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Volumn 5, Issue , 2015, Pages

RACK1 antagonizes TNF-α-induced cell death by promoting p38 activation

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; GNB2-RS1 PROTEIN, MOUSE; GNB2L1 PROTEIN, HUMAN; GUANINE NUCLEOTIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 6; MITOGEN ACTIVATED PROTEIN KINASE P38; NEUROPEPTIDE; PROTEIN BINDING; TUMOR NECROSIS FACTOR; TUMOR PROTEIN;

EID: 84941966262     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep14298     Document Type: Article
Times cited : (10)

References (25)
  • 1
    • 76749088358 scopus 로고    scopus 로고
    • Pathological roles of MAPK signaling pathways in human diseases
    • Kim, E. K. & Choi, E. J. Pathological roles of MAPK signaling pathways in human diseases. Biochim. Biophys. Acta. 1802, 396-405 (2010).
    • (2010) Biochim. Biophys. Acta. , vol.1802 , pp. 396-405
    • Kim, E.K.1    Choi, E.J.2
  • 2
    • 84883199752 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in innate immunity
    • Arthur, J. S. & Ley, S. C. Mitogen-activated protein kinases in innate immunity. Nat. Rev. Immunol. 13, 679-692 (2013).
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 679-692
    • Arthur, J.S.1    Ley, S.C.2
  • 3
    • 76749126360 scopus 로고    scopus 로고
    • Selective unresponsiveness to the inhibition of p38 MAPK activation by cAMP helps L929 fbroblastoma cells escape TNF-α-induced cell death
    • Wang, J., Tang, R., Lv, M., Zhang, J. & Shen, B. Selective unresponsiveness to the inhibition of p38 MAPK activation by cAMP helps L929 fbroblastoma cells escape TNF-α-induced cell death. Mol. Cancer. 9, 6 (2010).
    • (2010) Mol. Cancer. , vol.9 , pp. 6
    • Wang, J.1    Tang, R.2    Lv, M.3    Zhang, J.4    Shen, B.5
  • 4
    • 84864597042 scopus 로고    scopus 로고
    • RACK1 research-ships passing in the night?
    • Gibson, T. J. RACK1 research-ships passing in the night? FEBS Lett. 586, 2787-2789 (2012).
    • (2012) FEBS Lett. , vol.586 , pp. 2787-2789
    • Gibson, T.J.1
  • 5
    • 0029113131 scopus 로고
    • Interaction of protein kinase C with RACK1, a receptor for activated C-kinase: A role in beta protein kinase C mediated signal transduction
    • Mochly-Rosen, D., Smith, B., Chen, C., Disatnik, M. & Ron, D. Interaction of protein kinase C with RACK1, a receptor for activated C-kinase: a role in beta protein kinase C mediated signal transduction. Biochem. Soc. Trans. 23, 596-600 (1995).
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 596-600
    • Mochly-Rosen, D.1    Smith, B.2    Chen, C.3    Disatnik, M.4    Ron, D.5
  • 6
    • 23044464191 scopus 로고    scopus 로고
    • RACK1 mediates activation of JNK by protein kinase C
    • Lopez-Bergami, P. et al. RACK1 mediates activation of JNK by protein kinase C. Mol. Cell. 19, 309-320 (2005).
    • (2005) Mol. Cell. , vol.19 , pp. 309-320
    • Lopez-Bergami, P.1
  • 7
    • 34247606483 scopus 로고    scopus 로고
    • Rewired ERK-JNK signaling pathways in melanoma
    • Lopez-Bergami, P. et al. Rewired ERK-JNK signaling pathways in melanoma. Cancer Cell. 11, 447-460 (2007).
    • (2007) Cancer Cell. , vol.11 , pp. 447-460
    • Lopez-Bergami, P.1
  • 8
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto K., Fukuda, H., Imajoh-Ohmi, S., Saito, H. & Takekawa, M. Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat. Cell. Biol. 10, 1324-1332 (2008).
    • (2008) Nat. Cell. Biol. , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 9
    • 84872127055 scopus 로고    scopus 로고
    • Receptor for activated C kinase 1 promotes hepatocellular carcinoma growth by enhancing mitogen-activated protein kinase kinase 7 activity
    • Guo, Y. et al. Receptor for activated C kinase 1 promotes hepatocellular carcinoma growth by enhancing mitogen-activated protein kinase kinase 7 activity. Hepatology. 57, 140-151 (2013).
    • (2013) Hepatology. , vol.57 , pp. 140-151
    • Guo, Y.1
  • 10
    • 83155192804 scopus 로고    scopus 로고
    • TNF-α-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex i and II members
    • Vanlangenakker, N. et al. TNF-α-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
  • 11
    • 10044265209 scopus 로고    scopus 로고
    • JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species
    • Ventura, J. J., Cogswell, P., Flavell, R. A., Baldwin Jr., A. S. & Davis, R. J. JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species. Genes. Dev. 18, 2905-2915 (2004).
    • (2004) Genes. Dev. , vol.18 , pp. 2905-2915
    • Ventura, J.J.1    Cogswell, P.2    Flavell, R.A.3    Baldwin, A.S.4    Davis, R.J.5
  • 12
    • 34249817910 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling in hepatocyte apoptosis
    • Hatano, E. Tumor necrosis factor signaling in hepatocyte apoptosis. J. Gastroenterol. Hepatol. 22, S43-S44 (2008).
    • (2008) J. Gastroenterol. Hepatol. , vol.22 , pp. S43-S44
    • Hatano, E.1
  • 13
    • 84863549085 scopus 로고    scopus 로고
    • Ribosomal RACK1 promotes chemoresistance and growth in human hepatocellular carcinoma
    • Ruan, Y. et al. Ribosomal RACK1 promotes chemoresistance and growth in human hepatocellular carcinoma. J. Clin. Invest. 122, 2554-2566 (2012).
    • (2012) J. Clin. Invest. , vol.122 , pp. 2554-2566
    • Ruan, Y.1
  • 14
    • 75649127967 scopus 로고    scopus 로고
    • Identifcation of RACK1 and protein kinase C alpha as integral components of the mammalian circadian clock
    • Robles, M. S., Boyault, C., Knutti, D., Padmanabhan, K. & Weitz, C. J. Identifcation of RACK1 and protein kinase C alpha as integral components of the mammalian circadian clock. Science. 327, 463-466 (2010).
    • (2010) Science. , vol.327 , pp. 463-466
    • Robles, M.S.1    Boyault, C.2    Knutti, D.3    Padmanabhan, K.4    Weitz, C.J.5
  • 15
    • 84863271200 scopus 로고    scopus 로고
    • RACK1 promotes non-small-cell lung cancer tumorigenicity through activating sonic hedgehog signaling pathway
    • Shi, S. et al. RACK1 promotes non-small-cell lung cancer tumorigenicity through activating sonic hedgehog signaling pathway. J. Biol. Chem. 287, 7845-7858 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 7845-7858
    • Shi, S.1
  • 16
    • 84874522368 scopus 로고    scopus 로고
    • Interaction of MCM7 and RACK1 for activation of MCM7 and cell growth
    • Zhang, X. Y. et al. Interaction of MCM7 and RACK1 for activation of MCM7 and cell growth. Am. J. Pathol. 182, 796-805 (2013).
    • (2013) Am. J. Pathol. , vol.182 , pp. 796-805
    • Zhang, X.Y.1
  • 17
    • 84930511364 scopus 로고    scopus 로고
    • Te scafold protein RACK1 mediates the RANKL-dependent activation of p38 MAPK in osteoclast precursors
    • Jin, J., Lee, D., Choi, Y. & Lee, S. Y. Te scafold protein RACK1 mediates the RANKL-dependent activation of p38 MAPK in osteoclast precursors. Sci. Signal. 8, ra54 (2015).
    • (2015) Sci. Signal. , vol.8 , pp. ra54
    • Jin, J.1    Lee, D.2    Choi, Y.3    Lee, S.Y.4
  • 18
    • 84897634211 scopus 로고    scopus 로고
    • RACK1 modulates NF-κ B activation by interfering with the interaction between TRAF2 and the IKK complex
    • Yao, F. et al. RACK1 modulates NF-κ B activation by interfering with the interaction between TRAF2 and the IKK complex. Cell. Res. 24, 359-371 (2014).
    • (2014) Cell. Res. , vol.24 , pp. 359-371
    • Yao, F.1
  • 19
    • 36849058617 scopus 로고    scopus 로고
    • RACK1 targets the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway to link integrin engagement with focal adhesion disassembly and cell motility
    • Vomastek, T. et al. RACK1 targets the extracellular signal-regulated kinase/mitogen-activated protein kinase pathway to link integrin engagement with focal adhesion disassembly and cell motility. Mol. Cell. Biol. 27, 8296-8305 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8296-8305
    • Vomastek, T.1
  • 20
    • 36448978124 scopus 로고    scopus 로고
    • TNF-α is critical for antitumor but not antiviral T cell immunity in mice
    • Calzascia, T. et al. TNF-α is critical for antitumor but not antiviral T cell immunity in mice. J. Clin. Invest. 117, 3833-3845 (2007).
    • (2007) J. Clin. Invest. , vol.117 , pp. 3833-3845
    • Calzascia, T.1
  • 21
    • 0019781507 scopus 로고
    • Mouse liver cell culture. I. Hepatocyte isolation
    • Klaunig, J. E. et al. Mouse liver cell culture. I. Hepatocyte isolation. In Vitro. 17, 913-925 (1981).
    • (1981) Vitro. , vol.17 , pp. 913-925
    • Klaunig, J.E.1
  • 22
    • 8344260568 scopus 로고    scopus 로고
    • Ferritin heavy chain upregulation by NF-kappaB inhibits TNF-α-induced apoptosis by suppressing reactive oxygen species
    • Pham, C. G. et al. Ferritin heavy chain upregulation by NF-kappaB inhibits TNF-α-induced apoptosis by suppressing reactive oxygen species. Cell. 119, 529-542 (2004).
    • (2004) Cell. , vol.119 , pp. 529-542
    • Pham, C.G.1
  • 23
    • 10044247350 scopus 로고    scopus 로고
    • C-Jun N-terminal protein kinase 1 (JNK1), but not JNK2, is essential for tumor necrosis factor α-induced c-Jun kinase activation and apoptosis
    • Liu, J., Minemoto, Y. & Lin, A. c-Jun N-terminal protein kinase 1 (JNK1), but not JNK2, is essential for tumor necrosis factor α-induced c-Jun kinase activation and apoptosis. Mol. Cell. Biol. 24, 10844-10856 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10844-10856
    • Liu, J.1    Minemoto, Y.2    Lin, A.3
  • 24
    • 34249331264 scopus 로고    scopus 로고
    • Novel strategies for inhibition of the p38 MAPK pathway
    • Zhang, J., Shen, B. & Lin, A. Novel strategies for inhibition of the p38 MAPK pathway. Trends Pharmacol. Sci. 28, 286-295 (2007).
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 286-295
    • Zhang, J.1    Shen, B.2    Lin, A.3
  • 25
    • 84883740369 scopus 로고    scopus 로고
    • Disruption of TAB1/p38α interaction using a cell-permeable peptide limits myocardial ischemia/reperfusion injury
    • Wang, Q. et al. Disruption of TAB1/p38α interaction using a cell-permeable peptide limits myocardial ischemia/reperfusion injury. Mol. Ter. 21, 1668-1677 (2013).
    • (2013) Mol. Ter. , vol.21 , pp. 1668-1677
    • Wang, Q.1


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