메뉴 건너뛰기




Volumn 66, Issue 5, 2017, Pages 698-710.e5

MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death

Author keywords

caspase 8; cell death; complex II; cytokine; IAPs; MK2; necroptosis; p38; RIPK1; TNF

Indexed keywords

CASPASE 8; FAS ASSOCIATED DEATH DOMAIN PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 14; MK2 PROTEIN; PHOSPHOTRANSFERASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RIPK1 PROTEIN; SUCCINATE DEHYDROGENASE (UBIQUINONE); TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; CASP8 PROTEIN, MOUSE; FADD PROTEIN, MOUSE; MAP KINASE KINASE KINASE 7; MAP-KINASE-ACTIVATED KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; MULTIPROTEIN COMPLEX; PROTEIN SERINE THREONINE KINASE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK1 PROTEIN, HUMAN; RIPK1 PROTEIN, MOUSE; SIGNAL PEPTIDE;

EID: 85019106871     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2017.05.003     Document Type: Article
Times cited : (247)

References (55)
  • 1
    • 67349162130 scopus 로고    scopus 로고
    • Tumour necrosis factor and cancer
    • Balkwill, F., Tumour necrosis factor and cancer. Nat. Rev. Cancer 9 (2009), 361–371.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 361-371
    • Balkwill, F.1
  • 2
    • 84901678314 scopus 로고    scopus 로고
    • Cutting edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice
    • Berger, S.B., Kasparcova, V., Hoffman, S., Swift, B., Dare, L., Schaeffer, M., Capriotti, C., Cook, M., Finger, J., Hughes-Earle, A., et al. Cutting edge: RIP1 kinase activity is dispensable for normal development but is a key regulator of inflammation in SHARPIN-deficient mice. J. Immunol. 192 (2014), 5476–5480.
    • (2014) J. Immunol. , vol.192 , pp. 5476-5480
    • Berger, S.B.1    Kasparcova, V.2    Hoffman, S.3    Swift, B.4    Dare, L.5    Schaeffer, M.6    Capriotti, C.7    Cook, M.8    Finger, J.9    Hughes-Earle, A.10
  • 4
    • 79952435349 scopus 로고    scopus 로고
    • Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
    • Cargnello, M., Roux, P.P., Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases. Microbiol. Mol. Biol. Rev. 75 (2011), 50–83.
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 50-83
    • Cargnello, M.1    Roux, P.P.2
  • 11
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • Feng, S., Yang, Y., Mei, Y., Ma, L., Zhu, D.E., Hoti, N., Castanares, M., Wu, M., Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell. Signal. 19 (2007), 2056–2067.
    • (2007) Cell. Signal. , vol.19 , pp. 2056-2067
    • Feng, S.1    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.E.5    Hoti, N.6    Castanares, M.7    Wu, M.8
  • 13
    • 85042783008 scopus 로고    scopus 로고
    • MAPK-activated protein kinases (MKs): novel insights and challenges
    • Gaestel, M., MAPK-activated protein kinases (MKs): novel insights and challenges. Front. Cell Dev. Biol., 3, 2016, 88.
    • (2016) Front. Cell Dev. Biol. , vol.3 , pp. 88
    • Gaestel, M.1
  • 14
    • 59649127763 scopus 로고    scopus 로고
    • Inhibition of p38: has the fat lady sung?
    • Genovese, M.C., Inhibition of p38: has the fat lady sung?. Arthritis Rheum. 60 (2009), 317–320.
    • (2009) Arthritis Rheum. , vol.60 , pp. 317-320
    • Genovese, M.C.1
  • 17
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • Haas, T.L., Emmerich, C.H., Gerlach, B., Schmukle, A.C., Cordier, S.M., Rieser, E., Feltham, R., Vince, J., Warnken, U., Wenger, T., et al. Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol. Cell 36 (2009), 831–844.
    • (2009) Mol. Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6    Feltham, R.7    Vince, J.8    Warnken, U.9    Wenger, T.10
  • 18
    • 70449084692 scopus 로고    scopus 로고
    • Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities
    • Hjerpe, R., Aillet, F., Lopitz-Otsoa, F., Lang, V., England, P., Rodriguez, M.S., Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. EMBO Rep. 10 (2009), 1250–1258.
    • (2009) EMBO Rep. , vol.10 , pp. 1250-1258
    • Hjerpe, R.1    Aillet, F.2    Lopitz-Otsoa, F.3    Lang, V.4    England, P.5    Rodriguez, M.S.6
  • 19
    • 84925949741 scopus 로고    scopus 로고
    • Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest)
    • Hospenthal, M.K., Mevissen, T.E., Komander, D., Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest). Nat. Protoc. 10 (2015), 349–361.
    • (2015) Nat. Protoc. , vol.10 , pp. 349-361
    • Hospenthal, M.K.1    Mevissen, T.E.2    Komander, D.3
  • 23
    • 84990210741 scopus 로고    scopus 로고
    • SPATA2-mediated binding of CYLD to HOIP enables CYLD recruitment to signaling complexes
    • Kupka, S., De Miguel, D., Draber, P., Martino, L., Surinova, S., Rittinger, K., Walczak, H., SPATA2-mediated binding of CYLD to HOIP enables CYLD recruitment to signaling complexes. Cell Rep. 16 (2016), 2271–2280.
    • (2016) Cell Rep. , vol.16 , pp. 2271-2280
    • Kupka, S.1    De Miguel, D.2    Draber, P.3    Martino, L.4    Surinova, S.5    Rittinger, K.6    Walczak, H.7
  • 25
    • 69049092633 scopus 로고    scopus 로고
    • NEMO/IKKgamma regulates an early NF-kappaB-independent cell-death checkpoint during TNF signaling
    • Legarda-Addison, D., Hase, H., O'Donnell, M.A., Ting, A.T., NEMO/IKKgamma regulates an early NF-kappaB-independent cell-death checkpoint during TNF signaling. Cell Death Differ. 16 (2009), 1279–1288.
    • (2009) Cell Death Differ. , vol.16 , pp. 1279-1288
    • Legarda-Addison, D.1    Hase, H.2    O'Donnell, M.A.3    Ting, A.T.4
  • 27
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin, Y., Devin, A., Rodriguez, Y., Liu, Z.G., Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev. 13 (1999), 2514–2526.
    • (1999) Genes Dev. , vol.13 , pp. 2514-2526
    • Lin, Y.1    Devin, A.2    Rodriguez, Y.3    Liu, Z.G.4
  • 29
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau, O., Tschopp, J., Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114 (2003), 181–190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 31
    • 79952503999 scopus 로고    scopus 로고
    • RIP1 comes back to life as a cell death regulator in TNFR1 signaling
    • O'Donnell, M.A., Ting, A.T., RIP1 comes back to life as a cell death regulator in TNFR1 signaling. FEBS J. 278 (2011), 877–887.
    • (2011) FEBS J. , vol.278 , pp. 877-887
    • O'Donnell, M.A.1    Ting, A.T.2
  • 32
    • 33847251527 scopus 로고    scopus 로고
    • Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling
    • O'Donnell, M.A., Legarda-Addison, D., Skountzos, P., Yeh, W.C., Ting, A.T., Ubiquitination of RIP1 regulates an NF-kappaB-independent cell-death switch in TNF signaling. Curr. Biol. 17 (2007), 418–424.
    • (2007) Curr. Biol. , vol.17 , pp. 418-424
    • O'Donnell, M.A.1    Legarda-Addison, D.2    Skountzos, P.3    Yeh, W.C.4    Ting, A.T.5
  • 36
    • 84922602504 scopus 로고    scopus 로고
    • Necroptosis and its role in inflammation
    • Pasparakis, M., Vandenabeele, P., Necroptosis and its role in inflammation. Nature 517 (2015), 311–320.
    • (2015) Nature , vol.517 , pp. 311-320
    • Pasparakis, M.1    Vandenabeele, P.2
  • 37
    • 84968919520 scopus 로고    scopus 로고
    • Holding RIPK1 on the ubiquitin leash in TNFR1 signaling
    • Peltzer, N., Darding, M., Walczak, H., Holding RIPK1 on the ubiquitin leash in TNFR1 signaling. Trends Cell Biol. 26 (2016), 445–461.
    • (2016) Trends Cell Biol. , vol.26 , pp. 445-461
    • Peltzer, N.1    Darding, M.2    Walczak, H.3
  • 39
    • 84866731086 scopus 로고    scopus 로고
    • Targeting of TAK1 in inflammatory disorders and cancer
    • Sakurai, H., Targeting of TAK1 in inflammatory disorders and cancer. Trends Pharmacol. Sci. 33 (2012), 522–530.
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 522-530
    • Sakurai, H.1
  • 41
    • 80053602333 scopus 로고    scopus 로고
    • The regulation of TNF signalling: what a tangled web we weave
    • Silke, J., The regulation of TNF signalling: what a tangled web we weave. Curr. Opin. Immunol. 23 (2011), 620–626.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 620-626
    • Silke, J.1
  • 42
    • 84931377023 scopus 로고    scopus 로고
    • The diverse role of RIP kinases in necroptosis and inflammation
    • Silke, J., Rickard, J.A., Gerlic, M., The diverse role of RIP kinases in necroptosis and inflammation. Nat. Immunol. 16 (2015), 689–697.
    • (2015) Nat. Immunol. , vol.16 , pp. 689-697
    • Silke, J.1    Rickard, J.A.2    Gerlic, M.3
  • 45
    • 84979523727 scopus 로고    scopus 로고
    • More to Life than NF-κB in TNFR1 Signaling
    • Ting, A.T., Bertrand, M.J., More to Life than NF-κB in TNFR1 Signaling. Trends Immunol. 37 (2016), 535–545.
    • (2016) Trends Immunol. , vol.37 , pp. 535-545
    • Ting, A.T.1    Bertrand, M.J.2
  • 49
    • 84960363656 scopus 로고    scopus 로고
    • NEMO prevents RIP kinase 1-mediated epithelial cell death and chronic intestinal inflammation by NF-κB-dependent and -independent functions
    • Vlantis, K., Wullaert, A., Polykratis, A., Kondylis, V., Dannappel, M., Schwarzer, R., Welz, P., Corona, T., Walczak, H., Weih, F., et al. NEMO prevents RIP kinase 1-mediated epithelial cell death and chronic intestinal inflammation by NF-κB-dependent and -independent functions. Immunity 44 (2016), 553–567.
    • (2016) Immunity , vol.44 , pp. 553-567
    • Vlantis, K.1    Wullaert, A.2    Polykratis, A.3    Kondylis, V.4    Dannappel, M.5    Schwarzer, R.6    Welz, P.7    Corona, T.8    Walczak, H.9    Weih, F.10
  • 50
    • 84984904321 scopus 로고    scopus 로고
    • SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes
    • Wagner, S.A., Satpathy, S., Beli, P., Choudhary, C., SPATA2 links CYLD to the TNF-α receptor signaling complex and modulates the receptor signaling outcomes. EMBO J. 35 (2016), 1868–1884.
    • (2016) EMBO J. , vol.35 , pp. 1868-1884
    • Wagner, S.A.1    Satpathy, S.2    Beli, P.3    Choudhary, C.4
  • 51
    • 80054852212 scopus 로고    scopus 로고
    • TNF and ubiquitin at the crossroads of gene activation, cell death, inflammation, and cancer
    • Walczak, H., TNF and ubiquitin at the crossroads of gene activation, cell death, inflammation, and cancer. Immunol. Rev. 244 (2011), 9–28.
    • (2011) Immunol. Rev. , vol.244 , pp. 9-28
    • Walczak, H.1
  • 52
    • 85013463994 scopus 로고    scopus 로고
    • ImmunoScore predicts gastric cancer postsurgical outcome
    • Wang, M., ImmunoScore predicts gastric cancer postsurgical outcome. Lancet Oncol., 18, 2017, e68.
    • (2017) Lancet Oncol. , vol.18 , pp. e68
    • Wang, M.1
  • 53
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang, L., Du, F., Wang, X., TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133 (2008), 693–703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 55
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang, Y., Fang, S., Jensen, J.P., Weissman, A.M., Ashwell, J.D., Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288 (2000), 874–877.
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.