메뉴 건너뛰기




Volumn 23, Issue 9, 2016, Pages 1448-1457

PACS-2 mediates the ATM and NF-κB-dependent induction of anti-apoptotic Bcl-xL in response to DNA damage

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; CASPASE 3; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PHOSPHOFURIN ACIDIC CLUSTER SORTING PROTEIN 2; PROTEIN; PROTEIN BCL XL; SMALL INTERFERING RNA; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; CYCLIN DEPENDENT KINASE INHIBITOR 1A; PACS2 PROTEIN, MOUSE; PROTEIN BCL X; TUMOR NECROSIS FACTOR; VESICULAR TRANSPORT PROTEIN;

EID: 84959556923     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2016.23     Document Type: Article
Times cited : (32)

References (59)
  • 1
    • 84877757564 scopus 로고    scopus 로고
    • Molecular basis of NF-kappaB signaling
    • Napetschnig J, Wu H. Molecular basis of NF-kappaB signaling. Annu Rev Biophys 2013; 42: 443-468.
    • (2013) Annu Rev Biophys , vol.42 , pp. 443-468
    • Napetschnig, J.1    Wu, H.2
  • 2
    • 0033621956 scopus 로고    scopus 로고
    • The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L)
    • Chen C, Edelstein LC, Gelinas C. The Rel/NF-kappaB family directly activates expression of the apoptosis inhibitor Bcl-x(L). Mol Cell Biol. 2000; 20: 2687-2695.
    • (2000) Mol Cell Biol. , vol.20 , pp. 2687-2695
    • Chen, C.1    Edelstein, L.C.2    Gelinas, C.3
  • 3
    • 0344897663 scopus 로고    scopus 로고
    • Bcl-2 on the endoplasmic reticulum: Protecting the mitochondria from a distance
    • Thomenius MJ, Distelhorst CW. Bcl-2 on the endoplasmic reticulum: protecting the mitochondria from a distance. J Cell Sci 2003; 116 (Pt 22): 4493-4499.
    • (2003) J Cell Sci , vol.116 , pp. 4493-4499
    • Thomenius, M.J.1    Distelhorst, C.W.2
  • 4
    • 84863522547 scopus 로고    scopus 로고
    • Distinct roles of mitochondriaand ER-localized Bcl-xL in apoptosis resistance and Ca2+ homeostasis
    • Eno CO, Eckenrode EF, Olberding KE, Zhao G, White C, Li C. Distinct roles of mitochondriaand ER-localized Bcl-xL in apoptosis resistance and Ca2+ homeostasis. Mol Biol Cell 2012; 23: 2605-2618.
    • (2012) Mol Biol Cell , vol.23 , pp. 2605-2618
    • Eno, C.O.1    Eckenrode, E.F.2    Olberding, K.E.3    Zhao, G.4    White, C.5    Li, C.6
  • 6
  • 7
    • 80052619373 scopus 로고    scopus 로고
    • Bcl-2 interaction with the inositol 1 4,5-trisphosphate receptor: Role in Ca(2+) signaling and disease
    • Distelhorst CW, Bootman MD. Bcl-2 interaction with the inositol 1,4,5-trisphosphate receptor: role in Ca(2+) signaling and disease. Cell Calcium 2011; 50: 234-241.
    • (2011) Cell Calcium , vol.50 , pp. 234-241
    • Distelhorst, C.W.1    Bootman, M.D.2
  • 8
    • 68149108384 scopus 로고    scopus 로고
    • PUMA, a potent killer with or without p53
    • Yu J, Zhang L. PUMA, a potent killer with or without p53. Oncogene 2008; 27(Suppl 1): S71-S83.
    • (2008) Oncogene , vol.27 , pp. S71-S83
    • Yu, J.1    Zhang, L.2
  • 9
    • 84874044758 scopus 로고    scopus 로고
    • PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis
    • Follis AV, Chipuk JE, Fisher JC, Yun MK, Grace CR, Nourse A et al. PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis. Nat Chem Biol 2013; 9: 163-168.
    • (2013) Nat Chem Biol , vol.9 , pp. 163-168
    • Follis, A.V.1    Chipuk, J.E.2    Fisher, J.C.3    Yun, M.K.4    Grace, C.R.5    Nourse, A.6
  • 10
    • 79959658547 scopus 로고    scopus 로고
    • NF-kappaB and cancer: A paradigm of Yin-Yang
    • Xiao G, Fu J. NF-kappaB and cancer: a paradigm of Yin-Yang. Am J Cancer Res 2011; 1: 192-221.
    • (2011) Am J Cancer Res , vol.1 , pp. 192-221
    • Xiao, G.1    Fu, J.2
  • 11
    • 0032589462 scopus 로고    scopus 로고
    • IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain
    • Sakurai H, Chiba H, Miyoshi H, Sugita T, Toriumi W. IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain. J Biol Chem 1999; 274: 30353-30356.
    • (1999) J Biol Chem , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 12
    • 77957252647 scopus 로고    scopus 로고
    • The IKK complex, a central regulator of NF-kappaB activation
    • Israel A. The IKK complex, a central regulator of NF-kappaB activation. Cold Spring Harb Perspect Biol 2010; 2: a000158.
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , pp. a000158
    • Israel, A.1
  • 13
    • 0034663779 scopus 로고    scopus 로고
    • The NF-kappa B cascade is important in Bcl-xL expression and for the anti-apoptotic effects of the CD28 receptor in primary human CD4+ lymphocytes
    • Khoshnan A, Tindell C, Laux I, Bae D, Bennett B, Nel AE. The NF-kappa B cascade is important in Bcl-xL expression and for the anti-apoptotic effects of the CD28 receptor in primary human CD4+ lymphocytes. J Immunol 2000; 165: 1743-1754.
    • (2000) J Immunol , vol.165 , pp. 1743-1754
    • Khoshnan, A.1    Tindell, C.2    Laux, I.3    Bae, D.4    Bennett, B.5    Nel, A.E.6
  • 14
    • 84921901945 scopus 로고    scopus 로고
    • DNA damage-induced NF-kappaB activation in human glioblastoma cells promotes miR-181b expression and cell proliferation
    • Xu RX, Liu RY, Wu CM, Zhao YS, Li Y, Yao YQ et al. DNA damage-induced NF-kappaB activation in human glioblastoma cells promotes miR-181b expression and cell proliferation. Cell Physiol Biochem 2015; 35: 913-925.
    • (2015) Cell Physiol Biochem , vol.35 , pp. 913-925
    • Xu, R.X.1    Liu, R.Y.2    Wu, C.M.3    Zhao, Y.S.4    Li, Y.5    Yao, Y.Q.6
  • 15
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-kappaB transcription factors in the immune system
    • Vallabhapurapu S, Karin M. Regulation and function of NF-kappaB transcription factors in the immune system. Annu Rev Immunol. 2009; 27: 693-733.
    • (2009) Annu Rev Immunol. , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 16
    • 33644538632 scopus 로고    scopus 로고
    • Molecular linkage between the kinase ATM and NFkappaB signaling in response to genotoxic stimuli
    • Wu ZH, Shi Y, Tibbetts RS, Miyamoto S. Molecular linkage between the kinase ATM and NFkappaB signaling in response to genotoxic stimuli. Science 2006; 311: 1141-1146.
    • (2006) Science , vol.311 , pp. 1141-1146
    • Zh, W.1    Shi, Y.2    Tibbetts, R.S.3    Miyamoto, S.4
  • 17
    • 77957333810 scopus 로고    scopus 로고
    • A cytoplasmic ATMTRAF6-cIAP1 module links nuclear DNA damage signaling to ubiquitin-mediated NF-kappaB activation
    • Hinz M, Stilmann M, Arslan SC, Khanna KK, Dittmar G, Scheidereit C. A cytoplasmic ATMTRAF6-cIAP1 module links nuclear DNA damage signaling to ubiquitin-mediated NF-kappaB activation. Mol Cell 2010; 40: 63-74.
    • (2010) Mol Cell , vol.40 , pp. 63-74
    • Hinz, M.1    Stilmann, M.2    Arslan, S.C.3    Khanna, K.K.4    Dittmar, G.5    Scheidereit, C.6
  • 18
    • 77957374335 scopus 로고    scopus 로고
    • ATM-and NEMO-dependent ELKS ubiquitination coordinates TAK1-mediated IKK activation in response to genotoxic stress
    • Wu ZH, Wong ET, Shi Y, Niu J, Chen Z, Miyamoto S et al. ATM-and NEMO-dependent ELKS ubiquitination coordinates TAK1-mediated IKK activation in response to genotoxic stress. Mol Cell 2010; 40: 75-86.
    • (2010) Mol Cell , vol.40 , pp. 75-86
    • Zh, W.1    Wong, E.T.2    Shi, Y.3    Niu, J.4    Chen, Z.5    Miyamoto, S.6
  • 19
    • 79960352030 scopus 로고    scopus 로고
    • A cytosolic ATM/NEMO/RIP1 complex recruits TAK1 to mediate the NF-kappaB and p38 mitogen-activated protein kinase (MAPK)/MAPK-activated protein 2 responses to DNA damage
    • Yang Y, Xia F, Hermance N, Mabb A, Simonson S, Morrissey S et al. A cytosolic ATM/NEMO/RIP1 complex recruits TAK1 to mediate the NF-kappaB and p38 mitogen-activated protein kinase (MAPK)/MAPK-activated protein 2 responses to DNA damage. Mol Cell Biol 2011; 31: 2774-2786.
    • (2011) Mol Cell Biol , vol.31 , pp. 2774-2786
    • Yang, Y.1    Xia, F.2    Hermance, N.3    Mabb, A.4    Simonson, S.5    Morrissey, S.6
  • 20
    • 65849216826 scopus 로고    scopus 로고
    • Akt and 14-3-3 control a PACS-2 homeostatic switch that integrates membrane traffic with TRAIL-induced apoptosis
    • Aslan JE, You H, Williamson DM, Endig J, Youker RT, Thomas L et al. Akt and 14-3-3 control a PACS-2 homeostatic switch that integrates membrane traffic with TRAIL-induced apoptosis. Mol Cell 2009; 34: 497-509.
    • (2009) Mol Cell , vol.34 , pp. 497-509
    • Aslan, J.E.1    You, H.2    Williamson, D.M.3    Endig, J.4    Youker, R.T.5    Thomas, L.6
  • 21
    • 44649173294 scopus 로고    scopus 로고
    • HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers major histocompatibility complex class i (MHC-I) down-regulation: Analysis using short interfering RNA and knock-out mice
    • Atkins KM, Thomas L, Youker RT, Harriff MJ, Pissani F, You H et al. HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers major histocompatibility complex class I (MHC-I) down-regulation: analysis using short interfering RNA and knock-out mice. J Biol Chem 2008; 283: 11772-11784.
    • (2008) J Biol Chem , vol.283 , pp. 11772-11784
    • Atkins, K.M.1    Thomas, L.2    Youker, R.T.3    Harriff, M.J.4    Pissani, F.5    You, H.6
  • 22
    • 84861708657 scopus 로고    scopus 로고
    • An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I
    • Dikeakos JD, Thomas L, Kwon G, Elferich J, Shinde U, Thomas G. An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I. Mol Biol Cell 2012; 23: 2184-2197.
    • (2012) Mol Biol Cell , vol.23 , pp. 2184-2197
    • Dikeakos, J.D.1    Thomas, L.2    Kwon, G.3    Elferich, J.4    Shinde, U.5    Thomas, G.6
  • 23
    • 84933056607 scopus 로고    scopus 로고
    • The sorting protein PACS-2 promotes ErbB signalling by regulating recycling of the metalloproteinase ADAM17
    • Dombernowsky SL, Samsoe-Petersen J, Petersen CH, Instrell R, Hedegaard AM, Thomas L et al. The sorting protein PACS-2 promotes ErbB signalling by regulating recycling of the metalloproteinase ADAM17. Nat Commun 2015; 6: 7518.
    • (2015) Nat Commun , vol.6 , pp. 7518
    • Dombernowsky, S.L.1    Samsoe-Petersen, J.2    Ch, P.3    Instrell, R.4    Hedegaard, A.M.5    Thomas, L.6
  • 24
    • 20144383835 scopus 로고    scopus 로고
    • Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation
    • Kottgen M, Benzing T, Simmen T, Tauber R, Buchholz B, Feliciangeli S et al. Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation. EMBO J 2005; 24: 705-716.
    • (2005) EMBO J , vol.24 , pp. 705-716
    • Kottgen, M.1    Benzing, T.2    Simmen, T.3    Tauber, R.4    Buchholz, B.5    Feliciangeli, S.6
  • 26
    • 84863809112 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) protein-induced lysosomal translocation of proapoptotic effectors is mediated by phosphofurin acidic cluster sorting protein-2 (PACS-2)
    • Werneburg NW, Bronk SF, Guicciardi ME, Thomas L, Dikeakos JD, Thomas G et al. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) protein-induced lysosomal translocation of proapoptotic effectors is mediated by phosphofurin acidic cluster sorting protein-2 (PACS-2). J Biol Chem 2012; 287: 24427-24437.
    • (2012) J Biol Chem , vol.287 , pp. 24427-24437
    • Werneburg, N.W.1    Bronk, S.F.2    Guicciardi, M.E.3    Thomas, L.4    Dikeakos, J.D.5    Thomas, G.6
  • 27
    • 20144385980 scopus 로고    scopus 로고
    • PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis
    • Simmen T, Aslan JE, Blagoveshchenskaya AD, Thomas L, Wan L, Xiang Y et al. PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis. EMBO J 2005; 24: 717-729.
    • (2005) EMBO J , vol.24 , pp. 717-729
    • Simmen, T.1    Aslan, J.E.2    Blagoveshchenskaya, A.D.3    Thomas, L.4    Wan, L.5    Xiang, Y.6
  • 28
    • 84922581149 scopus 로고    scopus 로고
    • The multifunctional sorting protein PACS-2 regulates SIRT1-mediated deacetylation of p53 to modulate p21-dependent cell-cycle arrest
    • Atkins KM, Thomas LL, Barroso-Gonzalez J, Thomas L, Auclair S, Yin J et al. The multifunctional sorting protein PACS-2 regulates SIRT1-mediated deacetylation of p53 to modulate p21-dependent cell-cycle arrest. Cell Rep 2014; 8: 1545-1557.
    • (2014) Cell Rep , vol.8 , pp. 1545-1557
    • Atkins, K.M.1    Thomas, L.L.2    Barroso-Gonzalez, J.3    Thomas, L.4    Auclair, S.5    Yin, J.6
  • 29
    • 85043657013 scopus 로고    scopus 로고
    • Endosome traffic machinery meets the p53-p21 axis
    • Barroso-Gonzalez J, Thomas G. Endosome traffic machinery meets the p53-p21 axis. Mol Cell Oncol 2015; 2: e975075.
    • (2015) Mol Cell Oncol , vol.2 , pp. e975075
    • Barroso-Gonzalez, J.1    Thomas, G.2
  • 30
  • 31
    • 0033595893 scopus 로고    scopus 로고
    • How NF-kappaB is activated: The role of the IkappaB kinase (IKK) complex
    • Karin M. How NF-kappaB is activated: the role of the IkappaB kinase (IKK) complex. Oncogene 1999; 18: 6867-6874.
    • (1999) Oncogene , vol.18 , pp. 6867-6874
    • Karin, M.1
  • 32
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function
    • Perkins ND. Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat Rev Mol Cell Biol 2007; 8: 49-62.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 33
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, Frye RA et al. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 2004; 23: 2369-2380.
    • (2004) EMBO J , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6
  • 34
    • 0035937809 scopus 로고    scopus 로고
    • ATM is required for IkappaB kinase (IKKk) activation in response to DNA double strand breaks
    • Li N, Banin S, Ouyang H, Li GC, Courtois G, Shiloh Y et al. ATM is required for IkappaB kinase (IKKk) activation in response to DNA double strand breaks. J Biol Chem 2001; 276: 8898-8903.
    • (2001) J Biol Chem , vol.276 , pp. 8898-8903
    • Li, N.1    Banin, S.2    Ouyang, H.3    Li, G.C.4    Courtois, G.5    Shiloh, Y.6
  • 35
    • 0032977359 scopus 로고    scopus 로고
    • A high dose of ionizing radiation induces tissue-specific activation of nuclear factor-kappaB in vivo
    • Zhou D, Brown SA, Yu T, Chen G, Barve S, Kang BC et al. A high dose of ionizing radiation induces tissue-specific activation of nuclear factor-kappaB in vivo. Radiat Res 1999; 151: 703-709.
    • (1999) Radiat Res , vol.151 , pp. 703-709
    • Zhou, D.1    Brown, S.A.2    Yu, T.3    Chen, G.4    Barve, S.5    Kang, B.C.6
  • 36
    • 1442306054 scopus 로고    scopus 로고
    • IkappaB-kinasebetadependent NF-kappaB activation provides radioprotection to the intestinal epithelium
    • Egan LJ, Eckmann L, Greten FR, Chae S, Li ZW, Myhre GM et al. IkappaB-kinasebetadependent NF-kappaB activation provides radioprotection to the intestinal epithelium. Proc Natl Acad Sci USA 2004; 101: 2452-2457.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2452-2457
    • Egan, L.J.1    Eckmann, L.2    Greten, F.R.3    Chae, S.4    Li, Z.W.5    Myhre, G.M.6
  • 37
    • 4344669657 scopus 로고    scopus 로고
    • Activation of nuclear factor kappaB in vivo selectively protects the murine small intestine against ionizing radiationinduced damage
    • Wang Y, Meng A, Lang H, Brown SA, Konopa JL, Kindy MS et al. Activation of nuclear factor kappaB In vivo selectively protects the murine small intestine against ionizing radiationinduced damage. Cancer Res 2004; 64: 6240-6246.
    • (2004) Cancer Res , vol.64 , pp. 6240-6246
    • Wang, Y.1    Meng, A.2    Lang, H.3    Brown, S.A.4    Konopa, J.L.5    Kindy, M.S.6
  • 38
    • 21344435495 scopus 로고    scopus 로고
    • Enhanced G2-M arrest by nuclear factor-{kappa}B-dependent p21waf1/cip1 induction
    • Wuerzberger-Davis SM, Chang PY, Berchtold C, Miyamoto S. Enhanced G2-M arrest by nuclear factor-{kappa}B-dependent p21waf1/cip1 induction. Mol Cancer Res 2005; 3: 345-353.
    • (2005) Mol Cancer Res , vol.3 , pp. 345-353
    • Wuerzberger-Davis, S.M.1    Chang, P.Y.2    Berchtold, C.3    Miyamoto, S.4
  • 39
    • 79953288925 scopus 로고    scopus 로고
    • Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK catalytic subunit
    • So EY, Ouchi T. Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK catalytic subunit. Exp Ther Med 2011; 2: 443-447.
    • (2011) Exp Ther Med , vol.2 , pp. 443-447
    • So, E.Y.1    Ouchi, T.2
  • 40
    • 84904777934 scopus 로고    scopus 로고
    • BRAT1 deficiency causes increased glucose metabolism and mitochondrial malfunction
    • So EY, Ouchi T. BRAT1 deficiency causes increased glucose metabolism and mitochondrial malfunction. BMC Cancer 2014; 14: 548.
    • (2014) BMC Cancer , vol.14 , pp. 548
    • So, E.Y.1    Ouchi, T.2
  • 41
    • 84898479582 scopus 로고    scopus 로고
    • Cellular inhibitor of apoptosis (cIAP)-mediated ubiquitination of phosphofurin acidic cluster sorting protein 2 (PACS-2) negatively regulates tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) cytotoxicity
    • Guicciardi ME, Werneburg NW, Bronk SF, Franke A, Yagita H, Thomas G et al. Cellular inhibitor of apoptosis (cIAP)-mediated ubiquitination of phosphofurin acidic cluster sorting protein 2 (PACS-2) negatively regulates tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) cytotoxicity. PLoS One 2014; 9: e92124.
    • (2014) PLoS One , vol.9 , pp. e92124
    • Guicciardi, M.E.1    Werneburg, N.W.2    Bronk, S.F.3    Franke, A.4    Yagita, H.5    Thomas, G.6
  • 42
    • 84874721105 scopus 로고    scopus 로고
    • Evidence for a common mechanism of SIRT1 regulation by allosteric activators
    • Hubbard BP, Gomes AP, Dai H, Li J, Case AW, Considine T et al. Evidence for a common mechanism of SIRT1 regulation by allosteric activators. Science 2013; 339: 1216-1219.
    • (2013) Science , vol.339 , pp. 1216-1219
    • Hubbard, B.P.1    Gomes, A.P.2    Dai, H.3    Li, J.4    Case, A.W.5    Considine, T.6
  • 43
    • 84875423827 scopus 로고    scopus 로고
    • The ATM protein kinase: Regulating the cellular response to genotoxic stress, more
    • Shiloh Y, Ziv Y. The ATM protein kinase: regulating the cellular response to genotoxic stress, more. Nat Rev Mol Cell Biol 2013; 14: 197-210.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 197-210
    • Shiloh, Y.1    Ziv, Y.2
  • 44
    • 33846128759 scopus 로고    scopus 로고
    • Calcium-dependent regulation of NEMO nuclear export in response to genotoxic stimuli
    • Berchtold CM, Wu ZH, Huang TT, Miyamoto S. Calcium-dependent regulation of NEMO nuclear export in response to genotoxic stimuli. Mol Cell Biol 2007; 27: 497-509.
    • (2007) Mol Cell Biol , vol.27 , pp. 497-509
    • Berchtold, C.M.1    Zh, W.2    Huang, T.T.3    Miyamoto, S.4
  • 45
    • 84858722471 scopus 로고    scopus 로고
    • DNA damage-dependent NF-kappaB activation: NEMO turns nuclear signaling inside out
    • McCool KW, Miyamoto S. DNA damage-dependent NF-kappaB activation: NEMO turns nuclear signaling inside out. Immunol Rev 2012; 246: 311-326.
    • (2012) Immunol Rev , vol.246 , pp. 311-326
    • McCool, K.W.1    Miyamoto, S.2
  • 46
    • 34548430918 scopus 로고    scopus 로고
    • Intrinsic mitochondrial dysfunction in ATM-deficient lymphoblastoid cells
    • Ambrose M, Goldstine JV, Gatti RA. Intrinsic mitochondrial dysfunction in ATM-deficient lymphoblastoid cells. Hum Mol Genet 2007; 16: 2154-2164.
    • (2007) Hum Mol Genet , vol.16 , pp. 2154-2164
    • Ambrose, M.1    Goldstine, J.V.2    Gatti, R.A.3
  • 47
    • 79959785857 scopus 로고    scopus 로고
    • Cutaneous squamous cell carcinoma (SCC) and the DNA damage response: PATM expression patterns in premalignant and malignant keratinocyte skin lesions
    • Ismail F, Ikram M, Purdie K, Harwood C, Leigh I, Storey A. Cutaneous squamous cell carcinoma (SCC) and the DNA damage response: pATM expression patterns in premalignant and malignant keratinocyte skin lesions. PLoS One 2011; 6: e21271.
    • (2011) PLoS One , vol.6 , pp. e21271
    • Ismail, F.1    Ikram, M.2    Purdie, K.3    Harwood, C.4    Leigh, I.5    Storey, A.6
  • 50
    • 33744805133 scopus 로고    scopus 로고
    • CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM
    • Zhang L, Tie Y, Tian C, Xing G, Song Y, Zhu Y et al. CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM. Cell Signal 2006; 18: 1386-1395.
    • (2006) Cell Signal , vol.18 , pp. 1386-1395
    • Zhang, L.1    Tie, Y.2    Tian, C.3    Xing, G.4    Song, Y.5    Zhu, Y.6
  • 51
    • 84870885534 scopus 로고    scopus 로고
    • EGFR-induced and PKCepsilon monoubiquitylation-dependent NF-kappaB activation upregulates PKM2 expression and promotes tumorigenesis
    • Yang W, Xia Y, Cao Y, Zheng Y, Bu W, Zhang L et al. EGFR-induced and PKCepsilon monoubiquitylation-dependent NF-kappaB activation upregulates PKM2 expression and promotes tumorigenesis. Mol Cell 2012; 48: 771-784.
    • (2012) Mol Cell , vol.48 , pp. 771-784
    • Yang, W.1    Xia, Y.2    Cao, Y.3    Zheng, Y.4    Bu, W.5    Zhang, L.6
  • 52
    • 84961290180 scopus 로고    scopus 로고
    • Tyrosine 370 phosphorylation of ATM positively regulates DNA damage response
    • Lee HJ, Lan L, Peng G, Chang WC, Hsu MC, Wang YN et al. Tyrosine 370 phosphorylation of ATM positively regulates DNA damage response. Cell Res 2015; 25: 225-236.
    • (2015) Cell Res , vol.25 , pp. 225-236
    • Lee, H.J.1    Lan, L.2    Peng, G.3    Chang, W.C.4    Hsu, M.C.5    Wang, Y.N.6
  • 53
    • 84862324402 scopus 로고    scopus 로고
    • Moonlighting is mainstream: Paradigm adjustment required
    • Copley SD. Moonlighting is mainstream: paradigm adjustment required. BioEssays 2012; 34: 578-588.
    • (2012) BioEssays , vol.34 , pp. 578-588
    • Copley, S.D.1
  • 54
    • 23144441321 scopus 로고    scopus 로고
    • Systematic analysis of genes required for synapse structure and function
    • Sieburth D, Ch'ng Q, Dybbs M, Tavazoie M, Kennedy S, cWang D et al. Systematic analysis of genes required for synapse structure and function. Nature 2005; 436: 510-517.
    • (2005) Nature , vol.436 , pp. 510-517
    • Sieburth, D.1    Ch'Ng, Q.2    Dybbs, M.3    Tavazoie, M.4    Kennedy, S.5    Wang, D.6
  • 55
    • 84881098989 scopus 로고    scopus 로고
    • Feature Article: MTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology
    • Betz C, Stracka D, Prescianotto-Baschong C, Frieden M, Demaurex N, Hall MN. Feature Article: mTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology. Proc Natl Acad Sci USA 2013; 110: 12526-12534.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 12526-12534
    • Betz, C.1    Stracka, D.2    Prescianotto-Baschong, C.3    Frieden, M.4    Demaurex, N.5    Hall, M.N.6
  • 56
    • 77958041295 scopus 로고    scopus 로고
    • Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action
    • Dikeakos JD, Atkins KM, Thomas L, Emert-Sedlak L, Byeon IJ, Jung J et al. Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action. Mol Biol Cell 2010; 21: 3279-3292.
    • (2010) Mol Biol Cell , vol.21 , pp. 3279-3292
    • Dikeakos, J.D.1    Atkins, K.M.2    Thomas, L.3    Emert-Sedlak, L.4    Byeon, I.J.5    Jung, J.6
  • 57
    • 65849472289 scopus 로고    scopus 로고
    • At the crossroads of homoeostasis and disease: Roles of the PACS proteins in membrane traffic and apoptosis
    • Youker RT, Shinde U, Day R, Thomas G. At the crossroads of homoeostasis and disease: roles of the PACS proteins in membrane traffic and apoptosis. Biochem J 2009; 421: 1-15.
    • (2009) Biochem J , vol.421 , pp. 1-15
    • Youker, R.T.1    Shinde, U.2    Day, R.3    Thomas, G.4
  • 58
    • 70349445170 scopus 로고    scopus 로고
    • P53 ancestry: Gazing through an evolutionary lens
    • Lu WJ, Amatruda JF, Abrams JM. p53 ancestry: gazing through an evolutionary lens. Nature Rev Cancer 2009; 9: 758-762.
    • (2009) Nature Rev Cancer , vol.9 , pp. 758-762
    • Lu, W.J.1    Amatruda, J.F.2    Abrams, J.M.3
  • 59
    • 0142227023 scopus 로고    scopus 로고
    • No PUMA no death: Implications for p53-dependent apoptosis
    • Yu J, Zhang L. No PUMA, no death: implications for p53-dependent apoptosis. Cancer Cell 2003; 4: 248-249.
    • (2003) Cancer Cell , vol.4 , pp. 248-249
    • Yu, J.1    Zhang, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.