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Volumn 292, Issue 18, 2017, Pages 7285-7294

The molecular basis for differential type i interferon signaling

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BINDING ENERGY; BINS; CELL DEATH; CHEMICAL ACTIVATION; CYTOLOGY; ENZYME ACTIVITY; GENE EXPRESSION; GLYCOPROTEINS; INTERFERONS; MOLECULES; TISSUE;

EID: 85018416130     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R116.774562     Document Type: Review
Times cited : (173)

References (100)
  • 2
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I-and type-II-interferonmediated signalling
    • Platanias, L. C. (2005) Mechanisms of type-I-and type-II-interferonmediated signalling. Nat. Rev. Immunol. 5, 375-386
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 3
    • 84943815333 scopus 로고    scopus 로고
    • Cut, copy, move, delete: The study of human interferon genes reveal multiple mechanisms underlying their evolution in amniotes
    • Krause, C. D., and Pestka, S. (2015) Cut, copy, move, delete: the study of human interferon genes reveal multiple mechanisms underlying their evolution in amniotes. Cytokine 76, 480-495
    • (2015) Cytokine , vol.76 , pp. 480-495
    • Krause, C.D.1    Pestka, S.2
  • 5
    • 33644522358 scopus 로고    scopus 로고
    • Inquiring into the differential action of interferons (IFNs): An IFN-α2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-β
    • Jaitin, D. A., Roisman, L. C., Jaks, E., Gavutis, M., Piehler, J., Van der Heyden, J., Uze, G., and Schreiber, G. (2006) Inquiring into the differential action of interferons (IFNs): an IFN-α2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-β. Mol. Cell. Biol. 26, 1888-1897
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1888-1897
    • Jaitin, D.A.1    Roisman, L.C.2    Jaks, E.3    Gavutis, M.4    Piehler, J.5    Van Der Heyden, J.6    Uze, G.7    Schreiber, G.8
  • 6
    • 77957745555 scopus 로고    scopus 로고
    • Type I interferon: Friend or foe?
    • Trinchieri, G. (2010) Type I interferon: friend or foe? J. Exp. Med. 207, 2053-2063
    • (2010) J. Exp. Med. , vol.207 , pp. 2053-2063
    • Trinchieri, G.1
  • 9
    • 84924240604 scopus 로고    scopus 로고
    • The molecular basis for functional plasticity in type I interferon signaling
    • Schreiber, G., and Piehler, J. (2015) The molecular basis for functional plasticity in type I interferon signaling. Trends Immunol. 36, 139-149
    • (2015) Trends Immunol. , vol.36 , pp. 139-149
    • Schreiber, G.1    Piehler, J.2
  • 10
    • 0029052176 scopus 로고
    • Ligand-induced association of the type I interferon receptor components
    • Cohen, B., Novick, D., Barak, S., and Rubinstein, M. (1995) Ligand-induced association of the type I interferon receptor components. Mol. Cell. Biol. 15, 4208-4214
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4208-4214
    • Cohen, B.1    Novick, D.2    Barak, S.3    Rubinstein, M.4
  • 12
    • 0037632418 scopus 로고    scopus 로고
    • The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding
    • Chill, J. H., Quadt, S. R., Levy, R., Schreiber, G., and Anglister, J. (2003) The human type I interferon receptor: NMR structure reveals the molecular basis of ligand binding. Structure 11, 791-802
    • (2003) Structure , vol.11 , pp. 791-802
    • Chill, J.H.1    Quadt, S.R.2    Levy, R.3    Schreiber, G.4    Anglister, J.5
  • 15
    • 40649124460 scopus 로고    scopus 로고
    • The em structure of a type I interferon-receptor complex reveals a novel mechanism for cytokine signaling
    • Li, Z., Strunk, J. J., Lamken, P., Piehler, J., and Walz, T. (2008) The EM structure of a type I interferon-receptor complex reveals a novel mechanism for cytokine signaling. J. Mol. Biol. 377, 715-724
    • (2008) J. Mol. Biol. , vol.377 , pp. 715-724
    • Li, Z.1    Strunk, J.J.2    Lamken, P.3    Piehler, J.4    Walz, T.5
  • 16
    • 33745966693 scopus 로고    scopus 로고
    • Variations in the unstructured C-terminal tail of interferons contribute to differential receptor binding and biological activity
    • Slutzki, M., Jaitin, D. A., Yehezkel, T. B., and Schreiber, G. (2006) Variations in the unstructured C-terminal tail of interferons contribute to differential receptor binding and biological activity. J. Mol. Biol. 360, 1019-1030
    • (2006) J. Mol. Biol. , vol.360 , pp. 1019-1030
    • Slutzki, M.1    Jaitin, D.A.2    Yehezkel, T.B.3    Schreiber, G.4
  • 17
    • 84867411811 scopus 로고    scopus 로고
    • Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation
    • Piehler, J., Thomas, C., Garcia, K. C., and Schreiber, G. (2012) Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation. Immunol. Rev. 250, 317-334
    • (2012) Immunol. Rev. , vol.250 , pp. 317-334
    • Piehler, J.1    Thomas, C.2    Garcia, K.C.3    Schreiber, G.4
  • 19
    • 20444447772 scopus 로고    scopus 로고
    • Functional cartography of the ectodomain of the type I interferon receptor subunit ifnar1
    • Lamken, P., Gavutis, M., Peters, I., Van der Heyden, J., Uzé, G., and Piehler, J. (2005) Functional cartography of the ectodomain of the type I interferon receptor subunit ifnar1. J. Mol. Biol. 350, 476-488
    • (2005) J. Mol. Biol. , vol.350 , pp. 476-488
    • Lamken, P.1    Gavutis, M.2    Peters, I.3    Van Der Heyden, J.4    Uzé, G.5    Piehler, J.6
  • 20
    • 84964595928 scopus 로고    scopus 로고
    • Type I interferon signaling is decoupled from specific receptor orientation through lenient requirements of the transmembrane domain
    • Sharma, N., Longjam, G., and Schreiber, G. (2016) Type I interferon signaling is decoupled from specific receptor orientation through lenient requirements of the transmembrane domain. J. Biol. Chem. 291, 3371-3384
    • (2016) J. Biol. Chem. , vol.291 , pp. 3371-3384
    • Sharma, N.1    Longjam, G.2    Schreiber, G.3
  • 21
    • 84918543571 scopus 로고    scopus 로고
    • Live cell micropatterning reveals the dynamics of signaling complexes at the plasma membrane
    • Löchte, S., Waichman, S., Beutel, O., You, C., and Piehler, J. (2014) Live cell micropatterning reveals the dynamics of signaling complexes at the plasma membrane. J. Cell Biol. 207, 407-418
    • (2014) J. Cell Biol. , vol.207 , pp. 407-418
    • Löchte, S.1    Waichman, S.2    Beutel, O.3    You, C.4    Piehler, J.5
  • 24
    • 4143062575 scopus 로고    scopus 로고
    • Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers
    • Lamken, P., Lata, S., Gavutis, M., and Piehler, J. (2004) Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers. J. Mol. Biol. 341, 303-318
    • (2004) J. Mol. Biol. , vol.341 , pp. 303-318
    • Lamken, P.1    Lata, S.2    Gavutis, M.3    Piehler, J.4
  • 25
    • 75149162520 scopus 로고    scopus 로고
    • NMR mapping of the IFNAR1-EC binding site on IFNα2 reveals allosteric changes in the IFNAR2-EC binding site
    • Akabayov, S. R., Biron, Z., Lamken, P., Piehler, J., and Anglister, J. (2010) NMR mapping of the IFNAR1-EC binding site on IFNα2 reveals allosteric changes in the IFNAR2-EC binding site. Biochemistry 49, 687-695
    • (2010) Biochemistry , vol.49 , pp. 687-695
    • Akabayov, S.R.1    Biron, Z.2    Lamken, P.3    Piehler, J.4    Anglister, J.5
  • 27
    • 34249687020 scopus 로고    scopus 로고
    • An interferon α2 mutant optimized by phage display for IFNAR1 binding confers specifically enhanced antitumor activities
    • Kalie, E., Jaitin, D. A., Abramovich, R., and Schreiber, G. (2007) An interferon α2 mutant optimized by phage display for IFNAR1 binding confers specifically enhanced antitumor activities. J. Biol. Chem. 282, 11602-11611
    • (2007) J. Biol. Chem. , vol.282 , pp. 11602-11611
    • Kalie, E.1    Jaitin, D.A.2    Abramovich, R.3    Schreiber, G.4
  • 28
    • 79961163823 scopus 로고    scopus 로고
    • Stochastic receptor expression determines cell fate upon interferon treatment
    • Levin, D., Harari, D., and Schreiber, G. (2011) Stochastic receptor expression determines cell fate upon interferon treatment. Mol. Cell. Biol. 31, 3252-3266
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3252-3266
    • Levin, D.1    Harari, D.2    Schreiber, G.3
  • 36
    • 84921325776 scopus 로고    scopus 로고
    • Targeting of type I interferon in systemic autoimmune diseases
    • Crow, M. K., Olferiev, M., and Kirou, K. A. (2015) Targeting of type I interferon in systemic autoimmune diseases. Transl. Res. 165, 296-305
    • (2015) Transl. Res. , vol.165 , pp. 296-305
    • Crow, M.K.1    Olferiev, M.2    Kirou, K.A.3
  • 37
    • 85048742182 scopus 로고    scopus 로고
    • Targeted therapeutics in SLE: Emerging strategies to modulate the interferon pathway
    • Oon, S., Wilson, N. J., and Wicks, I. (2016) Targeted therapeutics in SLE: emerging strategies to modulate the interferon pathway. Clin. Transl. Immunology 5, e79
    • (2016) Clin. Transl. Immunology , vol.5 , pp. e79
    • Oon, S.1    Wilson, N.J.2    Wicks, I.3
  • 39
    • 56249084550 scopus 로고    scopus 로고
    • Mutation of the IFNAR-1 receptor binding site of human IFN-α2 generates type I IFN competitive antagonists
    • Pan, M., Kalie, E., Scaglione, B. J., Raveche, E. S., Schreiber, G., and Langer, J. A. (2008) Mutation of the IFNAR-1 receptor binding site of human IFN-α2 generates type I IFN competitive antagonists. Biochemistry 47, 12018-12027
    • (2008) Biochemistry , vol.47 , pp. 12018-12027
    • Pan, M.1    Kalie, E.2    Scaglione, B.J.3    Raveche, E.S.4    Schreiber, G.5    Langer, J.A.6
  • 41
  • 42
    • 3042859189 scopus 로고    scopus 로고
    • Interferon receptor expression regulates the antiproliferative effects of interferons on cancer cells and solid tumors
    • Wagner, T. C., Velichko, S., Chesney, S. K., Biroc, S., Harde, D., Vogel, D., and Croze, E. (2004) Interferon receptor expression regulates the antiproliferative effects of interferons on cancer cells and solid tumors. Int. J. Cancer 111, 32-42
    • (2004) Int. J. Cancer , vol.111 , pp. 32-42
    • Wagner, T.C.1    Velichko, S.2    Chesney, S.K.3    Biroc, S.4    Harde, D.5    Vogel, D.6    Croze, E.7
  • 44
    • 84861205347 scopus 로고    scopus 로고
    • Interferon-β induces cellular senescence in cutaneous human papilloma virus-transformed human keratinocytes by affecting p53 transactivating activity
    • Chiantore, M. V., Vannucchi, S., Accardi, R., Tommasino, M., Percario, Z. A., Vaccari, G., Affabris, E., Fiorucci, G., and Romeo, G. (2012) Interferon-β induces cellular senescence in cutaneous human papilloma virus-transformed human keratinocytes by affecting p53 transactivating activity. PLoS ONE 7, e36909
    • (2012) PLoS ONE , vol.7 , pp. e36909
    • Chiantore, M.V.1    Vannucchi, S.2    Accardi, R.3    Tommasino, M.4    Percario, Z.A.5    Vaccari, G.6    Affabris, E.7    Fiorucci, G.8    Romeo, G.9
  • 45
    • 84894555725 scopus 로고    scopus 로고
    • Influence of type-I interferon receptor expression level on the response to type-I interferons in human pancreatic cancer cells
    • Booy, S., van Eijck, C. H. J., Dogan, F., van Koetsveld, P. M., and Hofland, L. J. (2014) Influence of type-I interferon receptor expression level on the response to type-I interferons in human pancreatic cancer cells. J. Cell. Mol. Med. 18, 492-502
    • (2014) J. Cell. Mol. Med. , vol.18 , pp. 492-502
    • Booy, S.1    Van Eijck, C.H.J.2    Dogan, F.3    Van Koetsveld, P.M.4    Hofland, L.J.5
  • 47
    • 84876100198 scopus 로고    scopus 로고
    • Hope and fear for interferon: The receptor-centric outlook on the future of interferon therapy
    • Fuchs, S. Y. (2013) Hope and fear for interferon: the receptor-centric outlook on the future of interferon therapy. J. Interferon Cytokine Res. 33, 211-225
    • (2013) J. Interferon Cytokine Res. , vol.33 , pp. 211-225
    • Fuchs, S.Y.1
  • 48
    • 0036264330 scopus 로고    scopus 로고
    • Enhanced tumor development in mice lacking a functional type I interferon receptor
    • Picaud, S., Bardot, B., De Maeyer, E., and Seif, I. (2002) Enhanced tumor development in mice lacking a functional type I interferon receptor. J. Interferon Cytokine Res. 22, 457-462
    • (2002) J. Interferon Cytokine Res. , vol.22 , pp. 457-462
    • Picaud, S.1    Bardot, B.2    De Maeyer, E.3    Seif, I.4
  • 49
    • 68849114353 scopus 로고    scopus 로고
    • Receptor density is key to the α2/β interferon differential activities
    • Moraga, I., Harari, D., Schreiber, G., Uzé, G., and Pellegrini, S. (2009) Receptor density is key to the α2/β interferon differential activities. Mol. Cell. Biol. 29, 4778-4787
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 4778-4787
    • Moraga, I.1    Harari, D.2    Schreiber, G.3    Uzé, G.4    Pellegrini, S.5
  • 50
    • 57749092917 scopus 로고    scopus 로고
    • The stability of the ternary interferon-receptor complex rather than the affinity to the individual subunits dictates differential biological activities
    • Kalie, E., Jaitin, D. A., Podoplelova, Y., Piehler, J., and Schreiber, G. (2008) The stability of the ternary interferon-receptor complex rather than the affinity to the individual subunits dictates differential biological activities. J. Biol. Chem. 283, 32925-32936
    • (2008) J. Biol. Chem. , vol.283 , pp. 32925-32936
    • Kalie, E.1    Jaitin, D.A.2    Podoplelova, Y.3    Piehler, J.4    Schreiber, G.5
  • 51
    • 84859992161 scopus 로고    scopus 로고
    • The JAK-STAT pathway at twenty
    • Stark, G. R., and Darnell, J. E., Jr. (2012) The JAK-STAT pathway at twenty. Immunity 36, 503-514
    • (2012) Immunity , vol.36 , pp. 503-514
    • Stark, G.R.1    Darnell, J.E.2
  • 52
    • 0030945179 scopus 로고    scopus 로고
    • Functional subdomains of STAT2 required for preassociation with the α interferon receptor and for signaling
    • Li, X., Leung, S., Kerr, I. M., and Stark, G. R. (1997) Functional subdomains of STAT2 required for preassociation with the α interferon receptor and for signaling. Mol. Cell. Biol. 17, 2048-2056
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2048-2056
    • Li, X.1    Leung, S.2    Kerr, I.M.3    Stark, G.R.4
  • 55
    • 0026778338 scopus 로고
    • Subunit of an α-interferon-responsive transcription factor is related to interferon regulatory factor and Myb families of DNA-binding proteins
    • Veals, S. A., Schindler, C., Leonard, D., Fu, X. Y., Aebersold, R., Darnell, J. E., Jr., and Levy, D. E. (1992) Subunit of an α-interferon-responsive transcription factor is related to interferon regulatory factor and Myb families of DNA-binding proteins. Mol. Cell. Biol. 12, 3315-3324
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3315-3324
    • Veals, S.A.1    Schindler, C.2    Leonard, D.3    Fu, X.Y.4    Aebersold, R.5    Darnell, J.E.6    Levy, D.E.7
  • 56
    • 79957999601 scopus 로고    scopus 로고
    • Chromatin dynamics of gene activation and repression in response to interferon α (IFNα) reveal new roles for phosphorylated and unphosphorylated forms of the transcription factor STAT2
    • Testoni, B., Völlenkle, C., Guerrieri, F., Gerbal-Chaloin, S., Blandino, G., and Levrero, M. (2011) Chromatin dynamics of gene activation and repression in response to interferon α (IFNα) reveal new roles for phosphorylated and unphosphorylated forms of the transcription factor STAT2. J. Biol. Chem. 286, 20217-20227
    • (2011) J. Biol. Chem. , vol.286 , pp. 20217-20227
    • Testoni, B.1    Völlenkle, C.2    Guerrieri, F.3    Gerbal-Chaloin, S.4    Blandino, G.5    Levrero, M.6
  • 59
    • 53249115175 scopus 로고    scopus 로고
    • Organization of the mouse RNA-specific adenosine deaminase Adar1 gene 5′-region and demonstration of STAT1-independent, STAT2-dependent transcriptional activation by interferon
    • George, C. X., Das, S., and Samuel, C. E. (2008) Organization of the mouse RNA-specific adenosine deaminase Adar1 gene 5′-region and demonstration of STAT1-independent, STAT2-dependent transcriptional activation by interferon. Virology 380, 338-343
    • (2008) Virology , vol.380 , pp. 338-343
    • George, C.X.1    Das, S.2    Samuel, C.E.3
  • 60
    • 79952237300 scopus 로고    scopus 로고
    • STAT2 mediates innate immunity to Dengue virus in the absence of STAT1 via the type I interferon receptor
    • Perry, S. T., Buck, M. D., Lada, S. M., Schindler, C., and Shresta, S. (2011) STAT2 mediates innate immunity to Dengue virus in the absence of STAT1 via the type I interferon receptor. PLoS Pathog. 7, e1001297
    • (2011) PLoS Pathog. , vol.7 , pp. e1001297
    • Perry, S.T.1    Buck, M.D.2    Lada, S.M.3    Schindler, C.4    Shresta, S.5
  • 61
    • 0038644820 scopus 로고    scopus 로고
    • A hybrid IRF9-STAT2 protein recapitulates interferon-stimulated gene expression and antiviral response
    • Kraus, T. A., Lau, J. F., Parisien, J. P., and Horvath, C. M. (2003) A hybrid IRF9-STAT2 protein recapitulates interferon-stimulated gene expression and antiviral response. J. Biol. Chem. 278, 13033-13038
    • (2003) J. Biol. Chem. , vol.278 , pp. 13033-13038
    • Kraus, T.A.1    Lau, J.F.2    Parisien, J.P.3    Horvath, C.M.4
  • 62
    • 0031048046 scopus 로고    scopus 로고
    • Stat2 is a transcriptional activator that requires sequence-specific contacts provided by Stat1 and p48 for stable interaction with DNA
    • Bluyssen, H. A. R., and Levy, D. E. (1997) Stat2 is a transcriptional activator that requires sequence-specific contacts provided by Stat1 and p48 for stable interaction with DNA. J. Biol. Chem. 272, 4600-4605
    • (1997) J. Biol. Chem. , vol.272 , pp. 4600-4605
    • Bluyssen, H.A.R.1    Levy, D.E.2
  • 65
    • 84873871853 scopus 로고    scopus 로고
    • Type I interferons induce apoptosis by balancing cFLIP and Caspase-8 independent of death ligands
    • Apelbaum, A., Yarden, G., Warszawski, S., Harari, D., and Schreiber, G. (2013) Type I interferons induce apoptosis by balancing cFLIP and Caspase-8 independent of death ligands. Mol. Cell. Biol. 33, 800-814
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 800-814
    • Apelbaum, A.1    Yarden, G.2    Warszawski, S.3    Harari, D.4    Schreiber, G.5
  • 66
    • 84995595388 scopus 로고    scopus 로고
    • STAT2 is a pervasive cytokine regulator due to its inhibition of STAT1 in multiple signaling pathways
    • Ho, J., Pelzel, C., Begitt, A., Mee, M., Elsheikha, H. M., Scott, D. J., and Vinkemeier, U. (2016) STAT2 is a pervasive cytokine regulator due to its inhibition of STAT1 in multiple signaling pathways. PLoS Biol. 14, e2000117
    • (2016) PLoS Biol. , vol.14 , pp. e2000117
    • Ho, J.1    Pelzel, C.2    Begitt, A.3    Mee, M.4    Elsheikha, H.M.5    Scott, D.J.6    Vinkemeier, U.7
  • 67
    • 35448938101 scopus 로고    scopus 로고
    • Upregulation of a small subset of genes drives type I interferon-induced antiviral memory
    • Jaitin, D. A., and Schreiber, G. (2007) Upregulation of a small subset of genes drives type I interferon-induced antiviral memory. J. Interferon Cytokine Res. 27, 653-664
    • (2007) J. Interferon Cytokine Res. , vol.27 , pp. 653-664
    • Jaitin, D.A.1    Schreiber, G.2
  • 68
    • 67249144899 scopus 로고    scopus 로고
    • Unphosphorylated STAT1 prolongs the expression of interferon-induced immune regulatory genes
    • Cheon, H., and Stark, G. R. (2009) Unphosphorylated STAT1 prolongs the expression of interferon-induced immune regulatory genes. Proc. Natl. Acad. Sci. U.S.A. 106, 9373-9378
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9373-9378
    • Cheon, H.1    Stark, G.R.2
  • 70
    • 0033213949 scopus 로고    scopus 로고
    • IFN-α activates Stat6 and leads to the formation of Stat2:Stat6 complexes in B cells
    • Gupta, S., Jiang, M., and Pernis, A. B. (1999) IFN-α activates Stat6 and leads to the formation of Stat2:Stat6 complexes in B cells. J. Immunol. 163, 3834-3841
    • (1999) J. Immunol. , vol.163 , pp. 3834-3841
    • Gupta, S.1    Jiang, M.2    Pernis, A.B.3
  • 71
    • 80052687211 scopus 로고    scopus 로고
    • STAT3 negatively regulates type I IFN-mediated antiviral response
    • Wang, W. B., Levy, D. E., and Lee, C. K. (2011) STAT3 negatively regulates type I IFN-mediated antiviral response. J. Immunol. 187, 2578-2585
    • (2011) J. Immunol. , vol.187 , pp. 2578-2585
    • Wang, W.B.1    Levy, D.E.2    Lee, C.K.3
  • 72
    • 84959347832 scopus 로고    scopus 로고
    • Interferon α antagonizes STAT3 and SOCS3 signaling triggered by hepatitis C virus
    • Zhao, L.-J., He, S.-F., Wang, W., Ren, H., and Qi, Z.-T. (2016) Interferon α antagonizes STAT3 and SOCS3 signaling triggered by hepatitis C virus. Cytokine 80, 48-55
    • (2016) Cytokine , vol.80 , pp. 48-55
    • Zhao, L.-J.1    He, S.-F.2    Wang, W.3    Ren, H.4    Qi, Z.-T.5
  • 73
    • 84896372779 scopus 로고    scopus 로고
    • Transcription factor STAT3 and type I interferons are corepressive insulators for differentiation of follicular helper and T helper 1 cells
    • Ray, J. P., Marshall, H. D., Laidlaw, B. J., Staron, M. M., Kaech, S. M., and Craft, J. (2014) Transcription factor STAT3 and type I interferons are corepressive insulators for differentiation of follicular helper and T helper 1 cells. Immunity 40, 367-377
    • (2014) Immunity , vol.40 , pp. 367-377
    • Ray, J.P.1    Marshall, H.D.2    Laidlaw, B.J.3    Staron, M.M.4    Kaech, S.M.5    Craft, J.6
  • 75
    • 35548931300 scopus 로고    scopus 로고
    • Pre-assembly of STAT4 with the human IFN-α/β receptor-2 subunit is mediated by the STAT4 N-domain
    • Tyler, D. R., Persky, M. E., Matthews, L. A., Chan, S., and Farrar, J. D. (2007) Pre-assembly of STAT4 with the human IFN-α/β receptor-2 subunit is mediated by the STAT4 N-domain. Mol. Immunol. 44, 1864-1872
    • (2007) Mol. Immunol. , vol.44 , pp. 1864-1872
    • Tyler, D.R.1    Persky, M.E.2    Matthews, L.A.3    Chan, S.4    Farrar, J.D.5
  • 77
    • 84868580741 scopus 로고    scopus 로고
    • Regulating type 1 IFN effects in CD8 T cells during viral infections: Changing STAT4 and STAT1 expression for function
    • Gil, M. P., Ploquin, M. J. Y., Watford, W. T., Lee, S.-H., Kim, K., Wang, X., Kanno, Y., O'Shea, J. J., and Biron, C. A. (2012) Regulating type 1 IFN effects in CD8 T cells during viral infections: changing STAT4 and STAT1 expression for function. Blood 120, 3718-3728
    • (2012) Blood , vol.120 , pp. 3718-3728
    • Gil, M.P.1    Ploquin, M.J.Y.2    Watford, W.T.3    Lee, S.-H.4    Kim, K.5    Wang, X.6    Kanno, Y.7    O'Shea, J.J.8    Biron, C.A.9
  • 81
    • 84961282473 scopus 로고    scopus 로고
    • The anti-proliferative effects of type I IFN involve STAT6-mediated regulation of SP1 and BCL6
    • Hsu, Y. A., Huang, C. C., Kung, Y. J., Lin, H. J., Chang, C. Y., Lee, K. R., and Wan, L. (2016) The anti-proliferative effects of type I IFN involve STAT6-mediated regulation of SP1 and BCL6. Cancer Lett. 375, 303-312
    • (2016) Cancer Lett. , vol.375 , pp. 303-312
    • Hsu, Y.A.1    Huang, C.C.2    Kung, Y.J.3    Lin, H.J.4    Chang, C.Y.5    Lee, K.R.6    Wan, L.7
  • 82
    • 30344461860 scopus 로고    scopus 로고
    • The p38 mitogen-activated protein kinase pathway in interferon signal transduction
    • Katsoulidis, E., Li, Y., Mears, H., and Platanias, L. C. (2005) The p38 mitogen-activated protein kinase pathway in interferon signal transduction. J. Interferon Cytokine Res. 25, 749-756
    • (2005) J. Interferon Cytokine Res. , vol.25 , pp. 749-756
    • Katsoulidis, E.1    Li, Y.2    Mears, H.3    Platanias, L.C.4
  • 86
    • 84861670735 scopus 로고    scopus 로고
    • The interferons and their receptors: Distribution and regulation
    • de Weerd, N. A., and Nguyen, T. (2012) The interferons and their receptors: distribution and regulation. Immunol. Cell Biol. 90, 483-491
    • (2012) Immunol. Cell Biol. , vol.90 , pp. 483-491
    • De Weerd, N.A.1    Nguyen, T.2
  • 89
    • 49649111204 scopus 로고    scopus 로고
    • Basal ubiquitin-independent internalization of interferon α receptor is prevented by Tyk2-mediated masking of a linear endocytic motif
    • Kumar, K. G., Varghese, B., Banerjee, A., Baker, D. P., Constantinescu, S. N., Pellegrini, S., and Fuchs, S. Y. (2008) Basal ubiquitin-independent internalization of interferon α receptor is prevented by Tyk2-mediated masking of a linear endocytic motif. J. Biol. Chem. 283, 18566-18572
    • (2008) J. Biol. Chem. , vol.283 , pp. 18566-18572
    • Kumar, K.G.1    Varghese, B.2    Banerjee, A.3    Baker, D.P.4    Constantinescu, S.N.5    Pellegrini, S.6    Fuchs, S.Y.7
  • 92
    • 33745626171 scopus 로고    scopus 로고
    • Stat-mediated signaling induced by type I and type II interferons (IFNs) is differentially controlled through lipid microdomain association and clathrin-dependent endocytosis of IFN receptors
    • Marchetti, M., Monier, M. N., Fradagrada, A., Mitchell, K., Baychelier, F., Eid, P., Johannes, L., and Lamaze, C. (2006) Stat-mediated signaling induced by type I and type II interferons (IFNs) is differentially controlled through lipid microdomain association and clathrin-dependent endocytosis of IFN receptors. Mol. Biol. Cell 17, 2896-2909
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2896-2909
    • Marchetti, M.1    Monier, M.N.2    Fradagrada, A.3    Mitchell, K.4    Baychelier, F.5    Eid, P.6    Johannes, L.7    Lamaze, C.8
  • 93
    • 33745761009 scopus 로고    scopus 로고
    • UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity
    • Malakhova, O. A., Kim, K. I., Luo, J. K., Zou, W., Kumar, K. G., Fuchs, S. Y., Shuai, K., and Zhang, D. E. (2006) UBP43 is a novel regulator of interferon signaling independent of its ISG15 isopeptidase activity. EMBO J. 25, 2358-2367
    • (2006) EMBO J. , vol.25 , pp. 2358-2367
    • Malakhova, O.A.1    Kim, K.I.2    Luo, J.K.3    Zou, W.4    Kumar, K.G.5    Fuchs, S.Y.6    Shuai, K.7    Zhang, D.E.8
  • 96
  • 99
    • 80053210241 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling (SOCS) 1 inhibits type I interferon (IFN) signaling via the interferon α receptor (IFNAR1)-associated tyrosine kinase Tyk2
    • Piganis, R. A., De Weerd, N. A., Gould, J. A., Schindler, C. W., Mansell, A., Nicholson, S. E., and Hertzog, P. J. (2011) Suppressor of cytokine signaling (SOCS) 1 inhibits type I interferon (IFN) signaling via the interferon α receptor (IFNAR1)-associated tyrosine kinase Tyk2. J. Biol. Chem. 286, 33811-33818
    • (2011) J. Biol. Chem. , vol.286 , pp. 33811-33818
    • Piganis, R.A.1    De Weerd, N.A.2    Gould, J.A.3    Schindler, C.W.4    Mansell, A.5    Nicholson, S.E.6    Hertzog, P.J.7
  • 100
    • 84931032489 scopus 로고    scopus 로고
    • Kinase inhibition, competitive binding and proteasomal degradation: Resolving the molecular function of the suppressor of cytokine signaling (SOCS) proteins
    • Linossi, E. M., and Nicholson, S. E. (2015) Kinase inhibition, competitive binding and proteasomal degradation: resolving the molecular function of the suppressor of cytokine signaling (SOCS) proteins. Immunol. Rev. 266, 123-133
    • (2015) Immunol. Rev. , vol.266 , pp. 123-133
    • Linossi, E.M.1    Nicholson, S.E.2


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