM, Tjia WM, Deng W, Guan X et al. Genomic instability in laminopathy-based premature aging. Nat Med 2005; 11: 780-785.
    • (2005) Nat Med , vol.11 , pp. 780-785
    • Liu, B.1    Wang, J.2    Chan, K.M.3    Tjia, W.M.4    Deng, W.5    Guan, X.6
  • 8
    • 79954626173 scopus 로고    scopus 로고
    • Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome
    • Liu GH, Barkho BZ, Ruiz S, Diep D, Qu J, Yang SL et al. Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome. Nature 2011; 472: 221-225.
    • (2011) Nature , vol.472 , pp. 221-225
    • Liu, G.H.1    Barkho, B.Z.2    Ruiz, S.3    Diep, D.4    Qu, J.5    Yang, S.L.6
  • 9
    • 84863613755 scopus 로고    scopus 로고
    • Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds
    • Rajgor D, Mellad JA, Autore F, Zhang Q, Shanahan CM. Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds. PLoS One 2012; 7: e40098.
    • (2012) PLoS One , vol.7 , pp. e40098
    • Rajgor, D.1    Mellad, J.A.2    Autore, F.3    Zhang, Q.4    Shanahan, C.M.5
  • 10
    • 74049100497 scopus 로고    scopus 로고
    • Novel nuclear nesprin-2 variants tether active extracellular signal-regulated MAPK1 and MAPK2 at promyelocytic leukemia protein nuclear bodies and act to regulate smooth muscle cell proliferation
    • Warren DT, Tajsic T, Mellad JA, Searles R, Zhang Q, Shanahan CM. Novel nuclear nesprin-2 variants tether active extracellular signal-regulated MAPK1 and MAPK2 at promyelocytic leukemia protein nuclear bodies and act to regulate smooth muscle cell proliferation. J Biol Chem 2010; 285: 1311-1320.
    • (2010) J Biol Chem , vol.285 , pp. 1311-1320
    • Warren, D.T.1    Tajsic, T.2    Mellad, J.A.3    Searles, R.4    Zhang, Q.5    Shanahan, C.M.6
  • 11
    • 33847066413 scopus 로고    scopus 로고
    • Extracellular signal-related kinase positively regulates ataxia telangiectasia mutated, homologous recombination repair, and the DNA damage response
    • Golding SE, Rosenberg E, Neill S, Dent P, Povirk LF, Valerie K. Extracellular signal-related kinase positively regulates ataxia telangiectasia mutated, homologous recombination repair, and the DNA damage response. Cancer Res 2007; 67: 1046-1053.
    • (2007) Cancer Res , vol.67 , pp. 1046-1053
    • Golding, S.E.1    Rosenberg, E.2    Neill, S.3    Dent, P.4    Povirk, L.F.5    Valerie, K.6
  • 12
    • 33644522087 scopus 로고    scopus 로고
    • ERK activity facilitates activation of the S-phase DNA damage checkpoint by modulating ATR function
    • Wu D, Chen B, Parihar K, He L, Fan C, Zhang J et al. ERK activity facilitates activation of the S-phase DNA damage checkpoint by modulating ATR function. Oncogene 2006; 25: 1153-1164.
    • (2006) Oncogene , vol.25 , pp. 1153-1164
    • Wu, D.1    Chen, B.2    Parihar, K.3    He, L.4    Fan, C.5    Zhang, J.6
  • 15
    • 0142106346 scopus 로고    scopus 로고
    • Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization
    • Kurki S, Latonen L, Laiho M. Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization. J Cell Sci 2003; 116: 3917-3925.
    • (2003) J Cell Sci , vol.116 , pp. 3917-3925
    • Kurki, S.1    Latonen, L.2    Laiho, M.3
  • 16
    • 77955655466 scopus 로고    scopus 로고
    • Both ERK1 and ERK2 kinases promote G2/M arrest in etoposide-treated MCF7 cells by facilitating ATM activation
    • Wei F, Xie Y, Tao L, Tang D. Both ERK1 and ERK2 kinases promote G2/M arrest in etoposide-treated MCF7 cells by facilitating ATM activation. Cell Signal 2010; 22: 1783-1789.
    • (2010) Cell Signal , vol.22 , pp. 1783-1789
    • Wei, F.1    Xie, Y.2    Tao, L.3    Tang, D.4
  • 18
    • 84863511156 scopus 로고    scopus 로고
    • Trajectories and nuclear arrangement of PML bodies are influenced by A-type lamin deficiency
    • Stixova L, Matula P, Kozubek S, Gombitova A, Cmarko D, Raska I et al. Trajectories and nuclear arrangement of PML bodies are influenced by A-type lamin deficiency. Biol Cell 2012; 104: 418-432.
    • (2012) Biol Cell , vol.104 , pp. 418-432
    • Stixova, L.1    Matula, P.2    Kozubek, S.3    Gombitova, A.4    Cmarko, D.5    Raska, I.6
  • 19
    • 79961083402 scopus 로고    scopus 로고
    • Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice
    • Krishnan V, Chow MZ, Wang Z, Zhang L, Liu B, Liu X et al. Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice. Proc Natl Acad Sci USA 2011; 108: 12325-12330.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 12325-12330
    • Krishnan, V.1    Chow, M.Z.2    Wang, Z.3    Zhang, L.4    Liu, B.5    Liu, X.6
  • 20
    • 84901844237 scopus 로고    scopus 로고
    • Mechanisms controlling the smooth muscle cell death in progeria via down-regulation of poly(ADP-ribose) polymerase 1
    • Zhang H, Xiong ZM, Cao K. Mechanisms controlling the smooth muscle cell death in progeria via down-regulation of poly(ADP-ribose) polymerase 1. Proc Natl Acad Sci USA 2014; 111: E2261-E2270.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. E2261-E2270
    • Zhang, H.1    Xiong, Z.M.2    Cao, K.3
  • 21
    • 58149186768 scopus 로고    scopus 로고
    • Fast regulation of AP-1 activity through interaction of lamin A/C, ERK1/2, and c-Fos at the nuclear envelope
    • Gonzalez JM, Navarro-Puche A, Casar B, Crespo P, Andres V. Fast regulation of AP-1 activity through interaction of lamin A/C, ERK1/2, and c-Fos at the nuclear envelope. J Cell Biol 2008; 183: 653-666.
    • (2008) J Cell Biol , vol.183 , pp. 653-666
    • Gonzalez, J.M.1    Navarro-Puche, A.2    Casar, B.3    Crespo, P.4    Andres, V.5
  • 22
    • 21844432667 scopus 로고    scopus 로고
    • Lamin A/Cdependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope
    • Libotte T, Zaim H, Abraham S, Padmakumar VC, Schneider M, Lu W et al. Lamin A/Cdependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope. Mol Biol Cell 2005; 16: 3411-3424.
    • (2005) Mol Biol Cell , vol.16 , pp. 3411-3424
    • Libotte, T.1    Zaim, H.2    Abraham, S.3    Padmakumar, V.C.4    Schneider, M.5    Lu, W.6
  • 23
    • 84882573661 scopus 로고    scopus 로고
    • Mutations in LMNA modulate the lamin A-Nesprin-2 interaction and cause LINC complex alterations
    • Yang L, Munck M, Swaminathan K, Kapinos LE, Noegel AA, Neumann S. Mutations in LMNA modulate the lamin A-Nesprin-2 interaction and cause LINC complex alterations. PLoS One 2013; 8: e71850.
    • (2013) PLoS One , vol.8 , pp. e71850
    • Yang, L.1    Munck, M.2    Swaminathan, K.3    Kapinos, L.E.4    Noegel, A.A.5    Neumann, S.6
  • 24
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • Dellaire G, Bazett-Jones DP. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 2004; 26: 963-977.
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 25
    • 0037665234 scopus 로고    scopus 로고
    • ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation
    • Barr SM, Leung CG, Chang EE, Cimprich KA. ATR kinase activity regulates the intranuclear translocation of ATR and RPA following ionizing radiation. Curr Biol 2003; 13: 1047-1051.
    • (2003) Curr Biol , vol.13 , pp. 1047-1051
    • Barr, S.M.1    Leung, C.G.2    Chang, E.E.3    Cimprich, K.A.4
  • 26
    • 0037979238 scopus 로고    scopus 로고
    • PML colocalizes with and stabilizes the DNA damage response protein TopBP1
    • Xu ZX, Timanova-Atanasova A, Zhao RX, Chang KS. PML colocalizes with and stabilizes the DNA damage response protein TopBP1. Mol Cell Biol 2003; 23: 4247-4256.
    • (2003) Mol Cell Biol , vol.23 , pp. 4247-4256
    • Xu, Z.X.1    Timanova-Atanasova, A.2    Zhao, R.X.3    Chang, K.S.4
  • 27
    • 0034749425 scopus 로고    scopus 로고
    • DNA damage-dependent nuclear dynamics of the Mre11 complex
    • Mirzoeva OK, Petrini JH. DNA damage-dependent nuclear dynamics of the Mre11 complex. Mol Cell Biol 2001; 21: 281-288.
    • (2001) Mol Cell Biol , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 28
    • 84879685969 scopus 로고    scopus 로고
    • BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction
    • Yang Q, Liao L, Deng X, Chen R, Gray NS, Yates 3rd JR et al. BMK1 is involved in the regulation of p53 through disrupting the PML-MDM2 interaction. Oncogene 2013; 32: 3156-3164.
    • (2013) Oncogene , vol.32 , pp. 3156-3164
    • Yang, Q.1    Liao, L.2    Deng, X.3    Chen, R.4    Gray, N.S.5    Yates, J.R.6
  • 29
    • 84899145875 scopus 로고    scopus 로고
    • The tumor suppressor PML specifically accumulates at RPA/Rad51-containing DNA damage repair foci but is nonessential for DNA damage-induced fibroblast senescence
    • Munch S, Weidtkamp-Peters S, Klement K, Grigaravicius P, Monajembashi S, Salomoni P et al. The tumor suppressor PML specifically accumulates at RPA/Rad51-containing DNA damage repair foci but is nonessential for DNA damage-induced fibroblast senescence. Mol Cell Biol 2014; 34: 1733-1746.
    • (2014) Mol Cell Biol , vol.34 , pp. 1733-1746
    • Munch, S.1    Weidtkamp-Peters, S.2    Klement, K.3    Grigaravicius, P.4    Monajembashi, S.5    Salomoni, P.6
  • 30
    • 0037066686 scopus 로고    scopus 로고
    • ERK activation mediates cell cycle arrest and apoptosis after DNA damage independently of p53
    • Tang D, Wu D, Hirao A, Lahti JM, Liu L, Mazza B et al. ERK activation mediates cell cycle arrest and apoptosis after DNA damage independently of p53. J Biol Chem 2002; 277: 12710-12717.
    • (2002) J Biol Chem , vol.277 , pp. 12710-12717
    • Tang, D.1    Wu, D.2    Hirao, A.3    Lahti, J.M.4    Liu, L.5    Mazza, B.6
  • 31
    • 84877094603 scopus 로고    scopus 로고
    • Large-scale modelling of the divergent spectrin repeats in nesprins: Giant modular proteins
    • Autore F, Pfuhl M, Quan X, Williams A, Roberts RG, Shanahan CM et al. Large-scale modelling of the divergent spectrin repeats in nesprins: giant modular proteins. PLoS One 2013; 8: e63633.
    • (2013) PLoS One , vol.8 , pp. e63633
    • Autore, F.1    Pfuhl, M.2    Quan, X.3    Williams, A.4    Roberts, R.G.5    Shanahan, C.M.6
  • 32
    • 77955661779 scopus 로고    scopus 로고
    • Stabilization of the spectrin-like domains of nesprin-1alpha by the evolutionarily conserved "adaptive" domain
    • Zhong Z, Chang SA, Kalinowski A, Wilson KL, Dahl KN. Stabilization of the spectrin-like domains of nesprin-1alpha by the evolutionarily conserved "adaptive" domain. Cell Mol Bioeng 2010; 3: 139-150.
    • (2010) Cell Mol Bioeng , vol.3 , pp. 139-150
    • Zhong, Z.1    Chang, S.A.2    Kalinowski, A.3    Wilson, K.L.4    Dahl, K.N.5
  • 33
    • 33751294581 scopus 로고    scopus 로고
    • The role of scaffold proteins in MEK/ERK signalling
    • Sacks DB. The role of scaffold proteins in MEK/ERK signalling. Biochem Soc Trans 2006; 34: 833-836.
    • (2006) Biochem Soc Trans , vol.34 , pp. 833-836
    • Sacks, D.B.1
  • 35
    • 0032508538 scopus 로고    scopus 로고
    • MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade
    • Schaeffer HJ, Catling AD, Eblen ST, Collier LS, Krauss A, Weber MJ. MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 1998; 281: 1668-1671.
    • (1998) Science , vol.281 , pp. 1668-1671
    • Schaeffer, H.J.1    Catling, A.D.2    Eblen, S.T.3    Collier, L.S.4    Krauss, A.5    Weber, M.J.6
  • 36
    • 0033598796 scopus 로고    scopus 로고
    • Medial localization of mineralization-regulating proteins in association with Monckeberg's sclerosis: Evidence for smooth muscle cell-mediated vascular calcification
    • Shanahan CM, Cary NR, Salisbury JR, Proudfoot D, Weissberg PL, Edmonds ME. Medial localization of mineralization-regulating proteins in association with Monckeberg's sclerosis: evidence for smooth muscle cell-mediated vascular calcification. Circulation 1999; 100: 2168-2176.
    • (1999) Circulation , vol.100 , pp. 2168-2176
    • Shanahan, C.M.1    Cary, N.R.2    Salisbury, J.R.3    Proudfoot, D.4    Weissberg, P.L.5    Edmonds, M.E.6


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