메뉴 건너뛰기




Volumn 246, Issue 1, 2012, Pages 154-167

The atypical PKCs in inflammation: NF-κB and beyond

Author keywords

Carcinogenesis; Inflammation; NF B; p62; Par 4; PKC

Indexed keywords

DIACYLGLYCEROL; DROSOMYCIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 4; PROTEIN KINASE C; PROTEIN KINASE C ZETA; PROTEINASE ACTIVATED RECEPTOR 4; SERINE;

EID: 84858714507     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/j.1600-065X.2012.01093.x     Document Type: Article
Times cited : (112)

References (122)
  • 1
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification
    • Hanks SK, Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 1995;9:576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 2
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor H, Parker PJ. The extended protein kinase C superfamily. Biochem J 1998;332:281-292.
    • (1998) Biochem J , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 3
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 1984;308:693-698.
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 4
    • 77955180125 scopus 로고    scopus 로고
    • Yasutomi Nishizuka: father of protein kinase C
    • Nakamura S, Yamamura H. Yasutomi Nishizuka: father of protein kinase C. J Biochem 2010;148:125-130.
    • (2010) J Biochem , vol.148 , pp. 125-130
    • Nakamura, S.1    Yamamura, H.2
  • 5
    • 0020634260 scopus 로고
    • Protein kinase C as a possible receptor protein of tumor-promoting phorbol esters
    • Kikkawa U, Takai Y, Tanaka Y, Miyake R, Nishizuka Y. Protein kinase C as a possible receptor protein of tumor-promoting phorbol esters. J Biol Chem 1983;258:11442-11445.
    • (1983) J Biol Chem , vol.258 , pp. 11442-11445
    • Kikkawa, U.1    Takai, Y.2    Tanaka, Y.3    Miyake, R.4    Nishizuka, Y.5
  • 6
    • 0003053406 scopus 로고
    • Characterization of a specific phorbol ester aporeceptor in mouse brain cytosol
    • Leach KL, James ML, Blumberg PM. Characterization of a specific phorbol ester aporeceptor in mouse brain cytosol. Proc Natl Acad Sci USA 1983;80:4208-4212.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4208-4212
    • Leach, K.L.1    James, M.L.2    Blumberg, P.M.3
  • 7
    • 0020326790 scopus 로고
    • Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters
    • Castagna M, Takai Y, Kaibuchi K, Sano K, Kikkawa U, Nishizuka Y. Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters. J Biol Chem 1982;257:7847-7851.
    • (1982) J Biol Chem , vol.257 , pp. 7847-7851
    • Castagna, M.1    Takai, Y.2    Kaibuchi, K.3    Sano, K.4    Kikkawa, U.5    Nishizuka, Y.6
  • 8
    • 36749060688 scopus 로고    scopus 로고
    • Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants
    • Sumimoto H, Kamakura S, Ito T. Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants. Sci STKE 2007;2007:re6.
    • (2007) Sci STKE , vol.2007
    • Sumimoto, H.1    Kamakura, S.2    Ito, T.3
  • 9
    • 0035421234 scopus 로고    scopus 로고
    • Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif
    • Terasawa H, et al. Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. EMBO J 2001;20:3947-3956.
    • (2001) EMBO J , vol.20 , pp. 3947-3956
    • Terasawa, H.1
  • 10
    • 0034646677 scopus 로고    scopus 로고
    • Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase
    • Flynn P, Mellor H, Casamassima A, Parker PJ. Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase. J Biol Chem 2000;275:11064-11070.
    • (2000) J Biol Chem , vol.275 , pp. 11064-11070
    • Flynn, P.1    Mellor, H.2    Casamassima, A.3    Parker, P.J.4
  • 11
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm
    • Newton AC. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem J 2003;370:361-371.
    • (2003) Biochem J , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 12
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh DB, Ziegler W, Parker PJ. Multiple pathways control protein kinase C phosphorylation. EMBOJ 2000;19:496-503.
    • (2000) EMBOJ , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 13
    • 0025198526 scopus 로고
    • Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation
    • Pears CJ, Kour G, House C, Kemp BE, Parker PJ. Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation. Eur J Biochem 1990;194:89-94.
    • (1990) Eur J Biochem , vol.194 , pp. 89-94
    • Pears, C.J.1    Kour, G.2    House, C.3    Kemp, B.E.4    Parker, P.J.5
  • 14
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good JA, Ziegler WH, Parekh DB, Alessi DR, Cohen P, Parker PJ. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 1998;281:2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 15
    • 47949125486 scopus 로고    scopus 로고
    • The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C
    • Facchinetti V, et al. The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C. EMBO J 2008;27:1932-1943.
    • (2008) EMBO J , vol.27 , pp. 1932-1943
    • Facchinetti, V.1
  • 16
    • 47949104258 scopus 로고    scopus 로고
    • Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling
    • Ikenoue T, Inoki K, Yang Q, Zhou X, Guan KL. Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling. EMBO J 2008;27:1919-1931.
    • (2008) EMBO J , vol.27 , pp. 1919-1931
    • Ikenoue, T.1    Inoki, K.2    Yang, Q.3    Zhou, X.4    Guan, K.L.5
  • 17
    • 0034617281 scopus 로고    scopus 로고
    • A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta) and PKC-related kinase 2 by PDK1
    • Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR. A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta) and PKC-related kinase 2 by PDK1. J Biol Chem 2000;275:20806-20813.
    • (2000) J Biol Chem , vol.275 , pp. 20806-20813
    • Balendran, A.1    Biondi, R.M.2    Cheung, P.C.3    Casamayor, A.4    Deak, M.5    Alessi, D.R.6
  • 18
    • 0034161251 scopus 로고    scopus 로고
    • Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
    • Biondi RM, Cheung PC, Casamayor A, Deak M, Currie RA, Alessi DR. Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA. EMBO J 2000;19:979-988.
    • (2000) EMBO J , vol.19 , pp. 979-988
    • Biondi, R.M.1    Cheung, P.C.2    Casamayor, A.3    Deak, M.4    Currie, R.A.5    Alessi, D.R.6
  • 19
    • 33947603008 scopus 로고    scopus 로고
    • Protein kinase C and other diacylglycerol effectors in cancer
    • Griner EM, Kazanietz MG. Protein kinase C and other diacylglycerol effectors in cancer. Nat Rev Cancer 2007;7:281-294.
    • (2007) Nat Rev Cancer , vol.7 , pp. 281-294
    • Griner, E.M.1    Kazanietz, M.G.2
  • 20
    • 0033601367 scopus 로고    scopus 로고
    • Differential localization of protein kinase C delta by phorbol esters and related compounds using a fusion protein with green fluorescent protein
    • Wang QJ, Bhattacharyya D, Garfield S, Nacro K, Marquez VE, Blumberg PM. Differential localization of protein kinase C delta by phorbol esters and related compounds using a fusion protein with green fluorescent protein. J Biol Chem 1999;274:37233-37239.
    • (1999) J Biol Chem , vol.274 , pp. 37233-37239
    • Wang, Q.J.1    Bhattacharyya, D.2    Garfield, S.3    Nacro, K.4    Marquez, V.E.5    Blumberg, P.M.6
  • 21
    • 0027535742 scopus 로고
    • Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi H, Brewer KA, Exton JH. Activation of the zeta isozyme of protein kinase C by phosphatidylinositol 3, 4, 5-trisphosphate. J Biol Chem 1993;268:13-16.
    • (1993) J Biol Chem , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 22
    • 0028567280 scopus 로고
    • Phosphatidic acid activation of protein kinase C-zeta overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids
    • Limatola C, Schaap D, Moolenaar WH, van Blitterswijk WJ. Phosphatidic acid activation of protein kinase C-zeta overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids. Biochem J 1994;304:1001-1008.
    • (1994) Biochem J , vol.304 , pp. 1001-1008
    • Limatola, C.1    Schaap, D.2    Moolenaar, W.H.3    van Blitterswijk, W.J.4
  • 23
    • 0029003788 scopus 로고
    • PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid
    • Muller G, Ayoub M, Storz P, Rennecke J, Fabbro D, Pfizenmaier K. PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid. EMBO J 1995;14:1961-1969.
    • (1995) EMBO J , vol.14 , pp. 1961-1969
    • Muller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 24
    • 0027965006 scopus 로고
    • Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase
    • Lozano J, et al. Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase. J Biol Chem 1994;269:19200-19202.
    • (1994) J Biol Chem , vol.269 , pp. 19200-19202
    • Lozano, J.1
  • 25
    • 0030572696 scopus 로고    scopus 로고
    • The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C
    • DiazMeco MT, et al. The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C. Cell 1996;86:777-786.
    • (1996) Cell , vol.86 , pp. 777-786
    • DiazMeco, M.T.1
  • 26
    • 0034328882 scopus 로고    scopus 로고
    • The atypical protein kinase Cs - functional specificity mediated by specific protein adapters
    • Moscat J, Diaz-Meco MT. The atypical protein kinase Cs - functional specificity mediated by specific protein adapters. EMBO Rep 2000;1:399-403.
    • (2000) EMBO Rep , vol.1 , pp. 399-403
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 27
    • 0041625934 scopus 로고    scopus 로고
    • PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62
    • Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL. PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mol Cell 2003;12:39-50.
    • (2003) Mol Cell , vol.12 , pp. 39-50
    • Wilson, M.I.1    Gill, D.J.2    Perisic, O.3    Quinn, M.T.4    Williams, R.L.5
  • 28
    • 0141445968 scopus 로고    scopus 로고
    • Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins
    • Lamark T, et al. Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins. J Biol Chem 2003;278:34568-34581.
    • (2003) J Biol Chem , vol.278 , pp. 34568-34581
    • Lamark, T.1
  • 29
    • 1542350778 scopus 로고    scopus 로고
    • Par proteins: partners in polarization
    • Macara IG. Par proteins: partners in polarization. Curr Biol 2004;14:R160-R162.
    • (2004) Curr Biol , vol.14
    • Macara, I.G.1
  • 30
    • 0035479930 scopus 로고    scopus 로고
    • Intercellular junctions and cellular polarity: the PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity
    • Ohno S. Intercellular junctions and cellular polarity: the PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity. Curr Opin Cell Biol 2001;13:641-648.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 641-648
    • Ohno, S.1
  • 31
    • 0030911597 scopus 로고    scopus 로고
    • Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein
    • Puls A, Schmidt S, Grawe F, Stabel S. Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein. Proc Natl Acad Sci USA 1997;94:6191-6196.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6191-6196
    • Puls, A.1    Schmidt, S.2    Grawe, F.3    Stabel, S.4
  • 32
    • 0031946369 scopus 로고    scopus 로고
    • Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62
    • Sanchez P, De Carcer G, Sandoval IV, Moscat J, Diaz-Meco MT. Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol Cell Biol 1998;18:3069-3080.
    • (1998) Mol Cell Biol , vol.18 , pp. 3069-3080
    • Sanchez, P.1    De Carcer, G.2    Sandoval, I.V.3    Moscat, J.4    Diaz-Meco, M.T.5
  • 33
    • 66449114033 scopus 로고    scopus 로고
    • p62 at the crossroads of autophagy, apoptosis, and cancer
    • Moscat J, Diaz-Meco MT. p62 at the crossroads of autophagy, apoptosis, and cancer. Cell 2009;137:1001-1004.
    • (2009) Cell , vol.137 , pp. 1001-1004
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 34
    • 18744372992 scopus 로고    scopus 로고
    • The Drosophila atypical protein kinase C-ref(2)p complex constitutes a conserved module for signaling in the toll pathway
    • Avila A, Silverman N, Diaz-Meco MT, Moscat J. The Drosophila atypical protein kinase C-ref(2)p complex constitutes a conserved module for signaling in the toll pathway. Mol Cell Biol 2002;22:8787-8795.
    • (2002) Mol Cell Biol , vol.22 , pp. 8787-8795
    • Avila, A.1    Silverman, N.2    Diaz-Meco, M.T.3    Moscat, J.4
  • 35
    • 77953713630 scopus 로고    scopus 로고
    • C. elegans screen identifies autophagy genes specific to multicellular organisms
    • Tian Y, et al. C. elegans screen identifies autophagy genes specific to multicellular organisms. Cell 2010;141:1042-1055.
    • (2010) Cell , vol.141 , pp. 1042-1055
    • Tian, Y.1
  • 36
    • 70350037529 scopus 로고    scopus 로고
    • Of the atypical PKCs, Par-4 and p62: recent understandings of the biology and pathology of a PB1-dominated complex
    • Moscat J, Diaz-Meco MT, Wooten MW. Of the atypical PKCs, Par-4 and p62: recent understandings of the biology and pathology of a PB1-dominated complex. Cell Death Differ 2009;16:1426-1437.
    • (2009) Cell Death Differ , vol.16 , pp. 1426-1437
    • Moscat, J.1    Diaz-Meco, M.T.2    Wooten, M.W.3
  • 37
    • 0027395852 scopus 로고
    • Inhibition of protein kinase C zeta subspecies blocks the activation of an NF-kappa B-like activity in Xenopus laevis oocytes
    • Dominguez I, Sanz L, Arenzana-Seisdedos F, Diaz-Meco MT, Virelizier JL, Moscat J. Inhibition of protein kinase C zeta subspecies blocks the activation of an NF-kappa B-like activity in Xenopus laevis oocytes. Mol Cell Biol 1993;13:1290-1295.
    • (1993) Mol Cell Biol , vol.13 , pp. 1290-1295
    • Dominguez, I.1    Sanz, L.2    Arenzana-Seisdedos, F.3    Diaz-Meco, M.T.4    Virelizier, J.L.5    Moscat, J.6
  • 38
    • 0027178812 scopus 로고
    • Protein kinase C zeta isoform is critical for mitogenic signal transduction
    • Berra E, et al. Protein kinase C zeta isoform is critical for mitogenic signal transduction. Cell 1993;74:555-563.
    • (1993) Cell , vol.74 , pp. 555-563
    • Berra, E.1
  • 39
    • 0027295420 scopus 로고
    • A dominant negative protein kinase C zeta subspecies blocks NF-kappa B activation
    • Diaz-Meco MT, et al. A dominant negative protein kinase C zeta subspecies blocks NF-kappa B activation. Mol Cell Biol 1993;13:4770-4775.
    • (1993) Mol Cell Biol , vol.13 , pp. 4770-4775
    • Diaz-Meco, M.T.1
  • 40
    • 0029656248 scopus 로고    scopus 로고
    • Protein kinase C-zeta mediates NF-kappa B activation in human immunodeficiency virus-infected monocytes
    • Folgueira L, et al. Protein kinase C-zeta mediates NF-kappa B activation in human immunodeficiency virus-infected monocytes. J Virol 1996;70:223-231.
    • (1996) J Virol , vol.70 , pp. 223-231
    • Folgueira, L.1
  • 41
    • 0030769625 scopus 로고    scopus 로고
    • Protein phosphatase 2A is a critical regulator of protein kinase C zeta signaling targeted by SV40 small t to promote cell growth and NF-kappaB activation
    • Sontag E, Sontag JM, Garcia A. Protein phosphatase 2A is a critical regulator of protein kinase C zeta signaling targeted by SV40 small t to promote cell growth and NF-kappaB activation. EMBO J 1997;16:5662-5671.
    • (1997) EMBO J , vol.16 , pp. 5662-5671
    • Sontag, E.1    Sontag, J.M.2    Garcia, A.3
  • 42
    • 0033531795 scopus 로고    scopus 로고
    • Regulation of NF-kappaB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase C zeta in primary endothelial cells
    • Anrather J, Csizmadia V, Soares MP, Winkler H. Regulation of NF-kappaB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase C zeta in primary endothelial cells. J Biol Chem 1999;274:13594-13603.
    • (1999) J Biol Chem , vol.274 , pp. 13594-13603
    • Anrather, J.1    Csizmadia, V.2    Soares, M.P.3    Winkler, H.4
  • 43
    • 0035844233 scopus 로고    scopus 로고
    • Regulation of nuclear factor kappa B transactivation. Implication of phosphatidylinositol 3-kinase and protein kinase C zeta in c-Rel activation by tumor necrosis factor alpha
    • Martin AG, San-Antonio B, Fresno M. Regulation of nuclear factor kappa B transactivation. Implication of phosphatidylinositol 3-kinase and protein kinase C zeta in c-Rel activation by tumor necrosis factor alpha. J Biol Chem 2001;276:15840-15849.
    • (2001) J Biol Chem , vol.276 , pp. 15840-15849
    • Martin, A.G.1    San-Antonio, B.2    Fresno, M.3
  • 44
    • 33747640560 scopus 로고    scopus 로고
    • Protein kinase C zeta is up-regulated in osteoarthritic cartilage and is required for activation of NF-kappaB by tumor necrosis factor and interleukin-1 in articular chondrocytes
    • LaVallie ER, et al. Protein kinase C zeta is up-regulated in osteoarthritic cartilage and is required for activation of NF-kappaB by tumor necrosis factor and interleukin-1 in articular chondrocytes. J Biol Chem 2006;281:24124-24137.
    • (2006) J Biol Chem , vol.281 , pp. 24124-24137
    • LaVallie, E.R.1
  • 45
    • 0028176502 scopus 로고
    • zeta PKC induces phosphorylation and inactivation of I kappa B-alpha in vitro
    • Diaz-Meco MT, et al. zeta PKC induces phosphorylation and inactivation of I kappa B-alpha in vitro. EMBO J 1994;13:2842-2848.
    • (1994) EMBO J , vol.13 , pp. 2842-2848
    • Diaz-Meco, M.T.1
  • 47
    • 0029739626 scopus 로고    scopus 로고
    • Immunodeficiency in protein kinase C beta-deficient mice
    • Leitges M, et al. Immunodeficiency in protein kinase C beta-deficient mice. Science 1996;273:788-791.
    • (1996) Science , vol.273 , pp. 788-791
    • Leitges, M.1
  • 48
    • 0042525909 scopus 로고    scopus 로고
    • Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB transcriptional activation
    • Duran A, Diaz-Meco MT, Moscat J. Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB transcriptional activation. EMBO J 2003;22:3910-3918.
    • (2003) EMBO J , vol.22 , pp. 3910-3918
    • Duran, A.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 49
    • 2342522110 scopus 로고    scopus 로고
    • Shaping the nuclear action of NF-kappaB
    • Chen LF, Greene WC. Shaping the nuclear action of NF-kappaB. Nat Rev Mol Cell Biol 2004;5:392-401.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 392-401
    • Chen, L.F.1    Greene, W.C.2
  • 50
    • 33750457370 scopus 로고    scopus 로고
    • Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway
    • Perkins ND. Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway. Oncogene 2006;25:6717-6730.
    • (2006) Oncogene , vol.25 , pp. 6717-6730
    • Perkins, N.D.1
  • 51
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300
    • Zhong H, Voll RE, Ghosh S. Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell 1998;1:661-671.
    • (1998) Mol Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3
  • 52
    • 0037451357 scopus 로고    scopus 로고
    • Transcriptional activation of the NF-κB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)
    • Vermeulen L, De Wilde G, Damme PV, Vanden Berghe W, Haegeman G. Transcriptional activation of the NF-κB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1). EMBO J 2003;22:1313-1324.
    • (2003) EMBO J , vol.22 , pp. 1313-1324
    • Vermeulen, L.1    De Wilde, G.2    Damme, P.V.3    Vanden Berghe, W.4    Haegeman, G.5
  • 53
    • 0036203419 scopus 로고    scopus 로고
    • The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1
    • Zhong H, May MJ, Jimi E, Ghosh S. The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1. Mol Cell 2002;9:625-636.
    • (2002) Mol Cell , vol.9 , pp. 625-636
    • Zhong, H.1    May, M.J.2    Jimi, E.3    Ghosh, S.4
  • 54
    • 0030991201 scopus 로고    scopus 로고
    • The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism
    • Zhong H, SuYang H, Erdjument-Bromage H, Tempst P, Ghosh S. The transcriptional activity of NF-kappaB is regulated by the IkappaB-associated PKAc subunit through a cyclic AMP-independent mechanism. Cell 1997;89:413-424.
    • (1997) Cell , vol.89 , pp. 413-424
    • Zhong, H.1    SuYang, H.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 55
    • 13944253118 scopus 로고    scopus 로고
    • Targeted disruption of the zetaPKC gene results in the impairment of the NF-kappaB pathway
    • Leitges M, et al. Targeted disruption of the zetaPKC gene results in the impairment of the NF-kappaB pathway. Mol Cell 2001;8:771-780.
    • (2001) Mol Cell , vol.8 , pp. 771-780
    • Leitges, M.1
  • 56
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S. Shared principles in NF-kappaB signaling. Cell 2008;132:344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 57
    • 77950642805 scopus 로고    scopus 로고
    • Functional interplay between acetylation and methylation of the RelA subunit of NF-kappaB
    • Yang XD, Tajkhorshid E, Chen LF. Functional interplay between acetylation and methylation of the RelA subunit of NF-kappaB. Mol Cell Biol 2010;30:2170-2180.
    • (2010) Mol Cell Biol , vol.30 , pp. 2170-2180
    • Yang, X.D.1    Tajkhorshid, E.2    Chen, L.F.3
  • 58
    • 34248544993 scopus 로고    scopus 로고
    • C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB
    • Gringhuis SI, den Dunnen J, Litjens M, van Het Hof B, van Kooyk Y, Geijtenbeek TB. C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB. Immunity 2007;26:605-616.
    • (2007) Immunity , vol.26 , pp. 605-616
    • Gringhuis, S.I.1    den Dunnen, J.2    Litjens, M.3    van Het Hof, B.4    van Kooyk, Y.5    Geijtenbeek, T.B.6
  • 59
    • 67349285384 scopus 로고    scopus 로고
    • Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit
    • Yang XD, Huang B, Li M, Lamb A, Kelleher NL, Chen LF. Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit. EMBO J 2009;28:1055-1066.
    • (2009) EMBO J , vol.28 , pp. 1055-1066
    • Yang, X.D.1    Huang, B.2    Li, M.3    Lamb, A.4    Kelleher, N.L.5    Chen, L.F.6
  • 60
    • 73149099403 scopus 로고    scopus 로고
    • Regulation of NF-kappaB activity through lysine monomethylation of p65
    • Ea CK, Baltimore D. Regulation of NF-kappaB activity through lysine monomethylation of p65. Proc Natl Acad Sci USA 2009;106:18972-18977.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18972-18977
    • Ea, C.K.1    Baltimore, D.2
  • 61
    • 23944438917 scopus 로고    scopus 로고
    • Assessing acetylation of NF-kappaB
    • Chen LF, Greene WC. Assessing acetylation of NF-kappaB. Methods 2005;36:368-375.
    • (2005) Methods , vol.36 , pp. 368-375
    • Chen, L.F.1    Greene, W.C.2
  • 62
    • 78650308842 scopus 로고    scopus 로고
    • SETD6 lysine methylation of RelA couples GLP activity at chromatin to tonic repression of NF-kappaB signaling
    • Levy D, Kuo AJ, Chang Y, Schaefer U, Kitson C, Cheung P. SETD6 lysine methylation of RelA couples GLP activity at chromatin to tonic repression of NF-kappaB signaling. Nat Immunol 2011;12:29-36.
    • (2011) Nat Immunol , vol.12 , pp. 29-36
    • Levy, D.1    Kuo, A.J.2    Chang, Y.3    Schaefer, U.4    Kitson, C.5    Cheung, P.6
  • 63
    • 20144388930 scopus 로고    scopus 로고
    • Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9
    • Tachibana M, et al. Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Genes Dev 2005;19:815-826.
    • (2005) Genes Dev , vol.19 , pp. 815-826
    • Tachibana, M.1
  • 64
    • 54349095323 scopus 로고    scopus 로고
    • G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription
    • Tachibana M, Matsumura Y, Fukuda M, Kimura H, Shinkai Y. G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription. EMBO J 2008;27:2681-2690.
    • (2008) EMBO J , vol.27 , pp. 2681-2690
    • Tachibana, M.1    Matsumura, Y.2    Fukuda, M.3    Kimura, H.4    Shinkai, Y.5
  • 65
    • 80053582577 scopus 로고    scopus 로고
    • Structural basis of SETD6-mediated regulation of the NF-kB network via methyl-lysine signaling
    • Chang Y, et al. Structural basis of SETD6-mediated regulation of the NF-kB network via methyl-lysine signaling. Nucleic Acids Res 2011;39:6380-6389.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6380-6389
    • Chang, Y.1
  • 66
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of Drosophila
    • Hoffmann JA. The immune response of Drosophila. Nature 2003;426:33-38.
    • (2003) Nature , vol.426 , pp. 33-38
    • Hoffmann, J.A.1
  • 67
    • 79952757149 scopus 로고    scopus 로고
    • NF-kappaB/Rel proteins and the humoral immune responses of Drosophila melanogaster
    • Ganesan S, Aggarwal K, Paquette N, Silverman N. NF-kappaB/Rel proteins and the humoral immune responses of Drosophila melanogaster. Curr Top Microbiol Immunol 2011;349:25-60.
    • (2011) Curr Top Microbiol Immunol , vol.349 , pp. 25-60
    • Ganesan, S.1    Aggarwal, K.2    Paquette, N.3    Silverman, N.4
  • 69
    • 0345099608 scopus 로고    scopus 로고
    • Silencing of Toll pathway components by direct injection of double-stranded RNA into Drosophila adult flies
    • Goto A, Blandin S, Royet J, Reichhart JM, Levashina EA. Silencing of Toll pathway components by direct injection of double-stranded RNA into Drosophila adult flies. Nucleic Acids Res 2003;31:6619-6623.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6619-6623
    • Goto, A.1    Blandin, S.2    Royet, J.3    Reichhart, J.M.4    Levashina, E.A.5
  • 70
    • 0036682655 scopus 로고    scopus 로고
    • Role of zeta PKC in B-cell signaling and function
    • Martin P, et al. Role of zeta PKC in B-cell signaling and function. EMBO J 2002;21:4049-4057.
    • (2002) EMBO J , vol.21 , pp. 4049-4057
    • Martin, P.1
  • 71
    • 22244473678 scopus 로고    scopus 로고
    • Control of T helper 2 cell function and allergic airway inflammation by PKCζ
    • Martin P, et al. Control of T helper 2 cell function and allergic airway inflammation by PKCζ. Proc Natl Acad Sci USA 2005;102:9866-9871.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9866-9871
    • Martin, P.1
  • 72
    • 0036233983 scopus 로고    scopus 로고
    • Transcription: tantalizing times for T cells
    • Ho IC, Glimcher LH. Transcription: tantalizing times for T cells. Cell 2002;109(Suppl):S109-S120.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Ho, I.C.1    Glimcher, L.H.2
  • 73
    • 10644224394 scopus 로고    scopus 로고
    • Crosstalk between PKCzeta and the IL4/Stat6 pathway during T-cell-mediated hepatitis
    • Duran A, et al. Crosstalk between PKCzeta and the IL4/Stat6 pathway during T-cell-mediated hepatitis. EMBO J 2004;23:4595-4605.
    • (2004) EMBO J , vol.23 , pp. 4595-4605
    • Duran, A.1
  • 74
    • 0026643743 scopus 로고
    • A T-cell dependent experimental liver injury in mice inducible by concanavalin A
    • Tiegs G, Hentschel J, Wendel A. A T-cell dependent experimental liver injury in mice inducible by concanavalin A. J Clin Invest 1992;90:196-203.
    • (1992) J Clin Invest , vol.90 , pp. 196-203
    • Tiegs, G.1    Hentschel, J.2    Wendel, A.3
  • 75
    • 0344496062 scopus 로고    scopus 로고
    • IKKbeta is required for prevention of apoptosis mediated by cell-bound but not by circulating TNFalpha
    • Maeda S, Chang L, Li ZW, Luo JL, Leffert H, Karin M. IKKbeta is required for prevention of apoptosis mediated by cell-bound but not by circulating TNFalpha. Immunity 2003;19:725-737.
    • (2003) Immunity , vol.19 , pp. 725-737
    • Maeda, S.1    Chang, L.2    Li, Z.W.3    Luo, J.L.4    Leffert, H.5    Karin, M.6
  • 76
    • 21244472975 scopus 로고    scopus 로고
    • IKKbeta couples hepatocyte death to cytokine-driven compensatory proliferation that promotes chemical hepatocarcinogenesis
    • Maeda S, Kamata H, Luo JL, Leffert H, Karin M. IKKbeta couples hepatocyte death to cytokine-driven compensatory proliferation that promotes chemical hepatocarcinogenesis. Cell 2005;121:977-990.
    • (2005) Cell , vol.121 , pp. 977-990
    • Maeda, S.1    Kamata, H.2    Luo, J.L.3    Leffert, H.4    Karin, M.5
  • 77
    • 0042834253 scopus 로고    scopus 로고
    • Crucial role of IL-4/STAT6 in T cell-mediated hepatitis: up-regulating eotaxins and IL-5 and recruiting leukocytes
    • Jaruga B, Hong F, Sun R, Radaeva S, Gao B. Crucial role of IL-4/STAT6 in T cell-mediated hepatitis: up-regulating eotaxins and IL-5 and recruiting leukocytes. J Immunol 2003;171:3233-3244.
    • (2003) J Immunol , vol.171 , pp. 3233-3244
    • Jaruga, B.1    Hong, F.2    Sun, R.3    Radaeva, S.4    Gao, B.5
  • 78
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • Ghosh S, Karin M. Missing pieces in the NF-kappaB puzzle. Cell 2002;109(Suppl):S81-S96.
    • (2002) Cell , vol.109 , Issue.SUPPL.
    • Ghosh, S.1    Karin, M.2
  • 79
    • 0242585506 scopus 로고    scopus 로고
    • Genetic inactivation of Par4 results in hyperactivation of NF-κB and impairment of JNK and p38
    • Garcia-Cao I, Lafuente M, Criado L, Diaz-Meco M, Serrano M, Moscat J. Genetic inactivation of Par4 results in hyperactivation of NF-κB and impairment of JNK and p38. EMBO Rep 2003;4:307-312.
    • (2003) EMBO Rep , vol.4 , pp. 307-312
    • Garcia-Cao, I.1    Lafuente, M.2    Criado, L.3    Diaz-Meco, M.4    Serrano, M.5    Moscat, J.6
  • 81
    • 65249117082 scopus 로고    scopus 로고
    • Thymic OX40 expression discriminates cells undergoing strong responses to selection ligands
    • Klinger M, Kim JK, Chmura SA, Barczak A, Erle DJ, Killeen N. Thymic OX40 expression discriminates cells undergoing strong responses to selection ligands. J Immunol 2009;182:4581-4589.
    • (2009) J Immunol , vol.182 , pp. 4581-4589
    • Klinger, M.1    Kim, J.K.2    Chmura, S.A.3    Barczak, A.4    Erle, D.J.5    Killeen, N.6
  • 82
    • 59049090061 scopus 로고    scopus 로고
    • Loss of PKC lambda/iota impairs Th2 establishment and allergic airway inflammation in vivo
    • Yang JQ, Leitges M, Duran A, Diaz-Meco MT, Moscat J. Loss of PKC lambda/iota impairs Th2 establishment and allergic airway inflammation in vivo. Proc Natl Acad Sci USA 2009;106:1099-1104.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1099-1104
    • Yang, J.Q.1    Leitges, M.2    Duran, A.3    Diaz-Meco, M.T.4    Moscat, J.5
  • 83
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: lessons in polarity
    • Suzuki A, Ohno S. The PAR-aPKC system: lessons in polarity. J Cell Sci 2006;119:979-987.
    • (2006) J Cell Sci , vol.119 , pp. 979-987
    • Suzuki, A.1    Ohno, S.2
  • 84
    • 33751347857 scopus 로고    scopus 로고
    • The Scribble and Par complexes in polarity and migration: friends or foes?
    • Humbert PO, Dow LE, Russell SM. The Scribble and Par complexes in polarity and migration: friends or foes? Trends Cell Biol 2006;16:622-630.
    • (2006) Trends Cell Biol , vol.16 , pp. 622-630
    • Humbert, P.O.1    Dow, L.E.2    Russell, S.M.3
  • 85
    • 77956631023 scopus 로고    scopus 로고
    • PKCzeta-regulated inflammation in the nonhematopoietic compartment is critical for obesity-induced glucose intolerance
    • Lee SJ, et al. PKCzeta-regulated inflammation in the nonhematopoietic compartment is critical for obesity-induced glucose intolerance. Cell Metab 2010;12:65-77.
    • (2010) Cell Metab , vol.12 , pp. 65-77
    • Lee, S.J.1
  • 86
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • Hotamisligil GS. Inflammation and metabolic disorders. Nature 2006;444:860-867.
    • (2006) Nature , vol.444 , pp. 860-867
    • Hotamisligil, G.S.1
  • 87
    • 34250773451 scopus 로고    scopus 로고
    • Mechanisms of obesity-associated insulin resistance: many choices on the menu
    • Qatanani M, Lazar MA. Mechanisms of obesity-associated insulin resistance: many choices on the menu. Genes Dev 2007;21:1443-1455.
    • (2007) Genes Dev , vol.21 , pp. 1443-1455
    • Qatanani, M.1    Lazar, M.A.2
  • 88
    • 57349101675 scopus 로고    scopus 로고
    • A stress signaling pathway in adipose tissue regulates hepatic insulin resistance
    • Sabio G, et al. A stress signaling pathway in adipose tissue regulates hepatic insulin resistance. Science 2008;322:1539-1543.
    • (2008) Science , vol.322 , pp. 1539-1543
    • Sabio, G.1
  • 89
    • 51349156218 scopus 로고    scopus 로고
    • Insulin sensitivity: modulation by nutrients and inflammation
    • Schenk S, Saberi M, Olefsky JM. Insulin sensitivity: modulation by nutrients and inflammation. J Clin Invest 2008;118:2992-3002.
    • (2008) J Clin Invest , vol.118 , pp. 2992-3002
    • Schenk, S.1    Saberi, M.2    Olefsky, J.M.3
  • 91
    • 44349112305 scopus 로고    scopus 로고
    • Adipocyte-derived Th2 cytokines and myeloid PPARdelta regulate macrophage polarization and insulin sensitivity
    • Kang K, et al. Adipocyte-derived Th2 cytokines and myeloid PPARdelta regulate macrophage polarization and insulin sensitivity. Cell Metab 2008;7:485-495.
    • (2008) Cell Metab , vol.7 , pp. 485-495
    • Kang, K.1
  • 92
    • 44349161098 scopus 로고    scopus 로고
    • Alternative M2 activation of Kupffer cells by PPARdelta ameliorates obesity-induced insulin resistance
    • Odegaard JI, et al. Alternative M2 activation of Kupffer cells by PPARdelta ameliorates obesity-induced insulin resistance. Cell Metab 2008;7:496-507.
    • (2008) Cell Metab , vol.7 , pp. 496-507
    • Odegaard, J.I.1
  • 93
    • 33747886310 scopus 로고    scopus 로고
    • Cell signaling and function organized by PB1 domain interactions
    • Moscat J, Diaz-Meco MT, Albert A, Campuzano S. Cell signaling and function organized by PB1 domain interactions. Mol Cell 2006;23:631-640.
    • (2006) Mol Cell , vol.23 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 94
    • 0033153320 scopus 로고    scopus 로고
    • The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation
    • Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J. The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. EBMO J 1999;18:3044-3053.
    • (1999) EBMO J , vol.18 , pp. 3044-3053
    • Sanz, L.1    Sanchez, P.2    Lallena, M.J.3    Diaz-Meco, M.T.4    Moscat, J.5
  • 95
    • 0034599476 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway
    • Sanz L, Diaz-Meco MT, Nakano H, Moscat J. The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway. EMBO J 2000;19:1576-1586.
    • (2000) EMBO J , vol.19 , pp. 1576-1586
    • Sanz, L.1    Diaz-Meco, M.T.2    Nakano, H.3    Moscat, J.4
  • 96
    • 0036094026 scopus 로고    scopus 로고
    • Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone
    • Laurin N, Brown JP, Morissette J, Raymond V. Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone. Am J Hum Genet 2002;70:1582-1588.
    • (2002) Am J Hum Genet , vol.70 , pp. 1582-1588
    • Laurin, N.1    Brown, J.P.2    Morissette, J.3    Raymond, V.4
  • 97
    • 0037108914 scopus 로고    scopus 로고
    • Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease
    • Hocking LJ, et al. Domain-specific mutations in sequestosome 1 (SQSTM1) cause familial and sporadic Paget's disease. Hum Mol Genet 2002;11:2735-2739.
    • (2002) Hum Mol Genet , vol.11 , pp. 2735-2739
    • Hocking, L.J.1
  • 99
    • 0442325388 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis
    • Duran A, et al. The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis. Dev Cell 2004;6:303-309.
    • (2004) Dev Cell , vol.6 , pp. 303-309
    • Duran, A.1
  • 100
    • 56049117643 scopus 로고    scopus 로고
    • A SQSTM1/p62 mutation linked to Paget's disease increases the osteoclastogenic potential of the bone microenvironment
    • Hiruma Y, et al. A SQSTM1/p62 mutation linked to Paget's disease increases the osteoclastogenic potential of the bone microenvironment. Hum Mol Genet 2008;17:3708-3719.
    • (2008) Hum Mol Genet , vol.17 , pp. 3708-3719
    • Hiruma, Y.1
  • 101
    • 78650912040 scopus 로고    scopus 로고
    • Contributions of the measles virus nucleocapsid gene and the SQSTM1/p62(P392L) mutation to Paget's disease
    • Kurihara N, et al. Contributions of the measles virus nucleocapsid gene and the SQSTM1/p62(P392L) mutation to Paget's disease. Cell Metab 2011;13:23-34.
    • (2011) Cell Metab , vol.13 , pp. 23-34
    • Kurihara, N.1
  • 102
    • 27444433045 scopus 로고    scopus 로고
    • The p62 scaffold regulates nerve growth factor-induced NF-kappa B activation by influencing TRAF6 polyubiquitination
    • Wooten MW, Geetha T, Seibehener ML, Babu JR, Diaz-Meco MT, Moscat J. The p62 scaffold regulates nerve growth factor-induced NF-kappa B activation by influencing TRAF6 polyubiquitination. J Biol Chem 2005;280:35625-35629.
    • (2005) J Biol Chem , vol.280 , pp. 35625-35629
    • Wooten, M.W.1    Geetha, T.2    Seibehener, M.L.3    Babu, J.R.4    Diaz-Meco, M.T.5    Moscat, J.6
  • 103
    • 41249084239 scopus 로고    scopus 로고
    • The signaling adaptor p62 is an important NF-kappa B mediator in tumorigenesis
    • Duran A, et al. The signaling adaptor p62 is an important NF-kappa B mediator in tumorigenesis. Cancer Cell 2008;13:343-354.
    • (2008) Cancer Cell , vol.13 , pp. 343-354
    • Duran, A.1
  • 104
    • 33747624440 scopus 로고    scopus 로고
    • The signaling adapter p62 is an important mediator of T helper 2 cell function and allergic airway inflammation
    • Martin P, Diaz-Meco MT, Moscat J. The signaling adapter p62 is an important mediator of T helper 2 cell function and allergic airway inflammation. EMBO J 2006;25:3524-3533.
    • (2006) EMBO J , vol.25 , pp. 3524-3533
    • Martin, P.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 105
    • 66549108847 scopus 로고    scopus 로고
    • Increased signaling through p62 in the marrow microenvironment increases myeloma cell growth and osteoclast formation
    • Hiruma Y, et al. Increased signaling through p62 in the marrow microenvironment increases myeloma cell growth and osteoclast formation. Blood 2009;113:4894-4902.
    • (2009) Blood , vol.113 , pp. 4894-4902
    • Hiruma, Y.1
  • 106
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin V, et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell 2009;33:505-516.
    • (2009) Mol Cell , vol.33 , pp. 505-516
    • Kirkin, V.1
  • 107
    • 77957758100 scopus 로고    scopus 로고
    • NBR1 is a new PB1 signalling adapter in Th2 differentiation and allergic airway inflammation in vivo
    • Yang JQ, Liu H, Diaz-Meco MT, Moscat J. NBR1 is a new PB1 signalling adapter in Th2 differentiation and allergic airway inflammation in vivo. EMBO J 2010;29:3421-3433.
    • (2010) EMBO J , vol.29 , pp. 3421-3433
    • Yang, J.Q.1    Liu, H.2    Diaz-Meco, M.T.3    Moscat, J.4
  • 108
    • 0028015669 scopus 로고
    • Commonality of the gene programs induced by effectors of apoptosis in androgen-dependent and -independent prostate cells
    • Sells SF, et al. Commonality of the gene programs induced by effectors of apoptosis in androgen-dependent and -independent prostate cells. Cell Growth Differ 1994;5:457-466.
    • (1994) Cell Growth Differ , vol.5 , pp. 457-466
    • Sells, S.F.1
  • 109
    • 69149099134 scopus 로고    scopus 로고
    • Simultaneous inactivation of Par-4 and PTEN in vivo leads to synergistic NF-kappaB activation and invasive prostate carcinoma
    • Fernandez-Marcos PJ, et al. Simultaneous inactivation of Par-4 and PTEN in vivo leads to synergistic NF-kappaB activation and invasive prostate carcinoma. Proc Natl Acad Sci USA 2009;106:12962-12967.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12962-12967
    • Fernandez-Marcos, P.J.1
  • 110
    • 33745298519 scopus 로고    scopus 로고
    • Nuclear factor-[kappa]B in cancer development and progression
    • Karin M. Nuclear factor-[kappa]B in cancer development and progression. Nature 2006;441:431-436.
    • (2006) Nature , vol.441 , pp. 431-436
    • Karin, M.1
  • 111
    • 33947196921 scopus 로고    scopus 로고
    • Inactivation of the candidate tumor suppressor par-4 in endometrial cancer
    • Moreno-Bueno G, et al. Inactivation of the candidate tumor suppressor par-4 in endometrial cancer. Cancer Res 2007;67:1927-1934.
    • (2007) Cancer Res , vol.67 , pp. 1927-1934
    • Moreno-Bueno, G.1
  • 112
    • 22144496103 scopus 로고    scopus 로고
    • Tumour-suppression activity of the proapoptotic regulator Par4
    • Garcia-Cao I, et al. Tumour-suppression activity of the proapoptotic regulator Par4. EMBO Rep 2005;6:577-583.
    • (2005) EMBO Rep , vol.6 , pp. 577-583
    • Garcia-Cao, I.1
  • 113
    • 49949109707 scopus 로고    scopus 로고
    • Par-4 inhibits Akt and suppresses Ras-induced lung tumorigenesis
    • Joshi J, et al. Par-4 inhibits Akt and suppresses Ras-induced lung tumorigenesis. EMBO J 2008;27:2181-2193.
    • (2008) EMBO J , vol.27 , pp. 2181-2193
    • Joshi, J.1
  • 114
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer: a review
    • Bos JL. Ras oncogenes in human cancer: a review. Cancer Res 1989;49:4682-4689.
    • (1989) Cancer Res , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 115
    • 0041883654 scopus 로고    scopus 로고
    • Tumor induction by an endogenous K-ras oncogene is highly dependent on cellular context
    • Guerra C, et al. Tumor induction by an endogenous K-ras oncogene is highly dependent on cellular context. Cancer Cell 2003;4:111-120.
    • (2003) Cancer Cell , vol.4 , pp. 111-120
    • Guerra, C.1
  • 116
    • 11144356354 scopus 로고    scopus 로고
    • Endogenous oncogenic K-ras(G12D) stimulates proliferation and widespread neoplastic and developmental defects
    • Tuveson DA, et al. Endogenous oncogenic K-ras(G12D) stimulates proliferation and widespread neoplastic and developmental defects. Cancer Cell 2004;5:375-387.
    • (2004) Cancer Cell , vol.5 , pp. 375-387
    • Tuveson, D.A.1
  • 117
    • 0035893318 scopus 로고    scopus 로고
    • Induction and apoptotic regression of lung adenocarcinomas by regulation of a K-Ras transgene in the presence and absence of tumor suppressor genes
    • Fisher GH, et al. Induction and apoptotic regression of lung adenocarcinomas by regulation of a K-Ras transgene in the presence and absence of tumor suppressor genes. Genes Dev 2001;15:3249-3262.
    • (2001) Genes Dev , vol.15 , pp. 3249-3262
    • Fisher, G.H.1
  • 118
    • 15444374561 scopus 로고    scopus 로고
    • Mouse models for human lung cancer
    • Meuwissen R, Berns A. Mouse models for human lung cancer. Genes Dev 2005;19:643-664.
    • (2005) Genes Dev , vol.19 , pp. 643-664
    • Meuwissen, R.1    Berns, A.2
  • 119
    • 27844506524 scopus 로고    scopus 로고
    • Akt-regulated pathways in prostate cancer
    • Majumder PK, Sellers WR. Akt-regulated pathways in prostate cancer. Oncogene 2005;24:7465-7474.
    • (2005) Oncogene , vol.24 , pp. 7465-7474
    • Majumder, P.K.1    Sellers, W.R.2
  • 120
    • 44849117768 scopus 로고    scopus 로고
    • Akt-dependent regulation of NF-{kappa}B is controlled by mTOR and Raptor in association with IKK
    • Dan HC, Cooper MJ, Cogswell PC, Duncan JA, Ting JP, Baldwin AS. Akt-dependent regulation of NF-{kappa}B is controlled by mTOR and Raptor in association with IKK. Genes Dev 2008;22:1490-1500.
    • (2008) Genes Dev , vol.22 , pp. 1490-1500
    • Dan, H.C.1    Cooper, M.J.2    Cogswell, P.C.3    Duncan, J.A.4    Ting, J.P.5    Baldwin, A.S.6
  • 121
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM. Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 2005;307:1098-1101.
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 122
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
    • Manning BD, Tee AR, Logsdon MN, Blenis J, Cantley LC. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol Cell 2002;10:151-162.
    • (2002) Mol Cell , vol.10 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon, M.N.3    Blenis, J.4    Cantley, L.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.