메뉴 건너뛰기




Volumn 83, Issue 8, 1998, Pages 815-823

Interferon induction of TAP1: The phosphatase SHP-1 regulates crossover between the IFN-α/β and the IFN-γ signal-transduction pathways

Author keywords

Endothelial cell; Interferon; MHC class I; Phosphatase; Transporter associated with antigen processing (TAP)

Indexed keywords

ALPHA INTERFERON; BETA INTERFERON; GAMMA INTERFERON; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PHOSPHATASE; PROTEIN TYROSINE KINASE;

EID: 0032547850     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.83.8.815     Document Type: Article
Times cited : (42)

References (46)
  • 1
    • 0026500826 scopus 로고
    • Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer
    • Spies T, Cerundolo V, Colonna M, Cresswell P, Townsend A, DeMars R. Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. Nature. 1992;355:644-646.
    • (1992) Nature , vol.355 , pp. 644-646
    • Spies, T.1    Cerundolo, V.2    Colonna, M.3    Cresswell, P.4    Townsend, A.5    DeMars, R.6
  • 2
    • 0027050452 scopus 로고
    • TAP1 mutant mice are deficient in antigen presentation, surface class I molecules and CD4-CD8+T cells
    • Van Kaer L, Ashton-Rickardt P, Ploegh H, Tonegawa S. TAP1 mutant mice are deficient in antigen presentation, surface class I molecules and CD4-CD8+T cells. Cell. 1992;71:1205-1214.
    • (1992) Cell , vol.71 , pp. 1205-1214
    • Van Kaer, L.1    Ashton-Rickardt, P.2    Ploegh, H.3    Tonegawa, S.4
  • 4
    • 0025020492 scopus 로고
    • Antigen presentation requires transport of MHC class I molecules from the endoplasmic reticulum
    • Cox JH, Yewdell JW, Eisenlohr LC, Johnson PR, Bennink JR. Antigen presentation requires transport of MHC class I molecules from the endoplasmic reticulum. Science. 1990;247:715-718.
    • (1990) Science , vol.247 , pp. 715-718
    • Cox, J.H.1    Yewdell, J.W.2    Eisenlohr, L.C.3    Johnson, P.R.4    Bennink, J.R.5
  • 5
    • 0026055288 scopus 로고
    • Viral persistence in neurons explained by lack of major histocompatibility class I expression
    • Joly E, Mucke L, Oldstone M. Viral persistence in neurons explained by lack of major histocompatibility class I expression. Science. 1991;253: 1283-1285.
    • (1991) Science , vol.253 , pp. 1283-1285
    • Joly, E.1    Mucke, L.2    Oldstone, M.3
  • 6
    • 0023905982 scopus 로고
    • Effects of recombinant gamma-interferon on HLA-DR and DQ expression by skin cells in short-term organ culture
    • Messadi D, Pober J, Murphy G. Effects of recombinant gamma-interferon on HLA-DR and DQ expression by skin cells in short-term organ culture. Lab Invest. 1988;58:61-67.
    • (1988) Lab Invest , vol.58 , pp. 61-67
    • Messadi, D.1    Pober, J.2    Murphy, G.3
  • 7
    • 0021821539 scopus 로고
    • α-Interferon-induced transcription of HLA and metallothionein genes containing homologous upstream sequences
    • Friedman R, Stark G. α-Interferon-induced transcription of HLA and metallothionein genes containing homologous upstream sequences. Nature. 1985;314:637-639.
    • (1985) Nature , vol.314 , pp. 637-639
    • Friedman, R.1    Stark, G.2
  • 8
    • 0025357775 scopus 로고
    • Tumor necrosis factor and immune interferon synergistically increase transcription of HLA class I heavy- and light-chain genes in vascular endothelium
    • Johnson D, Pober J. Tumor necrosis factor and immune interferon synergistically increase transcription of HLA class I heavy- and light-chain genes in vascular endothelium. Proc Natl Acad Sci U S A. 1990;87: 5183-5187.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5183-5187
    • Johnson, D.1    Pober, J.2
  • 9
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell J Jr. STATs and gene regulation. Science. 1997;277:1630-1635.
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell J., Jr.1
  • 10
    • 0024989359 scopus 로고
    • Tyk2, prototype of a novel class of non-receptor tyrosine kinase genes
    • Firmbach-Kraft I, Byers M, Shows T, Dalla F, Krolewski J. Tyk2, prototype of a novel class of non-receptor tyrosine kinase genes. Oncogene. 1990;5:1329-1336.
    • (1990) Oncogene , vol.5 , pp. 1329-1336
    • Firmbach-Kraft, I.1    Byers, M.2    Shows, T.3    Dalla, F.4    Krolewski, J.5
  • 11
    • 0026648703 scopus 로고
    • Activation of transcription factors by interferon-alpha in a cell-free system
    • David M, Larner A. Activation of transcription factors by interferon-alpha in a cell-free system. Science. 1992;257:813-815.
    • (1992) Science , vol.257 , pp. 813-815
    • David, M.1    Larner, A.2
  • 12
    • 0025172081 scopus 로고
    • ISGF3, the transcriptional activator induced by interferon α, consists of multiple interacting polypeptide chains
    • Fu X-Y, Kessler D, Veals S, Levy D, Darnell JE Jr. ISGF3, the transcriptional activator induced by interferon α, consists of multiple interacting polypeptide chains. Proc Natl Acad Sci U S A. 1990;87: 8555-8559.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 8555-8559
    • Fu, X.-Y.1    Kessler, D.2    Veals, S.3    Levy, D.4    Darnell J.E., Jr.5
  • 13
    • 0023987751 scopus 로고
    • Interferon-induced nuclear factors that bind a shared promoter element correlate with positive and negative control
    • Levy D, Kessler D, Pine R, Reich N, Darnell J Jr. Interferon-induced nuclear factors that bind a shared promoter element correlate with positive and negative control. Genes Dev. 1988;2:383-393.
    • (1988) Genes Dev , vol.2 , pp. 383-393
    • Levy, D.1    Kessler, D.2    Pine, R.3    Reich, N.4    Darnell J., Jr.5
  • 14
    • 0026735084 scopus 로고
    • JAK2, a third member of the JAK family of protein tyrosine kjnases
    • Harpur A, Andres A, Ziemiecki A, Aston R, Wilks A. JAK2, a third member of the JAK family of protein tyrosine kjnases. Oncogene. 1992; 7:1347-1353.
    • (1992) Oncogene , vol.7 , pp. 1347-1353
    • Harpur, A.1    Andres, A.2    Ziemiecki, A.3    Aston, R.4    Wilks, A.5
  • 15
    • 0026019924 scopus 로고
    • Cytoplasmic activation of GAF, an IFN-γ-regulated DNA-binding factor
    • Decker T, Lew DJ, Mirkovitch J, Darnell JE Jr. Cytoplasmic activation of GAF, an IFN-γ-regulated DNA-binding factor. EMBO J. 1991;10: 927-932.
    • (1991) EMBO J , vol.10 , pp. 927-932
    • Decker, T.1    Lew, D.J.2    Mirkovitch, J.3    Darnell J.E., Jr.4
  • 16
    • 0025270456 scopus 로고
    • Synergistic interaction between interferon-α and interferon-γ through induced synthesis of one subunit of the transcription factor ISGF3
    • Levy D, Lew D, Decker T, Kessler D, Darnell J Jr. Synergistic interaction between interferon-α and interferon-γ through induced synthesis of one subunit of the transcription factor ISGF3. EMBO J. 1990;9:1105-1111.
    • (1990) EMBO J , vol.9 , pp. 1105-1111
    • Levy, D.1    Lew, D.2    Decker, T.3    Kessler, D.4    Darnell J., Jr.5
  • 17
    • 0026072139 scopus 로고
    • Two distinct alpha-interferon-dependent signal transduction pathways may contribute to activation of transcription of the guanylate-binding protein gene
    • Decker T, Lew D, Darnell J Jr. Two distinct alpha-interferon-dependent signal transduction pathways may contribute to activation of transcription of the guanylate-binding protein gene. Mol Cell Biol. 1991;11: 5147-5153.
    • (1991) Mol Cell Biol , vol.11 , pp. 5147-5153
    • Decker, T.1    Lew, D.2    Darnell J., Jr.3
  • 18
    • 0027090310 scopus 로고
    • Activation of transcription by IFN-γ: Tyrosine phosphorylation of a 91-kD DNa binding protein
    • Shuai K, Schindler C, Prezioso V, Darnell J Jr. Activation of transcription by IFN-γ: tyrosine phosphorylation of a 91-kD DNA binding protein. Science. 1992;258:1808-1812.
    • (1992) Science , vol.258 , pp. 1808-1812
    • Shuai, K.1    Schindler, C.2    Prezioso, V.3    Darnell J., Jr.4
  • 19
    • 0030582671 scopus 로고    scopus 로고
    • The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP?
    • Scharenberg A, Kinet J-P. The emerging field of receptor-mediated inhibitory signaling: SHP or SHIP? Cell. 1996;87:961-964.
    • (1996) Cell , vol.87 , pp. 961-964
    • Scharenberg, A.1    Kinet, J.-P.2
  • 20
    • 0030038677 scopus 로고    scopus 로고
    • The SH2 domain-containing tyrosine phosphate PTP1D is required for interferon α/β-induced gene expression
    • David M, Zhou G, Pine R, Dixon J, Larner A. The SH2 domain-containing tyrosine phosphate PTP1D is required for interferon α/β-induced gene expression. J Biol Chem. 1996;271:15862-15865.
    • (1996) J Biol Chem , vol.271 , pp. 15862-15865
    • David, M.1    Zhou, G.2    Pine, R.3    Dixon, J.4    Larner, A.5
  • 22
    • 0028972719 scopus 로고
    • Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1
    • David M, Chen H, Goelz S, Lamer A, Neel B. Differential regulation of the alpha/beta interferon-stimulated Jak/Stat pathway by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol Cell Biol. 1995;15: 7050-7058.
    • (1995) Mol Cell Biol , vol.15 , pp. 7050-7058
    • David, M.1    Chen, H.2    Goelz, S.3    Lamer, A.4    Neel, B.5
  • 23
    • 0029128365 scopus 로고
    • Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase
    • Yetter A, Uddin S, Krolewski J, Jiao H, Yi T, Platanias L. Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase. J Biol Chem. 1995;270:18179-18182.
    • (1995) J Biol Chem , vol.270 , pp. 18179-18182
    • Yetter, A.1    Uddin, S.2    Krolewski, J.3    Jiao, H.4    Yi, T.5    Platanias, L.6
  • 24
    • 0030457034 scopus 로고    scopus 로고
    • The role of protein tyrosine phosphatase SHP-1 in the regulation of IFN-gamma signaling in neural cells
    • Massa P, Wu C. The role of protein tyrosine phosphatase SHP-1 in the regulation of IFN-gamma signaling in neural cells. J Immunol. 1996;157: 5139-5144.
    • (1996) J Immunol , vol.157 , pp. 5139-5144
    • Massa, P.1    Wu, C.2
  • 25
    • 0031053335 scopus 로고    scopus 로고
    • Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells
    • Beauchemin N, Kunath T, Robitaille J, Chow B, Turbide C, Daniels E, Veillette A. Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells. Oncogene. 1997; 14:783-790.
    • (1997) Oncogene , vol.14 , pp. 783-790
    • Beauchemin, N.1    Kunath, T.2    Robitaille, J.3    Chow, B.4    Turbide, C.5    Daniels, E.6    Veillette, A.7
  • 26
    • 0030854145 scopus 로고    scopus 로고
    • Positive effects of SH2 domain-containing tyrosine phosphatase SHP-1 on epidermal growth factor- and interferon-γ-stimulated activation of STAT transcription factors in HeLa cells
    • You M, Zhao Z. Positive effects of SH2 domain-containing tyrosine phosphatase SHP-1 on epidermal growth factor- and interferon-γ-stimulated activation of STAT transcription factors in HeLa cells. J Biol Chem. 1997;272:23376-23381.
    • (1997) J Biol Chem , vol.272 , pp. 23376-23381
    • You, M.1    Zhao, Z.2
  • 27
    • 0026468645 scopus 로고
    • Cytokines increase transporter in antigen processing-1 expression more rapidly than HLA class I expression in endothelial cells
    • Epperson D, Arnold D, Spies T, Cresswell P, Pober J, Johnson D. Cytokines increase transporter in antigen processing-1 expression more rapidly than HLA class I expression in endothelial cells. J Immunol. 1992;149:3297-3301.
    • (1992) J Immunol , vol.149 , pp. 3297-3301
    • Epperson, D.1    Arnold, D.2    Spies, T.3    Cresswell, P.4    Pober, J.5    Johnson, D.6
  • 28
    • 0030999544 scopus 로고    scopus 로고
    • Interferon-γ rapidly increases peptide transporter (TAP) subunit expression and peptide transport capacity in endothelial cells
    • Ma W-L, Lehner P, Cresswell P, Pober J, Johnson D. Interferon-γ rapidly increases peptide transporter (TAP) subunit expression and peptide transport capacity in endothelial cells. J Biol Chem. 1997;272: 16585-16590.
    • (1997) J Biol Chem , vol.272 , pp. 16585-16590
    • Ma, W.-L.1    Lehner, P.2    Cresswell, P.3    Pober, J.4    Johnson, D.5
  • 29
    • 0029930581 scopus 로고    scopus 로고
    • Kinetically-coordinated induction of TAP1 and HLA class I by IFN-γ: The rapid induction of TAP1 by IFN-γ is mediated by STAT1α
    • Min W, Pober J, Johnson D. Kinetically-coordinated induction of TAP1 and HLA class I by IFN-γ: the rapid induction of TAP1 by IFN-γ is mediated by STAT1α. J Immunol. 1996;156:3174-3183.
    • (1996) J Immunol , vol.156 , pp. 3174-3183
    • Min, W.1    Pober, J.2    Johnson, D.3
  • 30
    • 0028097932 scopus 로고
    • Tyrosine phosphorylated p91 binds to a single element in the ISGF2/IRF-1 promoter to mediate induction by IFNα and IFNγ, and is likely to autoregulate the p91 gene
    • Pine R, Canova A, Schindler C. Tyrosine phosphorylated p91 binds to a single element in the ISGF2/IRF-1 promoter to mediate induction by IFNα and IFNγ, and is likely to autoregulate the p91 gene. Eur Mol Biol Org J. 1994;13:158-167.
    • (1994) Eur Mol Biol Org J , vol.13 , pp. 158-167
    • Pine, R.1    Canova, A.2    Schindler, C.3
  • 31
    • 0027957398 scopus 로고
    • HLA class I heavy chain gene promoter elements mediating synergy between tumor necrosis factor and interferons
    • Johnson D, Pober J. HLA class I heavy chain gene promoter elements mediating synergy between tumor necrosis factor and interferons. Mol Cell Biol. 1994;14:1322-1332.
    • (1994) Mol Cell Biol , vol.14 , pp. 1322-1332
    • Johnson, D.1    Pober, J.2
  • 32
    • 0025881471 scopus 로고
    • Peptide binding to empty HLA-B27 molecules of viable human cells
    • Benjamin R, Madrigal J, Parham P. Peptide binding to empty HLA-B27 molecules of viable human cells. Nature. 1991;351:74-77.
    • (1991) Nature , vol.351 , pp. 74-77
    • Benjamin, R.1    Madrigal, J.2    Parham, P.3
  • 33
    • 0030027139 scopus 로고    scopus 로고
    • Can graft endothelial cells initiate a host anti-graft immune response?
    • Pober J, Orosz C, Rose M, Savage C. Can graft endothelial cells initiate a host anti-graft immune response? Transplantation. 1996;61: 343-349.
    • (1996) Transplantation , vol.61 , pp. 343-349
    • Pober, J.1    Orosz, C.2    Rose, M.3    Savage, C.4
  • 34
    • 0028921613 scopus 로고
    • Transcriptional regulation of the intercellular adhesion molecule-1 gene by inflammatory cytokine in human endothelial cells
    • Ledebur H, Parks T. Transcriptional regulation of the intercellular adhesion molecule-1 gene by inflammatory cytokine in human endothelial cells. J Biol Chem. 1995;270:933-943.
    • (1995) J Biol Chem , vol.270 , pp. 933-943
    • Ledebur, H.1    Parks, T.2
  • 35
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells
    • Schreiber E, Matthias P, Müller M, Schaffner W. Rapid detection of octamer binding proteins with 'mini-extracts,' prepared from a small number of cells. Nucleic Acids Res. 1989;17:6419.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Müller, M.3    Schaffner, W.4
  • 36
    • 0020645073 scopus 로고
    • Eukaryotic gene transcription with purified components
    • Dignam J, Martin P, Shastry B, Roeder R. Eukaryotic gene transcription with purified components. Methods Enzymol. 1983;101: 582-598.
    • (1983) Methods Enzymol , vol.101 , pp. 582-598
    • Dignam, J.1    Martin, P.2    Shastry, B.3    Roeder, R.4
  • 37
    • 0030273083 scopus 로고    scopus 로고
    • Regulation of LMP2 and TAP1 genes by IRF-1 explains the paucity of CD8+ T cells in IRF-1 -/- Mice
    • White L, Wright K, Felix N, Ruffner H, Reis L, Pine R, Ting J. Regulation of LMP2 and TAP1 genes by IRF-1 explains the paucity of CD8+ T cells in IRF-1 -/- mice. Immunity. 1996;5:365-376.
    • (1996) Immunity , vol.5 , pp. 365-376
    • White, L.1    Wright, K.2    Felix, N.3    Ruffner, H.4    Reis, L.5    Pine, R.6    Ting, J.7
  • 38
    • 0025886837 scopus 로고
    • Isolation and characterization of a new mutant human cell line unresponsive to alpha and beta interferons
    • John J, McKendry R, Pellegrini S, Flavell D, Kerr I, Stark G. Isolation and characterization of a new mutant human cell line unresponsive to alpha and beta interferons. Mol Cell Biol. 1991;11:4189-4195.
    • (1991) Mol Cell Biol , vol.11 , pp. 4189-4195
    • John, J.1    McKendry, R.2    Pellegrini, S.3    Flavell, D.4    Kerr, I.5    Stark, G.6
  • 39
    • 0028242693 scopus 로고
    • Transcription factor ISGF-3 formation requires phosphorylated Stat91 protein, but Stat113 protein is phosphorylated independently of Stat91 protein
    • Improta T, Schindler C, Horvath C, Kerr I, Stark G, Darnell J Jr. Transcription factor ISGF-3 formation requires phosphorylated Stat91 protein, but Stat113 protein is phosphorylated independently of Stat91 protein. Proc Natl Acad Sci U S A. 1994;91:4776-4780.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 4776-4780
    • Improta, T.1    Schindler, C.2    Horvath, C.3    Kerr, I.4    Stark, G.5    Darnell J., Jr.6
  • 41
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signalling proteins
    • Darnell J Jr, Kerr I, Stark G. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signalling proteins. Science. 1994;264:1415-1421.
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell J., Jr.1    Kerr, I.2    Stark, G.3
  • 43
    • 17544381717 scopus 로고    scopus 로고
    • Application of genomic DNA affinity chromatography identifies multiple interferon-a-regulated Stat2 complexes
    • Ghislain J, Fish E. Application of genomic DNA affinity chromatography identifies multiple interferon-a-regulated Stat2 complexes. J Biol Chem. 1996;21:12408-12413.
    • (1996) J Biol Chem , vol.21 , pp. 12408-12413
    • Ghislain, J.1    Fish, E.2
  • 44
    • 0029923456 scopus 로고    scopus 로고
    • Formation of STAT1-STAT2 heterodimers and their role in the activation of IRF-1 gene transcription by interferon-α
    • Li X, Leung S, Qureshi S, Darnell J Jr, Stark G. Formation of STAT1-STAT2 heterodimers and their role in the activation of IRF-1 gene transcription by interferon-α. J Biol Chem. 1996;271:5790-5794.
    • (1996) J Biol Chem , vol.271 , pp. 5790-5794
    • Li, X.1    Leung, S.2    Qureshi, S.3    Darnell J., Jr.4    Stark, G.5
  • 45
    • 0027443228 scopus 로고
    • A nuclear tyrosine phosphatase downregulates interferon-induced gene expression
    • David M, Grimley P, Finbloom D, Lamer A. A nuclear tyrosine phosphatase downregulates interferon-induced gene expression. Mol Cell Biol. 1993;13:7515-7521.
    • (1993) Mol Cell Biol , vol.13 , pp. 7515-7521
    • David, M.1    Grimley, P.2    Finbloom, D.3    Lamer, A.4
  • 46
    • 0027359495 scopus 로고
    • Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice
    • Kozlowski M, Mlinaric R, Feng G, Shen R, Pawson T, Siminovitch K. Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice. J Exp Med. 1993;178:2157-2163.
    • (1993) J Exp Med , vol.178 , pp. 2157-2163
    • Kozlowski, M.1    Mlinaric, R.2    Feng, G.3    Shen, R.4    Pawson, T.5    Siminovitch, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.