메뉴 건너뛰기




Volumn 84, Issue 6, 1996, Pages 853-862

Site-specific phosphorylation of IκBα by a novel ubiquitination- dependent protein kinase activity

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; UBIQUITIN;

EID: 0030004897     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81064-8     Document Type: Article
Times cited : (894)

References (48)
  • 2
    • 0028970734 scopus 로고
    • Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway
    • I Alkalay A Yaron A Hatzubai A Orian A Ciechanover Y Ben-Neriah Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway Proc. Natl. Acad. Sci. USA 92 1995 10599 10603
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10599-10603
    • Alkalay, I1    Yaron, A2    Hatzubai, A3    Orian, A4    Ciechanover, A5    Ben-Neriah, Y6
  • 3
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • T Arnason M.J Ellison Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain Mol. Cell. Biol. 14 1994 7876 7883
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T1    Ellison, M.J2
  • 5
    • 0028916254 scopus 로고
    • Cactus protein degradation mediates Drosophila dorsal-ventral signaling
    • M.P Belvin Y Jin K.V Anderson Cactus protein degradation mediates Drosophila dorsal-ventral signaling Genes Dev. 9 1995 783 793
    • (1995) Genes Dev. , vol.9 , pp. 783-793
    • Belvin, M.P1    Jin, Y2    Anderson, K.V3
  • 7
    • 0028986075 scopus 로고
    • Control of IκB-α proteolysis by site-specific, signal- induced phosphorylation
    • K Brown S Gerstberger L Carlson G Franzoso U Siebenlist Control of IκB-α proteolysis by site-specific, signal- induced phosphorylation Science 267 1995 1485 1491
    • (1995) Science , vol.267 , pp. 1485-1491
    • Brown, K1    Gerstberger, S2    Carlson, L3    Franzoso, G4    Siebenlist, U5
  • 8
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • V Chau J.W Tobias A Bachmair D Marriott D.J Ecker D.K Gonda A Varshavsky A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein Science 243 1989 1576 1583
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V1    Tobias, J.W2    Bachmair, A3    Marriott, D4    Ecker, D.J5    Gonda, D.K6    Varshavsky, A7
  • 9
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • P Chen P Johnson T Sommer S Jentsch M Hochstrasser Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor Cell 74 1993 357 369
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P1    Johnson, P2    Sommer, T3    Jentsch, S4    Hochstrasser, M5
  • 10
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway
    • Z.J Chen J Hagler V.J Palombella F Melandri D Scherer D Ballard T Maniatis Signal-induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway Genes Dev. 9 1995 1586 1597
    • (1995) Genes Dev. , vol.9 , pp. 1586-1597
    • Chen, Z.J1    Hagler, J2    Palombella, V.J3    Melandri, F4    Scherer, D5    Ballard, D6    Maniatis, T7
  • 11
    • 0028018268 scopus 로고
    • The ubiquitin–proteasome proteolytic pathway
    • A Ciechanover The ubiquitin–proteasome proteolytic pathway Cell 79 1994 13 21
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A1
  • 12
    • 0028985190 scopus 로고
    • Phosphorylation of IκB precedes but is not sufficient for its dissociation from NF-κB
    • J.A DiDonato F Mercurio M Karin Phosphorylation of IκB precedes but is not sufficient for its dissociation from NF-κB Mol. Cell. Biol. 15 1995 1302 1311
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1302-1311
    • DiDonato, J.A1    Mercurio, F2    Karin, M3
  • 13
    • 0028972845 scopus 로고
    • Mechanistic aspects of NF-κB regulation: the emerging role of phosphorylation and proteolysis
    • T.S Finco A.S Baldwin Jr. Mechanistic aspects of NF-κB regulation the emerging role of phosphorylation and proteolysis Immunity 3 1995 263 272
    • (1995) Immunity , vol.3 , pp. 263-272
    • Finco, T.S1    Baldwin, A.S2
  • 14
    • 0028172869 scopus 로고
    • Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited by protease inhibitors
    • T.S Finco A.A Beg A.S Baldwin Jr. Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited by protease inhibitors Proc. Natl. Acad. Sci. USA 91 1994 11884 11888
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11884-11888
    • Finco, T.S1    Beg, A.A2    Baldwin, A.S3
  • 15
    • 0025266685 scopus 로고
    • Activation in vitro of NF-κB by phosphorylation of its inhibitor IκB
    • S Ghosh D Baltimore Activation in vitro of NF-κB by phosphorylation of its inhibitor IκB Nature 344 1990 678 682
    • (1990) Nature , vol.344 , pp. 678-682
    • Ghosh, S1    Baltimore, D2
  • 16
    • 0029071646 scopus 로고
    • Functions of the proteasome: the lysis at the end of the tunnel
    • A.L Goldberg Functions of the proteasome the lysis at the end of the tunnel Science 268 1995 522 523
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L1
  • 17
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates
    • A.L Haas P.M Bright The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates J. Biol. Chem. 250 1985 12464 12473
    • (1985) J. Biol. Chem. , vol.250 , pp. 12464-12473
    • Haas, A.L1    Bright, P.M2
  • 18
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • A.L Haas P.M Bright The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes J. Biol. Chem. 263 1988 13258 13267
    • (1988) J. Biol. Chem. , vol.263 , pp. 13258-13267
    • Haas, A.L1    Bright, P.M2
  • 20
    • 0021813071 scopus 로고
    • Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates
    • A Hershko H Heller Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates Biochem. Biophys. Res. Commun. 128 1985 1079 1086
    • (1985) Biochem. Biophys. Res. Commun. , vol.128 , pp. 1079-1086
    • Hershko, A1    Heller, H2
  • 21
    • 0022975275 scopus 로고
    • The protein substrate binding site of the ubiquitin-protein ligase system
    • A Hershko H Heller E Eytan Y Reiss The protein substrate binding site of the ubiquitin-protein ligase system J. Biol. Chem. 261 1986 11992 11999
    • (1986) J. Biol. Chem. , vol.261 , pp. 11992-11999
    • Hershko, A1    Heller, H2    Eytan, E3    Reiss, Y4
  • 22
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • J.M Huibregtse M Scheffner S Beaudenon P Howley A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase Proc. Natl. Acad. Sci. USA 92 1995 2563 2567
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M1    Scheffner, M2    Beaudenon, S3    Howley, P4
  • 23
    • 0029004815 scopus 로고
    • A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B
    • R.W King J.-M Peters S Tugendreich M Rolfe P Hieter M.W Kirschner A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B Cell 81 1995 279 288
    • (1995) Cell , vol.81 , pp. 279-288
    • King, R.W1    Peters, J.-M2    Tugendreich, S3    Rolfe, M4    Hieter, P5    Kirschner, M.W6
  • 24
    • 0028332026 scopus 로고
    • Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB
    • A Kumar J Haque J Lacoste J Hiscott B Williams Double-stranded RNA-dependent protein kinase activates transcription factor NF-κB by phosphorylating IκB Proc. Natl. Acad. Sci. USA 91 1994 6288 6292
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6288-6292
    • Kumar, A1    Haque, J2    Lacoste, J3    Hiscott, J4    Williams, B5
  • 25
    • 0028822436 scopus 로고
    • Identification of an IκBα-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on IκBα
    • K Kuno Y Ishikawa M.K Ernst M Ogata N.R Rice N Mukaida K Matsushima Identification of an IκBα-associated protein kinase in a human monocytic cell line and determination of its phosphorylation sites on IκBα J. Biol. Chem. 270 1995 27914 27919
    • (1995) J. Biol. Chem. , vol.270 , pp. 27914-27919
    • Kuno, K1    Ishikawa, Y2    Ernst, M.K3    Ogata, M4    Rice, N.R5    Mukaida, N6    Matsushima, K7
  • 26
    • 0027296517 scopus 로고
    • Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation
    • W.-C Lin S Desiderio Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation Science 260 1993 953 959
    • (1993) Science , vol.260 , pp. 953-959
    • Lin, W.-C1    Desiderio, S2
  • 27
    • 0028981050 scopus 로고
    • Activation of NF-κB requires proteolysis of the inhibitor IκB-α: signal-induced phosphorylation of IκB-α alone does not release active NF-κB
    • Y.-C Lin K Brown U Siebenlist Activation of NF-κB requires proteolysis of the inhibitor IκB-α signal-induced phosphorylation of IκB-α alone does not release active NF-κB Proc. Natl. Acad. Sci. USA 92 1995 552 556
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 552-556
    • Lin, Y.-C1    Brown, K2    Siebenlist, U3
  • 28
    • 0027521838 scopus 로고
    • Differential induction of nuclear NF-κB by protein phosphatase inhibitors in primary and transformed human cells
    • S.D Menon S Qin G.R Guy Y.H Tan Differential induction of nuclear NF-κB by protein phosphatase inhibitors in primary and transformed human cells J. Biol. Chem. 268 1993 26805 26812
    • (1993) J. Biol. Chem. , vol.268 , pp. 26805-26812
    • Menon, S.D1    Qin, S2    Guy, G.R3    Tan, Y.H4
  • 29
    • 0028557348 scopus 로고
    • Tumor necrosis factor α-induced phosphorylation of IκBα is a signal for its degradation but not dissociation from NF-κB
    • S Miyamoto M Maki M.J Schmitt M Hatanaka I.M Verma Tumor necrosis factor α-induced phosphorylation of IκBα is a signal for its degradation but not dissociation from NF-κB Proc. Natl. Acad. Sci. USA 91 1994 12740 12744
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12740-12744
    • Miyamoto, S1    Maki, M2    Schmitt, M.J3    Hatanaka, M4    Verma, I.M5
  • 30
  • 33
    • 0027980321 scopus 로고
    • The ubiquitin–proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • V.J Palombella O.J Rando A.L Goldberg T Maniatis The ubiquitin–proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB Cell 78 1994 773 785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J1    Rando, O.J2    Goldberg, A.L3    Maniatis, T4
  • 34
    • 0021996450 scopus 로고
    • Functional heterogeneity of ubiquitin carrier proteins
    • C.M Pickart I.A Rose Functional heterogeneity of ubiquitin carrier proteins J. Biol. Chem. 260 1985 1573 1581
    • (1985) J. Biol. Chem. , vol.260 , pp. 1573-1581
    • Pickart, C.M1    Rose, I.A2
  • 35
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin–protein ligase in the ubiquitination of p53
    • M Scheffner J.M Huibregtse R.D Vierstra P.M Howley The HPV-16 E6 and E6-AP complex functions as a ubiquitin–protein ligase in the ubiquitination of p53 Cell 75 1993 495 505
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M1    Huibregtse, J.M2    Vierstra, R.D3    Howley, P.M4
  • 37
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1
    • R Schreck P Rieber P.A Baeuerle Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1 EMBO J. 10 1991 2247 2258
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R1    Rieber, P2    Baeuerle, P.A3
  • 38
    • 0028114987 scopus 로고
    • The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae
    • SIC1 controls the G1 to S transition in S. cerevisiae Cell 79 1994 233 244
    • (1994) Cell , vol.79 , pp. 233-244
    • Schwob, E1    Böhm, T2    Mendenhall, M.D3    Nasmyth, K4
  • 39
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • W Seufert S Jentsch Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins EMBO J. 9 1990 543 550
    • (1990) EMBO J. , vol.9 , pp. 543-550
    • Seufert, W1    Jentsch, S2
  • 41
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • J Spence S Sadis A.L Haas D Finley A ubiquitin mutant with specific defects in DNA repair and multiubiquitination Mol. Cell. Biol. 15 1995 1265 1273
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J1    Sadis, S2    Haas, A.L3    Finley, D4
  • 42
    • 0029025606 scopus 로고
    • The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis
    • V Sudakin D Ganoth A Dahan H Heller J Hershko F.C Luca J.V Ruderman A Hershko The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis Mol. Biol. Cell 6 1995 185 198
    • (1995) Mol. Biol. Cell , vol.6 , pp. 185-198
    • Sudakin, V1    Ganoth, D2    Dahan, A3    Heller, H4    Hershko, J5    Luca, F.C6    Ruderman, J.V7    Hershko, A8
  • 43
    • 0028986193 scopus 로고
    • NF-κB: a lesson in family values
    • D Thanos T Maniatis NF-κB a lesson in family values Cell 80 1995 529 532
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D1    Maniatis, T2
  • 44
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB
    • E.B.-M Traenckner S Wilk P.A Baeuerle A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB EMBO J. 13 1994 5433 5441
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traenckner, E.B.-M1    Wilk, S2    Baeuerle, P.A3
  • 45
    • 0028978032 scopus 로고
    • Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli
    • E.B.-M Traenckner H.L Pahl T Henkel K.N Schmidt S Wilk P.A Baeuerle Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli EMBO J. 14 1995 2876 2883
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.-M1    Pahl, H.L2    Henkel, T3    Schmidt, K.N4    Wilk, S5    Baeuerle, P.A6
  • 47
    • 0029122799 scopus 로고
    • N- and C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity
    • S.T Whiteside M.K Ernst O LeBail C Laurent-Winter N Rice A Israel N- and C-terminal sequences control degradation of MAD3/IκBα in response to inducers of NF-κB activity Mol. Cell. Biol. 15 1995 5339 5345
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5339-5345
    • Whiteside, S.T1    Ernst, M.K2    LeBail, O3    Laurent-Winter, C4    Rice, N5    Israel, A6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.