메뉴 건너뛰기




Volumn 22, Issue 7, 2015, Pages 1131-1143

The endogenous caspase-8 inhibitor c-FLIPL regulates ER morphology and crosstalk with mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CASPASE; CASPASE 8; CASPASE 8 INHIBITOR; FLICE INHIBITORY PROTEIN; ISOPROTEIN; CASP8 PROTEIN, MOUSE; CFLAR PROTEIN, MOUSE; MYELIN PROTEIN; PROTEIN NOGO; RTN4 PROTEIN, MOUSE;

EID: 84930756510     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2014.197     Document Type: Article
Times cited : (29)

References (47)
  • 2
    • 0033556310 scopus 로고    scopus 로고
    • The role of c-FLIP in modulation of CD95-induced apoptosis
    • Scaffidi C, Schmitz I, Krammer PH, Peter ME. The role of c-FLIP in modulation of CD95-induced apoptosis. J Biol Chem 1999; 274: 1541-1548.
    • (1999) J Biol Chem , vol.274 , pp. 1541-1548
    • Scaffidi, C.1    Schmitz, I.2    Krammer, P.H.3    Peter, M.E.4
  • 4
    • 0036499140 scopus 로고    scopus 로고
    • Adhesion-mediated intracellular redistribution of c-Fas-associated death domain-like IL-1-converting enzyme-like inhibitory protein-long confers resistance to CD95-induced apoptosis in hematopoietic cancer cell lines
    • Shain KH, Landowski TH, Dalton WS. Adhesion-mediated intracellular redistribution of c-Fas-associated death domain-like IL-1-converting enzyme-like inhibitory protein-long confers resistance to CD95-induced apoptosis in hematopoietic cancer cell lines. J Immunol 2002; 168: 2544-2553.
    • (2002) J Immunol , vol.168 , pp. 2544-2553
    • Shain, K.H.1    Landowski, T.H.2    Dalton, W.S.3
  • 5
    • 34547111577 scopus 로고    scopus 로고
    • Caspase-8 and c-FLIPL associate in lipid rafts with NF-kappaB adaptors during T cell activation
    • Misra RS, Russell JQ, Koenig A, Hinshaw-Makepeace JA, Wen R, Wang D et al. Caspase-8 and c-FLIPL associate in lipid rafts with NF-kappaB adaptors during T cell activation. J Biol Chem 2007; 282: 19365-19374.
    • (2007) J Biol Chem , vol.282 , pp. 19365-19374
    • Misra, R.S.1    Russell, J.Q.2    Koenig, A.3    Hinshaw-Makepeace, J.A.4    Wen, R.5    Wang, D.6
  • 6
    • 0030705234 scopus 로고    scopus 로고
    • p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum
    • Ng FW, Nguyen M, Kwan T, Branton PE, Nicholson DW, Cromlish JA et al. p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum. J Cell Biol 1997; 139: 327-338.
    • (1997) J Cell Biol , vol.139 , pp. 327-338
    • Ng, F.W.1    Nguyen, M.2    Kwan, T.3    Branton, P.E.4    Nicholson, D.W.5    Cromlish, J.A.6
  • 7
    • 0037007141 scopus 로고    scopus 로고
    • The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum
    • Breckenridge DG, Nguyen M, Kuppig S, Reth M, Shore GC. The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum. Proc Natl Acad Sci USA. 2002; 99: 4331-4336.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4331-4336
    • Breckenridge, D.G.1    Nguyen, M.2    Kuppig, S.3    Reth, M.4    Shore, G.C.5
  • 8
    • 33750605285 scopus 로고    scopus 로고
    • Adaptor FADD is recruited by RTN3/HAP in ER-bound signaling complexes
    • Xiang R, Liu Y, Zhu L, Dong W, Qi Y. Adaptor FADD is recruited by RTN3/HAP in ER-bound signaling complexes. Apoptosis 2006; 11: 1923-1932.
    • (2006) Apoptosis , vol.11 , pp. 1923-1932
    • Xiang, R.1    Liu, Y.2    Zhu, L.3    Dong, W.4    Qi, Y.5
  • 11
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge DG, Stojanovic M, Marcellus RC, Shore GC. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J Cell Biol 2003; 160: 1115-1127.
    • (2003) J Cell Biol , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 12
    • 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
  • 13
    • 3242675057 scopus 로고    scopus 로고
    • Association of active caspase 8 with the mitochondrial membrane during apoptosis: Potential roles in cleaving BAP31 and caspase 3 and mediating mitochondrion-endoplasmic reticulum cross talk in etoposide-induced cell death
    • Chandra D, Choy G, Deng X, Bhatia B, Daniel P, Tang DG. Association of active caspase 8 with the mitochondrial membrane during apoptosis: potential roles in cleaving BAP31 and caspase 3 and mediating mitochondrion-endoplasmic reticulum cross talk in etoposide-induced cell death. Mol Cell Biol 2004; 24: 6592-6607.
    • (2004) Mol Cell Biol , vol.24 , pp. 6592-6607
    • Chandra, D.1    Choy, G.2    Deng, X.3    Bhatia, B.4    Daniel, P.5    Tang, D.G.6
  • 14
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance JE. Phospholipid synthesis in a membrane fraction associated with mitochondria. J Biol Chem 1990; 265: 7248-7256.
    • (1990) J Biol Chem , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 15
    • 77955824765 scopus 로고    scopus 로고
    • An intimate liaison: Spatial organization of the endoplasmic reticulum-mitochondria relationship
    • de Brito OM, Scorrano L. An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship. EMBO J 2010; 29: 2715-2723.
    • (2010) EMBO J , vol.29 , pp. 2715-2723
    • De Brito, O.M.1    Scorrano, L.2
  • 17
    • 0032511112 scopus 로고    scopus 로고
    • Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses
    • Rizzuto R, Pinton P, Carrington W, Fay FS, Fogarty KE, Lifshitz LM et al. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science 1998; 280: 1763-1766.
    • (1998) Science , vol.280 , pp. 1763-1766
    • Rizzuto, R.1    Pinton, P.2    Carrington, W.3    Fay, F.S.4    Fogarty, K.E.5    Lifshitz, L.M.6
  • 18
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito OM, Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008; 456: 605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 19
    • 81355137930 scopus 로고    scopus 로고
    • The ER in 3D: A multifunctional dynamic membrane network
    • Friedman JR, Voeltz GK. The ER in 3D: a multifunctional dynamic membrane network. Trends Cell Biol 2011; 21: 709-717.
    • (2011) Trends Cell Biol , vol.21 , pp. 709-717
    • Friedman, J.R.1    Voeltz, G.K.2
  • 20
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 2006; 124: 573-586.
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 21
    • 49649084487 scopus 로고    scopus 로고
    • The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum
    • Shibata Y, Voss C, Rist JM, Hu J, Rapoport TA, Prinz WA et al. The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J Biol Chem 2008; 283: 18892-18904.
    • (2008) J Biol Chem , vol.283 , pp. 18892-18904
    • Shibata, Y.1    Voss, C.2    Rist, J.M.3    Hu, J.4    Rapoport, T.A.5    Prinz, W.A.6
  • 22
    • 68049096310 scopus 로고    scopus 로고
    • A class of dynamin-like GTPases involved in the generation of the tubular ER network
    • Hu J, Shibata Y, Zhu PP, Voss C, Rismanchi N, Prinz WA et al. A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell 2009; 138: 549-561.
    • (2009) Cell , vol.138 , pp. 549-561
    • Hu, J.1    Shibata, Y.2    Zhu, P.P.3    Voss, C.4    Rismanchi, N.5    Prinz, W.A.6
  • 24
    • 34447519108 scopus 로고    scopus 로고
    • Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes
    • Nikonov AV, Hauri HP, Lauring B, Kreibich G. Climp-63-mediated binding of microtubules to the ER affects the lateral mobility of translocon complexes. J Cell Sci 2007; 120: 2248-2258.
    • (2007) J Cell Sci , vol.120 , pp. 2248-2258
    • Nikonov, A.V.1    Hauri, H.P.2    Lauring, B.3    Kreibich, G.4
  • 25
  • 26
    • 72449140675 scopus 로고    scopus 로고
    • Modulation of Wnt signaling by the nuclear localization of cellular FLIP-L
    • Katayama R, Ishioka T, Takada S, Takada R, Fujita N, Tsuruo T et al. Modulation of Wnt signaling by the nuclear localization of cellular FLIP-L. J Cell Sci 2010; 123: 23-28.
    • (2010) J Cell Sci , vol.123 , pp. 23-28
    • Katayama, R.1    Ishioka, T.2    Takada, S.3    Takada, R.4    Fujita, N.5    Tsuruo, T.6
  • 28
  • 29
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • Yeh WC, Itie A, Elia AJ, Ng M, Shu HB, Wakeham A et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development. Immunity 2000; 12: 633-642.
    • (2000) Immunity , vol.12 , pp. 633-642
    • Yeh, W.C.1    Itie, A.2    Elia, A.J.3    Ng, M.4    Shu, H.B.5    Wakeham, A.6
  • 30
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueousphase lumen of endoplasmic reticulum
    • Dayel MJ, Hom EF, Verkman AS. Diffusion of green fluorescent protein in the aqueousphase lumen of endoplasmic reticulum. Biophys J 1999; 76: 2843-2851.
    • (1999) Biophys J , vol.76 , pp. 2843-2851
    • Dayel, M.J.1    Hom, E.F.2    Verkman, A.S.3
  • 31
    • 0027418205 scopus 로고
    • Measurement of co-localisation of objects in dual-colour confocal images
    • Manders EM, Verbeek FJ, Aten JA. Measurement of co-localisation of objects in dual-colour confocal images. J Microscopy 1993; 169: 375-382.
    • (1993) J Microscopy , vol.169 , pp. 375-382
    • Manders, E.M.1    Verbeek, F.J.2    Aten, J.A.3
  • 32
    • 69249205412 scopus 로고    scopus 로고
    • Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin
    • Orso G, Pendin D, Liu S, Tosetto J, Moss TJ, Faust JE et al. Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature 2009; 460: 978-983.
    • (2009) Nature , vol.460 , pp. 978-983
    • Orso, G.1    Pendin, D.2    Liu, S.3    Tosetto, J.4    Moss, T.J.5    Faust, J.E.6
  • 33
    • 38049064947 scopus 로고    scopus 로고
    • Phosphorylation-regulated cleavage of the reticulon protein Nogo-B by caspase-7 at a noncanonical recognition site
    • Schweigreiter R, Stasyk T, Contarini I, Frauscher S, Oertle T, Klimaschewski L et al. Phosphorylation-regulated cleavage of the reticulon protein Nogo-B by caspase-7 at a noncanonical recognition site. Proteomics 2007; 7: 4457-4467.
    • (2007) Proteomics , vol.7 , pp. 4457-4467
    • Schweigreiter, R.1    Stasyk, T.2    Contarini, I.3    Frauscher, S.4    Oertle, T.5    Klimaschewski, L.6
  • 34
    • 56549112480 scopus 로고    scopus 로고
    • c-FLIP knockdown induces ligand-independent DR5-, FADD-, caspase-8-, and caspase-9-dependent apoptosis in breast cancer cells
    • Day TW, Huang S, Safa AR. c-FLIP knockdown induces ligand-independent DR5-, FADD-, caspase-8-, and caspase-9-dependent apoptosis in breast cancer cells. Biochem Pharmacol 2008; 76: 1694-1704.
    • (2008) Biochem Pharmacol , vol.76 , pp. 1694-1704
    • Day, T.W.1    Huang, S.2    Safa, A.R.3
  • 35
    • 84888237474 scopus 로고    scopus 로고
    • Cellular FLICE-like inhibitory protein secures intestinal epithelial cell survival and immune homeostasis by regulating caspase-8
    • Wittkopf N, Gunther C, Martini E, He G, Amann K, He YW et al. Cellular FLICE-like inhibitory protein secures intestinal epithelial cell survival and immune homeostasis by regulating caspase-8. Gastroenterology 2013; 145: 1369-1379.
    • (2013) Gastroenterology , vol.145 , pp. 1369-1379
    • Wittkopf, N.1    Gunther, C.2    Martini, E.3    He, G.4    Amann, K.5    He, Y.W.6
  • 36
    • 0027340729 scopus 로고
    • 2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria
    • 2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science 1993; 262: 744-747.
    • (1993) Science , vol.262 , pp. 744-747
    • Rizzuto, R.1    Brini, M.2    Murgia, M.3    Pozzan, T.4
  • 37
    • 78049342172 scopus 로고    scopus 로고
    • Trichoplein/mitostatin regulates endoplasmic reticulum-mitochondria juxtaposition
    • 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: 854-860.
    • (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
  • 40
    • 84897447156 scopus 로고    scopus 로고
    • Reticluon 4 is necessary for ER tubulation, STIM1-Orai1 coupling and store-operated calcium entry
    • Jozsef L, Tashiro K, Kuo A, Park E, Skoura A, Albinsson S et al. Reticluon 4 is necessary for ER tubulation, STIM1-Orai1 coupling and store-operated calcium entry. J Biol Chem 2014; 289: 9380-9395.
    • (2014) J Biol Chem , vol.289 , pp. 9380-9395
    • Jozsef, L.1    Tashiro, K.2    Kuo, A.3    Park, E.4    Skoura, A.5    Albinsson, S.6
  • 41
    • 73149088816 scopus 로고    scopus 로고
    • Functional and structural alterations in the endoplasmic reticulum and mitochondria during apoptosis triggered by C2-ceramide and CD95/APO-1/FAS receptor stimulation
    • Ferrari D, Pinton P, Campanella M, Callegari MG, Pizzirani C, Rimessi A et al. Functional and structural alterations in the endoplasmic reticulum and mitochondria during apoptosis triggered by C2-ceramide and CD95/APO-1/FAS receptor stimulation. Biochem Biophys Res Commun 2010; 391: 575-581.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 575-581
    • Ferrari, D.1    Pinton, P.2    Campanella, M.3    Callegari, M.G.4    Pizzirani, C.5    Rimessi, A.6
  • 42
    • 34249876378 scopus 로고    scopus 로고
    • The N- and C-termini of the human Nogo molecules are intrinsically unstructured: Bioinformatics, CD, NMR characterization, and functional implications
    • Li M, Song J. The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. Proteins 2007; 68: 100-108.
    • (2007) Proteins , vol.68 , pp. 100-108
    • Li, M.1    Song, J.2
  • 43
    • 77953177103 scopus 로고    scopus 로고
    • Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties
    • Sparkes I, Tolley N, Aller I, Svozil J, Osterrieder A, Botchway S et al. Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties. Plant Cell 2010; 22: 1333-1343.
    • (2010) Plant Cell , vol.22 , pp. 1333-1343
    • Sparkes, I.1    Tolley, N.2    Aller, I.3    Svozil, J.4    Osterrieder, A.5    Botchway, S.6
  • 44
    • 77951172861 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network
    • Park SH, Zhu PP, Parker RL, Blackstone C. Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network. J Clin Invest 2010; 120: 1097-1110.
    • (2010) J Clin Invest , vol.120 , pp. 1097-1110
    • Park, S.H.1    Zhu, P.P.2    Parker, R.L.3    Blackstone, C.4
  • 45
    • 34347236921 scopus 로고    scopus 로고
    • Organelle isolation: Functional mitochondria from mouse liver, muscle and cultured fibroblasts
    • Frezza C, Cipolat S, Scorrano L. Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts. Nat Protoc 2007; 2: 287-295.
    • (2007) Nat Protoc , vol.2 , pp. 287-295
    • Frezza, C.1    Cipolat, S.2    Scorrano, L.3
  • 46
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J Biol Chem 1985; 260: 3440-3450.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 47
    • 84868088934 scopus 로고    scopus 로고
    • Autophagy modulators sensitize prostate epithelial cancer cell lines to TNF-alpha-dependent apoptosis
    • Giampietri C, Petrungaro S, Padula F, D'Alessio A, Marini ES, Facchiano A et al. Autophagy modulators sensitize prostate epithelial cancer cell lines to TNF-alpha-dependent apoptosis. Apoptosis 2012; 17: 1210-1222.
    • (2012) Apoptosis , vol.17 , pp. 1210-1222
    • Giampietri, C.1    Petrungaro, S.2    Padula, F.3    D'Alessio, A.4    Marini, E.S.5    Facchiano, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.