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Volumn 140, Issue 3, 2010, Pages 338-348

Double-Stranded RNA-Dependent Protein Kinase Links Pathogen Sensing with Stress and Metabolic Homeostasis

Author keywords

CELLBIO; HUMDISEASE; SIGNALING

Indexed keywords

INSULIN; INSULIN RECEPTOR SUBSTRATE 1; INSULIN RECEPTOR SUBSTRATE 2; PROTEIN KINASE; PROTEIN KINASE R; STRESS ACTIVATED PROTEIN KINASE;

EID: 75749108288     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2010.01.001     Document Type: Article
Times cited : (425)

References (34)
  • 3
    • 3142590775 scopus 로고    scopus 로고
    • Association of diabetes and hepatitis C infection: epidemiologic evidence and pathophysiologic insights
    • Bahtiyar G., Shin J.J., Aytaman A., Sowers J.R., and McFarlane S.I. Association of diabetes and hepatitis C infection: epidemiologic evidence and pathophysiologic insights. Curr. Diab. Rep. 4 (2004) 194-198
    • (2004) Curr. Diab. Rep. , vol.4 , pp. 194-198
    • Bahtiyar, G.1    Shin, J.J.2    Aytaman, A.3    Sowers, J.R.4    McFarlane, S.I.5
  • 4
    • 0037064118 scopus 로고    scopus 로고
    • Functional characterization of pkr gene products expressed in cells from mice with a targeted deletion of the N terminus or C terminus domain of PKR
    • Baltzis D., Li S., and Koromilas A.E. Functional characterization of pkr gene products expressed in cells from mice with a targeted deletion of the N terminus or C terminus domain of PKR. J. Biol. Chem. 277 (2002) 38364-38372
    • (2002) J. Biol. Chem. , vol.277 , pp. 38364-38372
    • Baltzis, D.1    Li, S.2    Koromilas, A.E.3
  • 5
    • 0034082457 scopus 로고    scopus 로고
    • PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex
    • Bonnet M.C., Weil R., Dam E., Hovanessian A.G., and Meurs E.F. PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex. Mol. Cell. Biol. 20 (2000) 4532-4542
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4532-4542
    • Bonnet, M.C.1    Weil, R.2    Dam, E.3    Hovanessian, A.G.4    Meurs, E.F.5
  • 6
    • 54449092414 scopus 로고    scopus 로고
    • Protein kinase R-dependent regulation of interleukin-10 in response to double-stranded RNA
    • Chakrabarti A., Sadler A.J., Kar N., Young H.A., Silverman R.H., and Williams B.R. Protein kinase R-dependent regulation of interleukin-10 in response to double-stranded RNA. J. Biol. Chem. 283 (2008) 25132-25139
    • (2008) J. Biol. Chem. , vol.283 , pp. 25132-25139
    • Chakrabarti, A.1    Sadler, A.J.2    Kar, N.3    Young, H.A.4    Silverman, R.H.5    Williams, B.R.6
  • 7
    • 0035855632 scopus 로고    scopus 로고
    • Activation of the interferon-inducible protein kinase PKR by hepatocellular carcinoma derived-hepatitis C virus core protein
    • Delhem N., Sabile A., Gajardo R., Podevin P., Abadie A., Blaton M.A., Kremsdorf D., Beretta L., and Brechot C. Activation of the interferon-inducible protein kinase PKR by hepatocellular carcinoma derived-hepatitis C virus core protein. Oncogene 20 (2001) 5836-5845
    • (2001) Oncogene , vol.20 , pp. 5836-5845
    • Delhem, N.1    Sabile, A.2    Gajardo, R.3    Podevin, P.4    Abadie, A.5    Blaton, M.A.6    Kremsdorf, D.7    Beretta, L.8    Brechot, C.9
  • 8
    • 39149104320 scopus 로고    scopus 로고
    • The role for endoplasmic reticulum stress in diabetes mellitus
    • Eizirik D.L., Cardozo A.K., and Cnop M. The role for endoplasmic reticulum stress in diabetes mellitus. Endocr. Rev. 29 (2008) 42-61
    • (2008) Endocr. Rev. , vol.29 , pp. 42-61
    • Eizirik, D.L.1    Cardozo, A.K.2    Cnop, M.3
  • 10
    • 3442895916 scopus 로고    scopus 로고
    • Inhibition of insulin sensitivity by free fatty acids requires activation of multiple serine kinases in 3T3-L1 adipocytes
    • Gao Z., Zhang X., Zuberi A., Hwang D., Quon M.J., Lefevre M., and Ye J. Inhibition of insulin sensitivity by free fatty acids requires activation of multiple serine kinases in 3T3-L1 adipocytes. Mol. Endocrinol. 18 (2004) 2024-2034
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2024-2034
    • Gao, Z.1    Zhang, X.2    Zuberi, A.3    Hwang, D.4    Quon, M.J.5    Lefevre, M.6    Ye, J.7
  • 12
    • 0034663942 scopus 로고    scopus 로고
    • The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin
    • Goh K.C., deVeer M.J., and Williams B.R. The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin. EMBO J. 19 (2000) 4292-4297
    • (2000) EMBO J. , vol.19 , pp. 4292-4297
    • Goh, K.C.1    deVeer, M.J.2    Williams, B.R.3
  • 14
    • 34548419344 scopus 로고    scopus 로고
    • Adipocyte stress: The endoplasmic reticulum and metabolic disease
    • Gregor M.G., and Hotamisligil G.S. Adipocyte stress: The endoplasmic reticulum and metabolic disease. J. Lipid Res. 48 (2007) 1905-1914
    • (2007) J. Lipid Res. , vol.48 , pp. 1905-1914
    • Gregor, M.G.1    Hotamisligil, G.S.2
  • 15
    • 0028804388 scopus 로고
    • Potential requirement of a functional double-stranded RNA-dependent protein kinase (PKR) for the tumoricidal activation of macrophages by lipopolysaccharide or IFN-alpha beta, but not IFN-gamma
    • Gusella G.L., Musso T., Rottschafer S.E., Pulkki K., and Varesio L. Potential requirement of a functional double-stranded RNA-dependent protein kinase (PKR) for the tumoricidal activation of macrophages by lipopolysaccharide or IFN-alpha beta, but not IFN-gamma. J. Immunol. 154 (1995) 345-354
    • (1995) J. Immunol. , vol.154 , pp. 345-354
    • Gusella, G.L.1    Musso, T.2    Rottschafer, S.E.3    Pulkki, K.4    Varesio, L.5
  • 17
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M., and Sonenberg N. Translational control in stress and apoptosis. Nat. Rev. Mol. Cell Biol. 6 (2005) 318-327
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 18
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • Hotamisligil G.S. Inflammation and metabolic disorders. Nature 444 (2006) 860-867
    • (2006) Nature , vol.444 , pp. 860-867
    • Hotamisligil, G.S.1
  • 19
    • 56749164791 scopus 로고    scopus 로고
    • Nutrient sensing and inflammation in metabolic diseases
    • Hotamisligil G.S., and Erbay E. Nutrient sensing and inflammation in metabolic diseases. Nat. Rev. Immunol. 8 (2008) 923-934
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 923-934
    • Hotamisligil, G.S.1    Erbay, E.2
  • 20
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance
    • Hotamisligil G.S., Peraldi P., Budavari A., Ellis R., White M.F., and Spiegelman B.M. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha- and obesity-induced insulin resistance. Science 271 (1996) 665-668
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 22
    • 0028243096 scopus 로고
    • Mechanism of interferon action motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity
    • McCormack S.J., Ortega L.G., Doohan J.P., and Samuel C.E. Mechanism of interferon action motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity. Virology 198 (1994) 92-99
    • (1994) Virology , vol.198 , pp. 92-99
    • McCormack, S.J.1    Ortega, L.G.2    Doohan, J.P.3    Samuel, C.E.4
  • 24
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 25
    • 0027418321 scopus 로고
    • The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • Samuel C.E. The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans. J. Biol. Chem. 268 (1993) 7603-7606
    • (1993) J. Biol. Chem. , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 26
    • 0035408430 scopus 로고    scopus 로고
    • Mechanisms of beta-cell death in response to double-stranded (ds) RNA and interferon-gamma: dsRNA-dependent protein kinase apoptosis and nitric oxide-dependent necrosis
    • Scarim A.L., Arnush M., Blair L.A., Concepcion J., Heitmeier M.R., Scheuner D., Kaufman R.J., Ryerse J., Buller R.M., and Corbett J.A. Mechanisms of beta-cell death in response to double-stranded (ds) RNA and interferon-gamma: dsRNA-dependent protein kinase apoptosis and nitric oxide-dependent necrosis. Am. J. Pathol. 159 (2001) 273-283
    • (2001) Am. J. Pathol. , vol.159 , pp. 273-283
    • Scarim, A.L.1    Arnush, M.2    Blair, L.A.3    Concepcion, J.4    Heitmeier, M.R.5    Scheuner, D.6    Kaufman, R.J.7    Ryerse, J.8    Buller, R.M.9    Corbett, J.A.10
  • 28
    • 33847236171 scopus 로고    scopus 로고
    • Genetic deletion of PKR abrogates TNF-induced activation of IkappaBalpha kinase, JNK, Akt and cell proliferation but potentiates p44/p42 MAPK and p38 MAPK activation
    • Takada Y., Ichikawa H., Pataer A., Swisher S., and Aggarwal B.B. Genetic deletion of PKR abrogates TNF-induced activation of IkappaBalpha kinase, JNK, Akt and cell proliferation but potentiates p44/p42 MAPK and p38 MAPK activation. Oncogene 26 (2007) 1201-1212
    • (2007) Oncogene , vol.26 , pp. 1201-1212
    • Takada, Y.1    Ichikawa, H.2    Pataer, A.3    Swisher, S.4    Aggarwal, B.B.5
  • 29
  • 30
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano F., Wang X., Bertolotti A., Zhang Y., Chung P., Harding H.P., and Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287 (2000) 664-666
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 31
    • 63249084374 scopus 로고    scopus 로고
    • Can we learn from viruses how to prevent type 1 diabetes?: the role of viral infections in the pathogenesis of type 1 diabetes and the development of novel combination therapies
    • von Herrath M. Can we learn from viruses how to prevent type 1 diabetes?: the role of viral infections in the pathogenesis of type 1 diabetes and the development of novel combination therapies. Diabetes 58 (2009) 2-11
    • (2009) Diabetes , vol.58 , pp. 2-11
    • von Herrath, M.1
  • 32
    • 0035800333 scopus 로고    scopus 로고
    • Signal integration via PKR
    • Williams B.R. Signal integration via PKR. Sci. STKE 2001 (2001) RE2
    • (2001) Sci. STKE , vol.2001
    • Williams, B.R.1
  • 33
    • 0030030997 scopus 로고    scopus 로고
    • Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR)
    • Wu S., and Kaufman R.J. Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR). J. Biol. Chem. 271 (1996) 1756-1763
    • (1996) J. Biol. Chem. , vol.271 , pp. 1756-1763
    • Wu, S.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.