메뉴 건너뛰기




Volumn 289, Issue 25, 2014, Pages 17610-17619

Glycogen synthase kinase-3β stabilizes the interleukin (IL)-22 receptor from proteasomal degradation in murine lung epithelia

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL ORGANS; CELLS; CHEMICAL COMPOUNDS; CYTOLOGY; ENZYME ACTIVITY; PHOSPHORYLATION;

EID: 84903479494     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.551747     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 45749101727 scopus 로고    scopus 로고
    • H17 cells
    • DOI 10.1038/nature07036, PII NATURE07036
    • Bettelli, E., Korn, T., Oukka, M., and Kuchroo, V. K. (2008) Induction and effector functions of TH17 cells. Nature 453, 1051-1057 (Pubitemid 351871737)
    • (2008) Nature , vol.453 , Issue.7198 , pp. 1051-1057
    • Bettelli, E.1    Korn, T.2    Oukka, M.3    Kuchroo, V.K.4
  • 2
    • 67349275024 scopus 로고    scopus 로고
    • IL-22: A critical mediator in mucosal host defense
    • Aujla, S. J., and Kolls, J. K. (2009) IL-22: a critical mediator in mucosal host defense. J. Mol. Med (Berl.) 87, 451-454
    • (2009) J. Mol. Med (Berl.) , vol.87 , pp. 451-454
    • Aujla, S.J.1    Kolls, J.K.2
  • 3
    • 69249145293 scopus 로고    scopus 로고
    • Th17 cells at the crossroads of innate and adaptive immunity against infectious diseases at the mucosa
    • Khader, S. A., Gaffen, S. L., and Kolls, J. K. (2009) Th17 cells at the crossroads of innate and adaptive immunity against infectious diseases at the mucosa. Mucosal Immunol. 2, 403-411
    • (2009) Mucosal Immunol. , vol.2 , pp. 403-411
    • Khader, S.A.1    Gaffen, S.L.2    Kolls, J.K.3
  • 5
    • 33749318470 scopus 로고    scopus 로고
    • Interleukin (IL)-22 and IL-17 are coexpressed by Th17 cells and cooperatively enhance expression of antimicrobial peptides
    • DOI 10.1084/jem.20061308
    • Liang, S. C., Tan, X. Y., Luxenberg, D. P., Karim, R., Dunussi-Joannopoulos, K., Collins, M., and Fouser, L. A. (2006) Interleukin (IL)-22 and IL-17 are coexpressed by Th17 cells and cooperatively enhance expression of antimicrobial peptides. J. Exp. Med. 203, 2271-2279 (Pubitemid 44498362)
    • (2006) Journal of Experimental Medicine , vol.203 , Issue.10 , pp. 2271-2279
    • Liang, S.C.1    Tan, X.-Y.2    Luxenberg, D.P.3    Karim, R.4    Dunussi-Joannopoulos, K.5    Collins, M.6    Fouser, L.A.7
  • 7
    • 35348983341 scopus 로고    scopus 로고
    • Interleukin-22 but Not Interleukin-17 Provides Protection to Hepatocytes during Acute Liver Inflammation
    • DOI 10.1016/j.immuni.2007.07.023, PII S1074761307004426
    • Zenewicz, L. A., Yancopoulos, G. D., Valenzuela, D. M., Murphy, A. J., Karow, M., and Flavell, R. A. (2007) Interleukin-22 but not interleukin-17 provides protection to hepatocytes during acute liver inflammation. Immunity 27, 647-659 (Pubitemid 47615503)
    • (2007) Immunity , vol.27 , Issue.4 , pp. 647-659
    • Zenewicz, L.A.1    Yancopoulos, G.D.2    Valenzuela, D.M.3    Murphy, A.J.4    Karow, M.5    Flavell, R.A.6
  • 10
    • 84856894610 scopus 로고    scopus 로고
    • Cutting edge: A variant of the IL-23R gene associated with inflammatory bowel disease induces loss of microRNA regulation and enhanced protein production
    • Zwiers, A., Kraal, L., van de Pouw Kraan, T. C., Wurdinger, T., Bouma, G., and Kraal, G. (2012) Cutting edge: a variant of the IL-23R gene associated with inflammatory bowel disease induces loss of microRNA regulation and enhanced protein production. J. Immunol. 188, 1573-1577
    • (2012) J. Immunol. , vol.188 , pp. 1573-1577
    • Zwiers, A.1    Kraal, L.2    Van De Pouw Kraan, T.C.3    Wurdinger, T.4    Bouma, G.5    Kraal, G.6
  • 11
    • 84862636380 scopus 로고    scopus 로고
    • F-box protein FBXL19-mediated ubiquitination and degradation of the receptor for IL-33 limits pulmonary inflammation
    • Zhao, J., Wei, J., Mialki, R. K., Mallampalli, D. F., Chen, B. B., Coon, T., Zou, C., Mallampalli, R. K., and Zhao, Y. (2012) F-box protein FBXL19-mediated ubiquitination and degradation of the receptor for IL-33 limits pulmonary inflammation. Nat. Immunol. 13, 651-658
    • (2012) Nat. Immunol. , vol.13 , pp. 651-658
    • Zhao, J.1    Wei, J.2    Mialki, R.K.3    Mallampalli, D.F.4    Chen, B.B.5    Coon, T.6    Zou, C.7    Mallampalli, R.K.8    Zhao, Y.9
  • 13
    • 0037072796 scopus 로고    scopus 로고
    • Interleukin-22 (IL-22) activates the JAK/STAT, ERK, JNK, and p38 MAP kinase pathways in a rat hepatoma cell line: Pathways that are shared with and distinct from IL-10
    • Lejeune, D., Dumoutier, L., Constantinescu, S., Kruijer, W., Schuringa, J. J., and Renauld, J. C. (2002) Interleukin-22 (IL-22) activates the JAK/STAT, ERK, JNK, and p38 MAP kinase pathways in a rat hepatoma cell line: pathways that are shared with and distinct from IL-10. J. Biol. Chem. 277, 33676-33682
    • (2002) J. Biol. Chem. , vol.277 , pp. 33676-33682
    • Lejeune, D.1    Dumoutier, L.2    Constantinescu, S.3    Kruijer, W.4    Schuringa, J.J.5    Renauld, J.C.6
  • 14
    • 80555140057 scopus 로고    scopus 로고
    • Regulation of interleukin-10 receptor ubiquitination and stability by β-TrCP-containing ubiquitin E3 ligase
    • Jiang, H., Lu, Y., Yuan, L., and Liu, J. (2011) Regulation of interleukin-10 receptor ubiquitination and stability by β-TrCP-containing ubiquitin E3 ligase. PLoS One 6, e27464
    • (2011) PLoS One , vol.6
    • Jiang, H.1    Lu, Y.2    Yuan, L.3    Liu, J.4
  • 17
    • 84861867814 scopus 로고    scopus 로고
    • Ubiquitin and membrane protein turnover: From cradle to grave
    • MacGurn, J. A., Hsu, P. C., and Emr, S. D. (2012) Ubiquitin and membrane protein turnover: from cradle to grave. Annu. Rev. Biochem. 81, 231-259
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 231-259
    • MacGurn, J.A.1    Hsu, P.C.2    Emr, S.D.3
  • 18
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • DOI 10.1242/jcs.00384
    • Doble, B. W., and Woodgett, J. R. (2003) GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116, 1175-1186 (Pubitemid 36410657)
    • (2003) Journal of Cell Science , vol.116 , Issue.7 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 19
    • 79959233776 scopus 로고    scopus 로고
    • What are the bona fide GSK3 substrates?
    • Sutherland, C. (2011) What are the bona fide GSK3 substrates? Int. J. Alzheimers Dis. 2011, 505607
    • (2011) Int. J. Alzheimers Dis. , vol.2011 , pp. 505607
    • Sutherland, C.1
  • 20
    • 78951480982 scopus 로고    scopus 로고
    • LPS impairs phospholipid synthesis by triggering β-transducin repeat-containing protein (β-TrCP)-mediated polyubiquitination and degradation of the surfactant enzyme acyl-CoA:Lysophosphatidylcholine acyltransferase I (LPCAT1)
    • Zou, C., Butler, P. L., Coon, T. A., Smith, R. M., Hammen, G., Zhao, Y., Chen, B. B., and Mallampalli, R. K. (2011) LPS impairs phospholipid synthesis by triggering β-transducin repeat-containing protein (β-TrCP)-mediated polyubiquitination and degradation of the surfactant enzyme acyl-CoA: lysophosphatidylcholine acyltransferase I (LPCAT1). J. Biol. Chem. 286, 2719-2727
    • (2011) J. Biol. Chem. , vol.286 , pp. 2719-2727
    • Zou, C.1    Butler, P.L.2    Coon, T.A.3    Smith, R.M.4    Hammen, G.5    Zhao, Y.6    Chen, B.B.7    Mallampalli, R.K.8
  • 21
    • 80051541985 scopus 로고    scopus 로고
    • Acyl-CoA:Lysophosphatidylcholine acyltransferase I (Lpcat1) catalyzes histone protein O-palmitoylation to regulate mRNA synthesis
    • Zou, C., Ellis, B. M., Smith, R. M., Chen, B. B., Zhao, Y., and Mallampalli, R. K. (2011) Acyl-CoA:lysophosphatidylcholine acyltransferase I (Lpcat1) catalyzes histone protein O-palmitoylation to regulate mRNA synthesis. J. Biol. Chem. 286, 28019-28025
    • (2011) J. Biol. Chem. , vol.286 , pp. 28019-28025
    • Zou, C.1    Ellis, B.M.2    Smith, R.M.3    Chen, B.B.4    Zhao, Y.5    Mallampalli, R.K.6
  • 22
    • 4744337565 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates RBL2/p130 during quiescence
    • DOI 10.1128/MCB.24.20.8970-8980.2004
    • Litovchick, L., Chestukhin, A., and DeCaprio, J. A. (2004) Glycogen synthase kinase 3 phosphorylates RBL2/p130 during quiescence. Mol. Cell. Biol. 24, 8970-8980 (Pubitemid 39313902)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.20 , pp. 8970-8980
    • Litovchick, L.1    Chestukhin, A.2    DeCaprio, J.A.3
  • 23
    • 0037172661 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β modulates notch signaling and stability
    • DOI 10.1016/S0960-9822(02)00888-6, PII S0960982202008886
    • Foltz, D. R., Santiago, M. C., Berechid, B. E., and Nye, J. S. (2002) Glycogen synthase kinase-3β modulates notch signaling and stability. Curr. Biol. 12, 1006-1011 (Pubitemid 34703331)
    • (2002) Current Biology , vol.12 , Issue.12 , pp. 1006-1011
    • Foltz, D.R.1    Santiago, M.C.2    Berechid, B.E.3    Nye, J.S.4
  • 24
    • 33947316888 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 phosphorylates and regulates the stability of p27kip1 protein
    • Surjit, M., and Lal, S. K. (2007) Glycogen synthase kinase-3 phosphorylates and regulates the stability of p27kip1 protein. Cell Cycle 6, 580-588 (Pubitemid 46440432)
    • (2007) Cell Cycle , vol.6 , Issue.5 , pp. 580-588
    • Surjit, M.1    Lal, S.K.2
  • 25
    • 33846185851 scopus 로고    scopus 로고
    • Dual kinase-mediated regulation of PITK by CaMKII and GSK3
    • DOI 10.1016/j.cellsig.2006.08.009, PII S0898656806002038
    • Kwiek, N. C., Thacker, D. F., and Haystead, T. A. (2007) Dual kinase-mediated regulation of PITK by CaMKII and GSK3. Cell. Signal. 19, 593-599 (Pubitemid 46107810)
    • (2007) Cellular Signalling , vol.19 , Issue.3 , pp. 593-599
    • Kwiek, N.C.1    Thacker, D.F.2    Haystead, T.A.J.3
  • 26
    • 0035090317 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-mediated actin polymerization by cortactin
    • DOI 10.1038/35060051
    • Uruno, T., Liu, J., Zhang, P., Fan, Y. x., Egile, C., Li, R., Mueller, S. C., and Zhan, X. (2001) Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nat. Cell Biol. 3, 259-266 (Pubitemid 32201321)
    • (2001) Nature Cell Biology , vol.3 , Issue.3 , pp. 259-266
    • Uruno, T.1    Liu, J.2    Zhang, P.3    Fan, Y.-X.4    Egile, C.5    Li, R.6    Mueller, S.C.7    Zhan, X.8
  • 28
    • 84861740175 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase (ERK) regulates cortactin ubiquitination and degradation in lung epithelial cells
    • Zhao, J., Wei, J., Mialki, R., Zou, C., Mallampalli, R. K., and Zhao, Y. (2012) Extracellular signal-regulated kinase (ERK) regulates cortactin ubiquitination and degradation in lung epithelial cells. J. Biol. Chem. 287, 19105-19114
    • (2012) J. Biol. Chem. , vol.287 , pp. 19105-19114
    • Zhao, J.1    Wei, J.2    Mialki, R.3    Zou, C.4    Mallampalli, R.K.5    Zhao, Y.6
  • 29
    • 0028840004 scopus 로고
    • Inactivation of glycogen synthase kinase-3 by epidermal growth factor is mediated by mitogen-activated protein kinase/p90 ribosomal protein S6 kinase signaling pathway in NIH/3T3 cells
    • Eldar-Finkelman, H., Seger, R., Vandenheede, J. R., and Krebs, E. G. (1995) Inactivation of glycogen synthase kinase-3 by epidermal growth factor is mediated by mitogen-activated protein kinase/p90 ribosomal protein S6 kinase signaling pathway in NIH/3T3 cells. J. Biol. Chem. 270, 987-990
    • (1995) J. Biol. Chem. , vol.270 , pp. 987-990
    • Eldar-Finkelman, H.1    Seger, R.2    Vandenheede, J.R.3    Krebs, E.G.4
  • 30
  • 31
    • 66349089861 scopus 로고    scopus 로고
    • Masking of a nuclear signal motif by monoubiquitination leads to mislocalization and degradation of the regulatory enzyme cytidylyltransferase
    • Chen, B. B., and Mallampalli, R. K. (2009) Masking of a nuclear signal motif by monoubiquitination leads to mislocalization and degradation of the regulatory enzyme cytidylyltransferase. Mol. Cell. Biol. 29, 3062-3075
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3062-3075
    • Chen, B.B.1    Mallampalli, R.K.2
  • 32
    • 0037031887 scopus 로고    scopus 로고
    • Wnt-3A/β-catenin signaling induces transcription from the LEF-1 promoter
    • DOI 10.1074/jbc.M107977200
    • Filali, M., Cheng, N., Abbott, D., Leontiev, V., and Engelhardt, J. F. (2002) Wnt-3A/β-catenin signaling induces transcription from the LEF-1 promoter. J. Biol. Chem. 277, 33398-33410 (Pubitemid 34984863)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 33398-33410
    • Filali, M.1    Cheng, N.2    Abbott, D.3    Leontiev, V.4    Engelhardt, J.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.