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      Dual roles of FLIP in controlling caspase-8 and their implications on cell death and survival

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      https://www.riss.kr/link?id=A105377477

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      다국어 초록 (Multilingual Abstract)

      Cellular FLIP (cFLIP; cellular FLICE inhibitory protein) is a key regulator of caspase-8 activity, and its viral homolog (vFLIP)is found in various viruses. cFLIP inhibits the caspase-8 activation in death-inducing signaling complex (DISC) when itsexpression level is high as in cancer cells. In contrast, cFLIP can also activate the caspase-8 in its lower expression leveland in lymphocyte in particular which results in the activation of NF-κB transcription factor. Recent biochemical studies onDISC has proposed that DED proteins in DISC, that are FADD, procaspase-8 & cFLIP, utilize two hydrophobic faces of theirDEDs for establishing DED-DED network for DISC assembly. Regarding the NF-κB activation, the crystal structure of K13-vFLIP showed that two grooves in the N-terminal DED in FLIP are the sites where dimeric IKKγ binds. FLIP is associatedwith various cancers seemingly through the dual functions of inhibiting apoptosis and promoting proliferation, so it wouldan attractive anti-cancer therapeutic target at either mRNA or protein level.
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      Cellular FLIP (cFLIP; cellular FLICE inhibitory protein) is a key regulator of caspase-8 activity, and its viral homolog (vFLIP)is found in various viruses. cFLIP inhibits the caspase-8 activation in death-inducing signaling complex (DISC) when itsexp...

      Cellular FLIP (cFLIP; cellular FLICE inhibitory protein) is a key regulator of caspase-8 activity, and its viral homolog (vFLIP)is found in various viruses. cFLIP inhibits the caspase-8 activation in death-inducing signaling complex (DISC) when itsexpression level is high as in cancer cells. In contrast, cFLIP can also activate the caspase-8 in its lower expression leveland in lymphocyte in particular which results in the activation of NF-κB transcription factor. Recent biochemical studies onDISC has proposed that DED proteins in DISC, that are FADD, procaspase-8 & cFLIP, utilize two hydrophobic faces of theirDEDs for establishing DED-DED network for DISC assembly. Regarding the NF-κB activation, the crystal structure of K13-vFLIP showed that two grooves in the N-terminal DED in FLIP are the sites where dimeric IKKγ binds. FLIP is associatedwith various cancers seemingly through the dual functions of inhibiting apoptosis and promoting proliferation, so it wouldan attractive anti-cancer therapeutic target at either mRNA or protein level.

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      참고문헌 (Reference)

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      4 Carrington, P. E., "The structure of FADD and its mode of interaction with procaspase-8" 22 : 599-610, 2006

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      2 Chang, D. W., "c-FLIP(L)is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis" 21 : 3704-3714, 2002

      3 Thome, M., "Viral FLICE-inhibitory proteins(FLIPs)prevent apoptosis induced by death receptors" 386 : 517-521, 1997

      4 Carrington, P. E., "The structure of FADD and its mode of interaction with procaspase-8" 22 : 599-610, 2006

      5 Scaffidi, C., "The role of c-FLIP in modulation of CD95-induced apoptosis" 274 : 1541-1548, 1999

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      7 Kataoka, T., "The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways" 10 : 640-648, 2000

      8 Golks, A., "The c-FLIPNH2terminus(p22-FLIP)induces NF-kappaB activation" 203 : 1295-1305, 2006

      9 Hengartner, M. O., "The biochemistry of apoptosis" 407 : 770-776, 2000

      10 Wang, L., "The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations" 17 : 1324-1329, 2010

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      20 Kataoka, T., "N-terminal fragment of c-FLIP(L)processed by caspase 8 specifically interacts with TRAF2 and induces activation of the NF-kappaB signaling pathway" 24 : 2627-2636, 2004

      21 Fischer, U., "Many cuts to ruin : a comprehensive update of caspase substrates" 10 : 76-100, 2003

      22 Han, D. K., "MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death" 94 : 11333-11338, 1997

      23 Soulier, J., "Kaposi's sarcoma-associated herpesvirus-like DNA sequences in multicentric Castleman's disease" 86 : 1276-1280, 1995

      24 Cesarman, E., "Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas" 332 : 1186-1191, 1995

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      27 Boldin, M. P., "Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death" 85 : 803-815, 1996

      28 Irmler, M., "Inhibition of death receptor signals by cellular FLIP" 388 : 190-195, 1997

      29 Hu, S., "I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1-and CD-95-induced apoptosis" 272 : 17255-17257, 1997

      30 Muppidi, J. R., "Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis" 13 : 1641-1650, 2006

      31 Hanahan, D., "Hallmarks of cancer : the next generation" 144 : 646-674, 2011

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      33 양진국, "FLIP as an Anti-Cancer Therapeutic Target" 연세대학교의과대학 49 (49): 19-27, 2008

      34 Yu, J. W., "FLIP and the death effector domain family" 27 : 6216-6227, 2008

      35 Muzio, M., "FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95(Fas/APO-1)death--inducing signaling complex" 85 : 817-827, 1996

      36 Chinnaiyan, A. M., "FADD/MORT1 is a common mediator of CD95(Fas/APO-1)and tumor necrosis factor receptor-induced apoptosis" 271 : 4961-4965, 1996

      37 Chinnaiyan, A. M., "FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis" 81 : 505-512, 1995

      38 Majkut, J., "Differential affinity of FLIP and procaspase 8 for FADD's DED binding surfaces regulates DISC assembly" 5 : 3350-, 2014

      39 Debatin, K. M., "Death receptors in chemotherapy and cancer" 23 : 2950-2966, 2004

      40 Bertin, J., "Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas-and TNFR1-induced apoptosis" 94 : 1172-1176, 1997

      41 Yang, J. K., "Death effecter domain for the assembly of deathinducing signaling complex" 20 : 235-239, 2015

      42 Kischkel, F. C., "Cytotoxicity-dependent APO-1(Fas/CD95)-associated proteins form a death-inducing signaling complex(DISC)with the receptor" 14 : 5579-5588, 1995

      43 Bagneris, C., "Crystal structure of a vFlip-IKKgamma complex : insights into viral activation of the IKK signalosome" 30 : 620-631, 2008

      44 Yang, J. K., "Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition" 20 : 939-949, 2005

      45 Djerbi, M., "Characterization of the human FLICE-inhibitory protein locus and comparison of the anti-apoptotic activity of four different flip isoforms" 54 : 180-189, 2001

      46 Wyllie, A. H., "Cell death : the significance of apoptosis" 68 : 251-306, 1980

      47 Shu, H. B., "Casper is a FADD-and caspase-related inducer of apoptosis" 6 : 751-763, 1997

      48 Misra, R. S., "Caspase-8 and c-FLIPL associate in lipid rafts with NFkappaB adaptors during T cell activation" 282 : 19365-19374, 2007

      49 Shi, Y., "Caspase activation : revisiting the induced proximity model" 117 : 855-858, 2004

      50 Inohara, N., "CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis" 94 : 10717-10722, 1997

      51 Goltsev, Y. V., "CASH, a novel caspase homologue with death effector domains" 272 : 19641-19644, 1997

      52 Garvey, T. L., "Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function" 76 : 697-706, 2002

      53 Kroemer, G., "Autophagic cell death : the story of a misnomer" 9 : 1004-1010, 2008

      54 Mattson, M. P., "Apoptosis in neurodegenerative disorders" 1 : 120-129, 2000

      55 Kerr, J. F., "Apoptosis : a basic biological phenomenon with wide-ranging implications in tissue kinetics" 26 : 239-257, 1972

      56 Chaudhary, P. M., "Activation of the NF-kappaB pathway by caspase 8 and its homologs" 19 : 4451-4460, 2000

      57 Hu, W. H., "Activation of NF-kappaB by FADD, Casper, and caspase-8" 275 : 10838-10844, 2000

      58 Hu, S., "A novel family of viral death effector domain-containing molecules that inhibit both CD-95-and tumor necrosis factor receptor-1-induced apoptosis" 272 : 9621-9624, 1997

      59 Dickens, L. S., "A death effector domain chain DISC model reveals a crucial role for caspase-8chain assembly in mediating apoptotic cell death" 47 : 291-305, 2012

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