메뉴 건너뛰기




Volumn 17, Issue 4, 2015, Pages 434-444

Ppm1b negatively regulates necroptosis through dephosphorylating Rip3

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEINS AND BINDING PROTEINS; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MIXED LINEAGE KINASE DOMAIN LIKE PROTEIN; PHOSPHATASE; PROTEIN PHOSPHATASE 1B; RECEPTOR INTERACTING PROTEIN 3; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; MLKL PROTEIN, MOUSE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE; PROTEIN PHOSPHATASE 2C; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK3 PROTEIN, MOUSE; SMALL INTERFERING RNA;

EID: 84925944209     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb3120     Document Type: Article
Times cited : (122)

References (52)
  • 2
    • 83155192804 scopus 로고    scopus 로고
    • TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex i and II members
    • Vanlangenakker, N., Bertrand, M. J., Bogaert, P., Vandenabeele, P. & Vanden Berghe, T. TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members. Cell Death Dis. 2, e230 (2011).
    • (2011) Cell Death Dis. , vol.2 , pp. e230
    • Vanlangenakker, N.1    Bertrand, M.J.2    Bogaert, P.3    Vandenabeele, P.4    Vanden Berghe, T.5
  • 3
    • 84886656964 scopus 로고    scopus 로고
    • Toll-like receptor 3-mediated necrosis via TRIF RIP3, and MLKL
    • Kaiser, W. et al. Toll-like receptor 3-mediated necrosis via TRIF, RIP3, and MLKL. J. Biol. Chem. 288, 31268-31279 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 31268-31279
    • Kaiser, W.1
  • 5
    • 84874263775 scopus 로고    scopus 로고
    • Necroptosis: The release of damage-Associated molecular patterns and its physiological relevance
    • Kaczmarek, A., Vandenabeele, P. & Krysko, D. V. Necroptosis: the release of damage-Associated molecular patterns and its physiological relevance. Immunity 38, 209-223 (2013).
    • (2013) Immunity , vol.38 , pp. 209-223
    • Kaczmarek, A.1    Vandenabeele, P.2    Krysko, D.V.3
  • 7
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler, N. et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1, 489-495 (2000).
    • (2000) Nat. Immunol. , vol.1 , pp. 489-495
    • Holler, N.1
  • 8
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang, D. W. et al. RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 325, 332-336 (2009).
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1
  • 9
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF
    • He, S. et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-. Cell 137, 1100-1111 (2009).
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1
  • 10
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho, Y. S. et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137, 1112-1123 (2009).
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1
  • 11
    • 84864240409 scopus 로고    scopus 로고
    • The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis
    • Li, J. et al. The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150, 339-350 (2012).
    • (2012) Cell , vol.150 , pp. 339-350
    • Li, J.1
  • 12
    • 84859467770 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
    • Zhao, J. et al. Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis. Proc. Natl Acad. Sci. USA 109, 5322-5327 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 5322-5327
    • Zhao, J.1
  • 13
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • Sun, L. et al. Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 148, 213-227 (2012).
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1
  • 14
    • 84884308522 scopus 로고    scopus 로고
    • The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism
    • Murphy, J. M. et al. The pseudokinase MLKL mediates necroptosis via a molecular switch mechanism. Immunity 39, 443-453 (2013).
    • (2013) Immunity , vol.39 , pp. 443-453
    • Murphy, J.M.1
  • 15
    • 84898027331 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3
    • Wang, H. et al. Mixed lineage kinase domain-like protein MLKL causes necrotic membrane disruption upon phosphorylation by RIP3. Mol. Cell 54, 133-146 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 133-146
    • Wang, H.1
  • 16
    • 84901280344 scopus 로고    scopus 로고
    • MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates
    • Dondelinger, Y. et al. MLKL compromises plasma membrane integrity by binding to phosphatidylinositol phosphates. Cell Rep. 7, 971-981 (2014).
    • (2014) Cell Rep. , vol.7 , pp. 971-981
    • Dondelinger, Y.1
  • 17
    • 84891739370 scopus 로고    scopus 로고
    • Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death
    • Chen, X. et al. Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death. Cell Res. 24, 105-121 (2014).
    • (2014) Cell Res. , vol.24 , pp. 105-121
    • Chen, X.1
  • 18
    • 84891343566 scopus 로고    scopus 로고
    • Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
    • Cai, Z. et al. Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat. Cell Biol. 16, 55-65 (2014).
    • (2014) Nat. Cell Biol. , vol.16 , pp. 55-65
    • Cai, Z.1
  • 19
    • 84878755914 scopus 로고    scopus 로고
    • Diverse sequence determinants control human and mouse receptor interacting protein 3 (RIP3) and mixed lineage kinase domain-like (MLKL) interaction in necroptotic signaling
    • Chen, W. et al. Diverse sequence determinants control human and mouse receptor interacting protein 3 (RIP3) and mixed lineage kinase domain-like (MLKL) interaction in necroptotic signaling. J. Biol. Chem. 288, 16247-16261 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 16247-16261
    • Chen, W.1
  • 20
    • 76249090489 scopus 로고    scopus 로고
    • BioGPS: An extensible and customizable portal for querying and organizing gene annotation resources
    • Wu, C. et al. BioGPS: an extensible and customizable portal for querying and organizing gene annotation resources. Genome Biol. 10, R130 (2009).
    • (2009) Genome Biol. , vol.10 , pp. R130
    • Wu, C.1
  • 21
    • 44249093277 scopus 로고    scopus 로고
    • Expression analysis of G protein-coupled receptors in mouse macrophages
    • Lattin, J. E. et al. Expression analysis of G protein-coupled receptors in mouse macrophages. Immunome Res. 4, 5 (2008).
    • (2008) Immunome Res. , vol.4 , pp. 5
    • Lattin, J.E.1
  • 22
    • 0027131224 scopus 로고
    • Molecular cloning of a novel isotype of Mg(2C)-dependent protein phosphatase-(type 2C-) enriched in brain and heart
    • Terasawa, T. et al. Molecular cloning of a novel isotype of Mg(2C)-dependent protein phosphatase-(type 2C-) enriched in brain and heart. Arch. Biochem. Biophys. 307, 342-349 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 342-349
    • Terasawa, T.1
  • 23
    • 0032524537 scopus 로고    scopus 로고
    • Mutational analysis of the domain structure of mouse protein phosphatase 2C
    • Kusuda, K. et al. Mutational analysis of the domain structure of mouse protein phosphatase 2C-. Biochem. J. 332, 243-250 (1998).
    • (1998) Biochem. J. , vol.332 , pp. 243-250
    • Kusuda, K.1
  • 24
    • 84899692435 scopus 로고    scopus 로고
    • Regulator of G-protein signaling 19 (RGS19) and its partner G-inhibiting activity polypeptide 3 (GNAI3) are required for zVAD-induced autophagy and cell death in L929 cells
    • Wu, T. et al. Regulator of G-protein signaling 19 (RGS19) and its partner G-inhibiting activity polypeptide 3 (GNAI3) are required for zVAD-induced autophagy and cell death in L929 cells. PLoS ONE 9, e94634 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e94634
    • Wu, T.1
  • 25
    • 42249102086 scopus 로고    scopus 로고
    • Identification of RIP1 kinase as a specific cellular target of necrostatins
    • Degterev, A. et al. Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat. Chem. Biol. 4, 313-321 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 313-321
    • Degterev, A.1
  • 26
    • 0037088632 scopus 로고    scopus 로고
    • Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3
    • Sun, X., Yin, J., Starovasnik, M. A., Fairbrother, W. J. & Dixit, V. M. Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3. J. Biol. Chem. 277, 9505-9511 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 9505-9511
    • Sun, X.1    Yin, J.2    Starovasnik, M.A.3    Fairbrother, W.J.4    Dixit, V.M.5
  • 27
    • 0029055145 scopus 로고
    • Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycinassociated protein and characterization of a critical serine residue
    • Chen, J., Zheng, X. F., Brown, E. J. & Schreiber, S. L. Identification of an 11-kDa FKBP12-rapamycin-binding domain within the 289-kDa FKBP12-rapamycinassociated protein and characterization of a critical serine residue. Proc. Natl Acad. Sci. USA 92, 4947-4951 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4947-4951
    • Chen, J.1    Zheng, X.F.2    Brown, E.J.3    Schreiber, S.L.4
  • 28
    • 84881184694 scopus 로고    scopus 로고
    • Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis
    • Wu, J. et al. Mlkl knockout mice demonstrate the indispensable role of Mlkl in necroptosis. Cell Res. 23, 994-1006 (2013).
    • (2013) Cell Res. , vol.23 , pp. 994-1006
    • Wu, J.1
  • 29
    • 78650175369 scopus 로고    scopus 로고
    • ZVAD-induced necroptosis in L929 cells depends on autocrine production of TNF-mediated by the PKC-MAPKs-AP-1 pathway
    • Wu, Y. T. et al. zVAD-induced necroptosis in L929 cells depends on autocrine production of TNF-mediated by the PKC-MAPKs-AP-1 pathway. Cell Death Differ. 18, 26-37 (2011).
    • (2011) Cell Death Differ. , vol.18 , pp. 26-37
    • Wu, Y.T.1
  • 30
    • 84873729095 scopus 로고    scopus 로고
    • Multiplex genome engineering using CRISPR/Cas systems
    • Cong, L. et al. Multiplex genome engineering using CRISPR/Cas systems. Science 339, 819-823 (2013).
    • (2013) Science , vol.339 , pp. 819-823
    • Cong, L.1
  • 31
    • 34248671648 scopus 로고    scopus 로고
    • Disruption of the mouse protein Ser/Thr phosphatase 2C-gene leads to early pre-implantation lethality
    • Sasaki, M. et al. Disruption of the mouse protein Ser/Thr phosphatase 2C-gene leads to early pre-implantation lethality. Mech. Dev. 124, 489-499 (2007).
    • (2007) Mech. Dev. , vol.124 , pp. 489-499
    • Sasaki, M.1
  • 32
    • 84897088275 scopus 로고    scopus 로고
    • Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis
    • Newton, K. et al. Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis. Science 343, 1357-1360 (2014).
    • (2014) Science , vol.343 , pp. 1357-1360
    • Newton, K.1
  • 33
    • 43049152912 scopus 로고    scopus 로고
    • TNF-induces two distinct caspase-8 activation pathways
    • Wang, L., Du, F. & Wang, X. TNF-induces two distinct caspase-8 activation pathways. Cell 133, 693-703 (2008).
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 34
    • 44949240664 scopus 로고    scopus 로고
    • CIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand, M. J. et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol. Cell 30, 689-700 (2008).
    • (2008) Mol. Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.1
  • 35
    • 56949087707 scopus 로고    scopus 로고
    • PPM1A and PPM1B act as IKK-phosphatases to terminate TNF-induced IKK-NF-B activation
    • Sun, W. et al. PPM1A and PPM1B act as IKK-phosphatases to terminate TNF-induced IKK-NF-B activation. Cell Signal. 21, 95-102 (2009).
    • (2009) Cell Signal. , vol.21 , pp. 95-102
    • Sun, W.1
  • 36
    • 11844305963 scopus 로고    scopus 로고
    • Attenuation of murine collagen-induced arthritis by a novel, potent, selective small molecule inhibitor of I-B Kinase 2, TPCA-1 (2-[(aminocarbonyl)amino]-5-(4-fluorophenyl)-3-Thiophenecarboxamide), occurs via reduction of proinflammatory cytokines and antigen-induced T cell Proliferation
    • Podolin, P. L. et al. Attenuation of murine collagen-induced arthritis by a novel, potent, selective small molecule inhibitor of I-B Kinase 2, TPCA-1 (2-[(aminocarbonyl)amino]-5-(4-fluorophenyl)-3-Thiophenecarboxamide), occurs via reduction of proinflammatory cytokines and antigen-induced T cell Proliferation. J. Pharmacol. Exp. Ther. 312, 373-381 (2005).
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 373-381
    • Podolin, P.L.1
  • 37
    • 15244341289 scopus 로고    scopus 로고
    • A novel NF-B inhibitor, IMD-0354, suppresses neoplastic proliferation of human mast cells with constitutively activated c-kit receptors
    • Tanaka, A. et al. A novel NF-B inhibitor, IMD-0354, suppresses neoplastic proliferation of human mast cells with constitutively activated c-kit receptors. Blood 105, 2324-2331 (2005).
    • (2005) Blood , vol.105 , pp. 2324-2331
    • Tanaka, A.1
  • 38
    • 0035937111 scopus 로고    scopus 로고
    • Regulation of the TAK1 signaling pathway by protein phosphatase 2C
    • Hanada, M. et al. Regulation of the TAK1 signaling pathway by protein phosphatase 2C. J. Biol. Chem. 276, 5753-5759 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 5753-5759
    • Hanada, M.1
  • 39
    • 0037903145 scopus 로고    scopus 로고
    • A resorcylic acid lactone, 5Z-7-oxozeaenol, prevents inflammation by inhibiting the catalytic activity of TAK1 MAPK kinase kinase
    • Ninomiya-Tsuji, J. et al. A resorcylic acid lactone, 5Z-7-oxozeaenol, prevents inflammation by inhibiting the catalytic activity of TAK1 MAPK kinase kinase. J. Biol. Chem. 278, 18485-18490 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 18485-18490
    • Ninomiya-Tsuji, J.1
  • 40
    • 84885868361 scopus 로고    scopus 로고
    • Structural insights into RIP3-mediated necroptotic signaling
    • Xie, T. et al. Structural insights into RIP3-mediated necroptotic signaling. Cell Rep. 5, 70-78 (2013).
    • (2013) Cell Rep. , vol.5 , pp. 70-78
    • Xie, T.1
  • 41
    • 84898035535 scopus 로고    scopus 로고
    • The G-Src signaling pathway regulates TNF-induced necroptosis via control of necrosome translocation
    • Li, L. et al. The G-Src signaling pathway regulates TNF-induced necroptosis via control of necrosome translocation. Cell Res. 24, 417-432 (2014).
    • (2014) Cell Res. , vol.24 , pp. 417-432
    • Li, L.1
  • 42
    • 33646950265 scopus 로고    scopus 로고
    • PPM1A functions as a Smad phosphatase to terminate TGF-signaling
    • Lin, X. et al. PPM1A functions as a Smad phosphatase to terminate TGF-signaling. Cell 125, 915-928 (2006).
    • (2006) Cell , vol.125 , pp. 915-928
    • Lin, X.1
  • 43
    • 84862175306 scopus 로고    scopus 로고
    • Dichotomy between RIP1-And RIP3-mediated necroptosis in tumor necrosis factor-induced shock
    • Linkermann, A. et al. Dichotomy between RIP1-And RIP3-mediated necroptosis in tumor necrosis factor-induced shock. Mol. Med. 18, 577-586 (2012).
    • (2012) Mol. Med. , vol.18 , pp. 577-586
    • Linkermann, A.1
  • 44
    • 84255162797 scopus 로고    scopus 로고
    • RIP kinase-dependent necrosis drives lethal systemic inflammatory response syndrome
    • Duprez, L. et al. RIP kinase-dependent necrosis drives lethal systemic inflammatory response syndrome. Immunity 35, 908-918 (2011).
    • (2011) Immunity , vol.35 , pp. 908-918
    • Duprez, L.1
  • 45
    • 0023028369 scopus 로고
    • Shock and tissue injury induced by recombinant human cachectin
    • Tracey, K. J. et al. Shock and tissue injury induced by recombinant human cachectin. Science 234, 470-474 (1986).
    • (1986) Science , vol.234 , pp. 470-474
    • Tracey, K.J.1
  • 46
    • 84879882622 scopus 로고    scopus 로고
    • PKA negatively regulates PP2C-To activate NF-B-mediated inflammatory signaling
    • Choi, H. K. et al. PKA negatively regulates PP2C-To activate NF-B-mediated inflammatory signaling. Biochem. Biophys. Res. Commun. 436, 473-477 (2013).
    • (2013) Biochem. Biophys. Res. Commun. , vol.436 , pp. 473-477
    • Choi, H.K.1
  • 47
    • 0032561396 scopus 로고    scopus 로고
    • Protein phosphatase type 2C active at physiological Mg2C: Stimulation by unsaturated fatty acids
    • Klumpp, S., Selke, D. & Hermesmeier, J. Protein phosphatase type 2C active at physiological Mg2C: stimulation by unsaturated fatty acids. FEBS Lett. 437, 229-232 (1998).
    • (1998) FEBS Lett. , vol.437 , pp. 229-232
    • Klumpp, S.1    Selke, D.2    Hermesmeier, J.3
  • 48
    • 33748150967 scopus 로고    scopus 로고
    • Wip1 phosphatase modulates ATM-dependent signaling pathways
    • Shreeram, S. et al. Wip1 phosphatase modulates ATM-dependent signaling pathways. Mol. Cell 23, 757-764 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 757-764
    • Shreeram, S.1
  • 49
    • 84873734105 scopus 로고    scopus 로고
    • RNA-guided human genome engineering via Cas9
    • Mali, P. et al. RNA-guided human genome engineering via Cas9. Science 339, 823-826 (2013).
    • (2013) Science , vol.339 , pp. 823-826
    • Mali, P.1
  • 51
    • 84870689198 scopus 로고    scopus 로고
    • Investigation of RIP3-dependent protein phosphorylation by quantitative phosphoproteomics
    • Wu, X. et al. Investigation of RIP3-dependent protein phosphorylation by quantitative phosphoproteomics. Mol. Cell Proteomics 11, 1640-1651 (2012).
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 1640-1651
    • Wu, X.1
  • 52
    • 19744368094 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium pathogenicity island 2 is necessary for complete virulence in a mouse model of infectious enterocolitis
    • Coburn, B., Li, Y., Owen, D., Vallance, B. A. & Finlay, B. B. Salmonella enterica serovar Typhimurium pathogenicity island 2 is necessary for complete virulence in a mouse model of infectious enterocolitis. Infect. Immun. 73, 3219-3227 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 3219-3227
    • Coburn, B.1    Li, Y.2    Owen, D.3    Vallance, B.A.4    Finlay, B.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.