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Volumn 8, Issue 3, 1996, Pages 340-347

Control of gene expression by proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MEMBRANE RECEPTOR; PROTEASOME; PROTEIN; PROTEIN P53; PROTEINASE; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; UBIQUITIN;

EID: 0029890442     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80007-X     Document Type: Article
Times cited : (146)

References (70)
  • 1
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter T, Karin M: The regulation of transcription by phosphorylation. Cell 1992, 70:375-378.
    • (1992) Cell , vol.70 , pp. 375-378
    • Hunter, T.1    Karin, M.2
  • 2
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters J-M: Proteasomes: protein degradation machines of the cell. Trends Biochem Sci 1994, 19:377-382.
    • (1994) Trends Biochem Sci , vol.19 , pp. 377-382
    • Peters, J.-M.1
  • 3
    • 0028500556 scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mechanisms of action and cellular physiology
    • Ciechanover A: The ubiquitin-mediated proteolytic pathway: mechanisms of action and cellular physiology. Biol Chem Hoppe Seyler 1994, 375:565-581.
    • (1994) Biol Chem Hoppe Seyler , vol.375 , pp. 565-581
    • Ciechanover, A.1
  • 4
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on the MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL: Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on the MHC class I molecules. Cell 1994, 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 5
    • 0027444947 scopus 로고
    • S. cerevisiae 26S protease mutants arrest cell cycle division in G2/metaphase
    • Ghislain M, Udvardy A, Mann C: S. cerevisiae 26S protease mutants arrest cell cycle division in G2/metaphase. Nature 1993, 366:358-362.
    • (1993) Nature , vol.366 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 6
    • 0142158945 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M, Murray AW, Kirschner MW: Cyclin is degraded by the ubiquitin pathway. Nature 1991, 366:355-357.
    • (1991) Nature , vol.366 , pp. 355-357
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 7
    • 0028967267 scopus 로고
    • Role of ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert W, Futscher B, Jentsch S: Role of ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature 1995, 373:78-81.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futscher, B.2    Jentsch, S.3
  • 8
    • 0029051233 scopus 로고
    • Cyclin ubiquitinilation: The destructive end of mitosis
    • Murray A: Cyclin ubiquitinilation: the destructive end of mitosis. Cell 1995, 81:149-152.
    • (1995) Cell , vol.81 , pp. 149-152
    • Murray, A.1
  • 9
    • 0029071646 scopus 로고
    • Function of the proteasome: The lysis at the end of the tunnel
    • Goldberg AL: Function of the proteasome: the lysis at the end of the tunnel. Science 1995, 268:522-523.
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 10
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser M: Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr Opin Cell Biol 1995, 7:215-223.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 11
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover A: The ubiquitin-proteasome proteolytic pathway. Cell 1994, 79:13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 12
    • 0029060166 scopus 로고
    • Proteasome from Thermoplasma acidophilum: A threonine protease
    • Seemüller E, Lupas A, Stock D, Löwe J, Huber R, Baumeister W: •• Proteasome from Thermoplasma acidophilum: a threonine protease. Science 1995, 268:579-582. Uses site-directed mutagenesis and protease inhibitors to elucidate the proteolytic mechanism of the proteasome.
    • (1995) Science , vol.268 , pp. 579-582
    • Seemüller, E.1    Lupas, A.2    Stock, D.3    Löwe, J.4    Huber, R.5    Baumeister, W.6
  • 13
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Ȧ resolution
    • Löwe J, Stoock D, Jap B, Zwickl P, Baumeister W, Huber R: •• Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Ȧ resolution. Science 1995, 268:533-539. Describes the crystal structure of the Thermoplasma acidophilum proteasome to very high resolution, and uses an inhibitor consisting of a peptide aldehyde to determine the active sites of the proteasome.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stoock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 14
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, •• Schreiber SL: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995, 268:726-731. Very elegant study which defines the X/MB1 subunit of the mammalian proteasome as the target of lactacystin. The metabolite shows remarkable specificity as it interacts with only one subunit, and it blocks the proteasome alone and not five other proteases tested.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 15
    • 0026065338 scopus 로고
    • Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells
    • Ömura S, Fujimoto T, Otoguro K: Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J Antibiot 1991, 44:113-116.
    • (1991) J Antibiot , vol.44 , pp. 113-116
    • Ömura, S.1    Fujimoto, T.2    Otoguro, K.3
  • 16
    • 0028136875 scopus 로고
    • A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces accumulation of ubiquitin protein conjugates in a neuronal cell
    • Figueiredo-Pereira ME, Berg KA, Wilk S: A new inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces accumulation of ubiquitin protein conjugates in a neuronal cell. J Neurochem 1994, 63:1578-1581.
    • (1994) J Neurochem , vol.63 , pp. 1578-1581
    • Figueiredo-Pereira, M.E.1    Berg, K.A.2    Wilk, S.3
  • 17
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky A, Michaud C, Powers JC, Orlowski M: Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 1992, 31:9421-9428.
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 18
    • 0025040233 scopus 로고
    • Suppression of human colorectal carcinoma cell growth by wild-type p53
    • Baker SJ, Markowitz ER, Fearon ER, Willson JKU, Vogelstein B: Suppression of human colorectal carcinoma cell growth by wild-type p53. Science 1990, 249:912-915.
    • (1990) Science , vol.249 , pp. 912-915
    • Baker, S.J.1    Markowitz, E.R.2    Fearon, E.R.3    Jku, W.4    Vogelstein, B.5
  • 20
    • 0024382760 scopus 로고
    • The p53 proto-oncogene can act as a suppressor of transformations
    • Finlay CA, Hinds PW, Levine AJ: The p53 proto-oncogene can act as a suppressor of transformations. Cell 1989, 57:1083-1093.
    • (1989) Cell , vol.57 , pp. 1083-1093
    • Finlay, C.A.1    Hinds, P.W.2    Levine, A.J.3
  • 22
  • 23
    • 0026452949 scopus 로고
    • Defects in a cell cycle checkpoint may be responsible for the genomic instability of cancer cells
    • Hartwell L: Defects in a cell cycle checkpoint may be responsible for the genomic instability of cancer cells. Cell 1992, 71:543-546.
    • (1992) Cell , vol.71 , pp. 543-546
    • Hartwell, L.1
  • 24
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M: Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 1986, 234:364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 25
    • 0028205667 scopus 로고
    • Accumulation of • p53 in a mutant cell line defective in the ubiquitin pathway
    • Chowdary DR, Dermody JJ, Jha KK, Ozer HL: Accumulation of • p53 in a mutant cell line defective In the ubiquitin pathway. Mol Cell Biol 1994, 14:1997-2003. Shows that p53 accumulates at the non-permissive temperature in a cell line carrying a thermolabile E1 enzyme. Introduction of wild-type E1 corrects the defect. Suggests that p53 is degraded via the ubiquitin/proteasome pathway in vivo.
    • (1994) Mol Cell Biol , vol.14 , pp. 1997-2003
    • Chowdary, D.R.1    Dermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 26
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by papillomavirus types 16 and 18 promotes degradation of p53
    • Scheffner M, Werness BA, Huibregtse JM, Levine AJ, Howley PM: The E6 oncoprotein encoded by papillomavirus types 16 and 18 promotes degradation of p53. Cell 1990, 63:1129-1136.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 27
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M, Huibregtse JM, Vierstra RD, Howley PM: The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 1993, 75:495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 28
    • 0028939392 scopus 로고
    • Reconstitution of p53-ubiquitinylation reactions from purified components: The role of human ubiqultin-conjugating enzyme UBC4 and E6-associated protein (E6AP)
    • Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, •• Theodoras A, Pagano M, Draetta G: Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiqultin-conjugating enzyme UBC4 and E6-associated protein (E6AP). Proc Natl Acad Sci USA 1995, 92:3264-3268. Descibes the cloning of a ubiquitin-conjugating (E2) enzyme that specifically ubiquitinylates E6-AP.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3264-3268
    • Rolfe, M.1    Beer-Romero, P.2    Glass, S.3    Eckstein, J.4    Berdo, I.5    Theodoras, A.6    Pagano, M.7    Draetta, G.8
  • 29
    • 0028276554 scopus 로고
    • Degradation of •• the tumor supppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2
    • Ciechanover A, Shkedy D, Oren M, Bercovich B: Degradation of •• the tumor supppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2. J Biol Chem 1994, 269:9582-9589. Reports that the ubiquitin-carrier protein E2-F1 and a novel species of E3 mediate p53 ubiquitinylation in a cell-free system.
    • (1994) J Biol Chem , vol.269 , pp. 9582-9589
    • Ciechanover, A.1    Shkedy, D.2    Oren, M.3    Bercovich, B.4
  • 30
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun •• degradation in vivo is mediated by the 5 domain
    • Treier M, Staszewski LM, Bohmann D: Ubiquitin-dependent c-Jun •• degradation in vivo is mediated by the 5 domain. Cell 1994, 76:787-798. Shows that c-Jun, but not v-Jun, is efficiently ubiquitinylated in vivo. c-Jun proteins with deletions in their δ domains are no longer ubiquitinylated. Transfer of the 6 domain of c-Jun onto β-galactosidase allows the ubiquitinylation and degradation of this heterologous protein.
    • (1994) Cell , vol.76 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 31
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-jun protein by the 26 S proteasome
    • Jariel-Encontre I, Pariat M, Martin F, Carillo S, Salvat C, • Piechaczyk M: Ubiquitinylation is not an absolute requirement for degradation of c-jun protein by the 26 S proteasome. J Biol Chem 1995, 270:11623-11627. Intriguingly, this paper shows that c-Jun does not require ubiquitinylation in order to be degraded in a cell-free degradation assay.
    • (1995) J Biol Chem , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 32
    • 0028174061 scopus 로고
    • Function and activation of NF-κB in the immune system
    • Baeuerle PA, Henkel T: Function and activation of NF-κB in the immune system. Annu Rev Immunol 1994, 12:141-179.
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 33
    • 0027176524 scopus 로고
    • Rapid proteolytic degradation of κB-α is necessary for activation of transcription factor NF-κB
    • Henkel T, Machleidt T, Alkalay I, Ben-Neriah Y, Kröncke M, Baeuerle PA: Rapid proteolytic degradation of κB-α is necessary for activation of transcription factor NF-κB. Nature 1993, 365:182-184.
    • (1993) Nature , vol.365 , pp. 182-184
    • Henkel, T.1    Machleidt, T.2    Alkalay, I.3    Ben-Neriah, Y.4    Kröncke, M.5    Baeuerle, P.A.6
  • 34
    • 0027207242 scopus 로고
    • Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of lκB-α: A mechanism for NF-κB activation
    • Beg AA, Finco TS, Nantermet PV, Baldwin AS Jr: Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of lκB-α: a mechanism for NF-κB activation. Mol Cell Biol 1993, 13:3301-3310.
    • (1993) Mol Cell Biol , vol.13 , pp. 3301-3310
    • Beg, A.A.1    Finco, T.S.2    Nantermet, P.V.3    Baldwin A.S., Jr.4
  • 35
    • 0026066613 scopus 로고
    • Generation of p50 subunit of NF-kappa B by processing of p105 through an ATP-dependent pathway
    • Fan CM, Maniatis T: Generation of p50 subunit of NF-kappa B by processing of p105 through an ATP-dependent pathway. Nature 1991, 354:395-398.
    • (1991) Nature , vol.354 , pp. 395-398
    • Fan, C.M.1    Maniatis, T.2
  • 36
    • 0026509949 scopus 로고
    • NF-kappa B and related proteins: Rel/dorsal homologies meet ankyrin-like repeats
    • Blank V, Kourilsky P, Israel A: NF-kappa B and related proteins: Rel/dorsal homologies meet ankyrin-like repeats. Trends Biochem Sci 1992, 17:135-140.
    • (1992) Trends Biochem Sci , vol.17 , pp. 135-140
    • Blank, V.1    Kourilsky, P.2    Israel, A.3
  • 37
    • 0025266685 scopus 로고
    • Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B
    • Ghosh S, Baltimore D: Activation in vitro of NF-kappa B by phosphorylation of its inhibitor I kappa B. Nature 1990, 344:678-682.
    • (1990) Nature , vol.344 , pp. 678-682
    • Ghosh, S.1    Baltimore, D.2
  • 38
    • 0024355977 scopus 로고
    • In vitro activation and nuclear translocation of NF-kappa B catalyzed by cyclic AMP-dependent protein kinase and protein kinase C
    • Shirakawa F, Mizel SB: In vitro activation and nuclear translocation of NF-kappa B catalyzed by cyclic AMP-dependent protein kinase and protein kinase C. Mol Cell Biol 1989, 9:2424-2430.
    • (1989) Mol Cell Biol , vol.9 , pp. 2424-2430
    • Shirakawa, F.1    Mizel, S.B.2
  • 39
    • 0028985190 scopus 로고
    • Phosphorylation of lκBα precedes but is not sufficient for its dissociation from NF-κB
    • DiDonato D, Mercurio F, Karin M: Phosphorylation of lκBα precedes but is not sufficient for its dissociation from NF-κB. Mol Cell Biol 1995, 15:1302-1311.
    • (1995) Mol Cell Biol , vol.15 , pp. 1302-1311
    • Didonato, D.1    Mercurio, F.2    Karin, M.3
  • 41
    • 0028981050 scopus 로고
    • Activation of NF-κB requires proteolysis of the inhibitor lκB-α: Signal-induced phosphorylation of lκB-α alone does not release active NF-κB
    • Lin Y-C, Brown K, Siebenlist U: Activation of NF-κB requires proteolysis of the inhibitor lκB-α: signal-induced phosphorylation of lκB-α alone does not release active NF-κB. Proc Natl Acad Sci USA 1995, 92:552-556.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 552-556
    • Lin, Y.-C.1    Brown, K.2    Siebenlist, U.3
  • 42
    • 0028172869 scopus 로고
    • Inducible phosphorylation of kBa is not sufficient for its dissociation from NF-κB and is inhibited by protease inhibitors
    • Finco TS, Beg AA, Baldwin ASJ: Inducible phosphorylation of kBa is not sufficient for its dissociation from NF-κB and is inhibited by protease inhibitors. Proc Natl Acad Sci USA 1994, 91:11884-11888.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11884-11888
    • Finco, T.S.1    Beg, A.A.2    Asj, B.3
  • 43
    • 0028557348 scopus 로고
    • Tumor necrosis factor α-induced phosphorylation of lκBα is a signal for its degradation but not dissociation from NF-κB
    • Miyamoto S, Maki M, Schmitt MJ, Hatanaka M, Verma IM: Tumor necrosis factor α-induced phosphorylation of lκBα is a signal for its degradation but not dissociation from NF-κB. Proc Natl Acad Sci USA 1994, 91:12740-12744.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12740-12744
    • Miyamoto, S.1    Maki, M.2    Schmitt, M.J.3    Hatanaka, M.4    Verma, I.M.5
  • 45
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of lκB-α that is still bound to NF-κB
    • ••], this paper provides the first evidence that the proteasome degrades lκBα.
    • (1994) EMBO J , vol.13 , pp. 5433-5441
    • Traenckner, E.B.-M.1    Wilk, S.2    Baeuerle, P.A.3
  • 46
    • 0029010658 scopus 로고
    • The proteasome pathway is required for cytokine-induced endothelial-leukocyte adhesion molecule expression
    • Read MA, Neish AS, Luscinskas FW, Palombella VJ, Maniatis T, Collins T: The proteasome pathway is required for cytokine-induced endothelial-leukocyte adhesion molecule expression. Immunity 1995, 2:493-506.
    • (1995) Immunity , vol.2 , pp. 493-506
    • Read, M.A.1    Neish, A.S.2    Luscinskas, F.W.3    Palombella, V.J.4    Maniatis, T.5    Collins, T.6
  • 47
    • 0028978032 scopus 로고
    • Phosphorylation of human lκB-α on serine 32 and 36 controls lκB-α proteolysis and NF-κB activation in response to diverse stimuli
    • Traenckner EB-M, Pahl HL, Henkel T, Schmidt KN, Wilk S, •• Baeuerle PA: Phosphorylation of human lκB-α on serine 32 and 36 controls lκB-α proteolysis and NF-κB activation in response to diverse stimuli. EMBO J 1995, 14:2876-2883. Maps the sites of phosphorylation of lκB-α to Ser32 and Ser36, and shows that mutant lκB-α proteins behave as dominant-negative proteins, preventing NF-κB activation in response to TNF-α, PMA and okadaic acid. This suggests that various signal transduction pathways converge at the level of lκB phosphorylation in order to mediate NF-κB activation.
    • (1995) EMBO J , vol.14 , pp. 2876-2883
    • Traenckner, E.B.-M.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 48
    • 0028970734 scopus 로고
    • Stimulation-dependent lκBα phosphoralytion marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay I, Yaron A, Hatzubai A, Orian A, Ciechanover A, Ben-•• Neriah Y: Stimulation-dependent lκBα phosphoralytion marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway. Proc Natl Acad Sci USA 1995, 92:10599-10603. Direct evidence for lκB-α ubiquitinylation using methylated ubiquitin. (Methylated ubiquitin interferes with polyubiquitinylation. Mono-ubiquitinylated proteins are bad substrates for degradation, and are hence more stable.) Implicates the E2-F1 ubiquitin-conjugating enzyme in lκB ubiquitinylation.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10599-10603
    • Alkalay, I.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5    Ben-Neriah, Y.6
  • 49
    • 0029442332 scopus 로고
    • Appearance of apparently ubiquitin-conjugated lκB-α during its phosphorylation-induced degradation in intact cells
    • Traenckner EB-M, Baeuerle PA: Appearance of apparently ubiquitin-conjugated lκB-α during its phosphorylation-induced degradation in intact cells. J Cell Sci 1995, Suppl 19:79-84.
    • (1995) J Cell Sci , vol.19 , Issue.SUPPL. , pp. 79-84
    • Traenckner, E.B.-M.1    Baeuerle, P.A.2
  • 50
    • 0028986075 scopus 로고
    • Control of lκB-α proteolysis by site-specific, signal induced phosphorylation
    • Brown K, Gerstberger S, Carlson L, Franzoso G, Siebenlist U: •• Control of lκB-α proteolysis by site-specific, signal induced phosphorylation. Science 1995, 267:1485-1488. Maps the sites of phosphorylation of lκB-α to Ser32 and Ser36 using site-directed mutagenesis. Mutant lκB proteins prevent transactivation of a κB-driven reporter gene by p65.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 51
    • 0028986111 scopus 로고
    • Inducible degradation of lκBα in vitro and in vivo requires the acidic C-terminal domain of the protein
    • Rodriguez MS, Michalpopoulos I, Arenzana-Siesdedos F, Hay RT: Inducible degradation of lκBα in vitro and in vivo requires the acidic C-terminal domain of the protein. Mol Cell Biol 1995, 15:2413-2419.
    • (1995) Mol Cell Biol , vol.15 , pp. 2413-2419
    • Rodriguez, M.S.1    Michalpopoulos, I.2    Arenzana-Siesdedos, F.3    Hay, R.T.4
  • 52
    • 0029091013 scopus 로고
    • Selective inhibition of E-selectin, vascular cell adhesion molecule-1, and intercellular adhesion molecule-1 expression by inhibitors of lκB-α phosphorylation
    • Chen CC, Rosen bloom CL, Anderson DC, Manning AM: Selective inhibition of E-selectin, vascular cell adhesion molecule-1, and intercellular adhesion molecule-1 expression by inhibitors of lκB-α phosphorylation. J Immunol 1995, 151:3538-3545.
    • (1995) J Immunol , vol.151 , pp. 3538-3545
    • Chen, C.C.1    Rosen Bloom, C.L.2    Anderson, D.C.3    Manning, A.M.4
  • 53
    • 0027243576 scopus 로고
    • p105 and p98 precursor proteins play an active role in NF-κB mediated signal transduction
    • Mercurio F, DiDonato JA, Caridad R, Karin M: p105 and p98 precursor proteins play an active role in NF-κB mediated signal transduction. Genes Dev 1993, 7:705-718.
    • (1993) Genes Dev , vol.7 , pp. 705-718
    • Mercurio, F.1    Didonato, J.A.2    Caridad, R.3    Karin, M.4
  • 54
    • 0026742527 scopus 로고
    • The precursor of NF-κB p50 has lκB like functions
    • Rice NR, MacKichan ML, Israël A: The precursor of NF-κB p50 has lκB like functions. Cell 1992, 71:243-253.
    • (1992) Cell , vol.71 , pp. 243-253
    • Rice, N.R.1    MacKichan, M.L.2    Israël, A.3
  • 55
    • 0028804551 scopus 로고
    • Targeted disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses
    • Sha WC, Liou HC, Tuomanen El, Baltimore D: Targeted •• disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses. Cell 1995, 80:321-330. The first report of a p50 knockout mouse. Underscores the importance of p50 in mediating immune responses.
    • (1995) Cell , vol.80 , pp. 321-330
    • Sha, W.C.1    Liou, H.C.2    El, T.3    Baltimore, D.4
  • 56
    • 0028971291 scopus 로고
    • Constitutive NF-κB activation, enhanced granulopoiesis and neonatal lethality in lκB-α deficient mice
    • Beg AA, Sha WC, Bronson RT, Baltimore D: Constitutive NF-κB •• activation, enhanced granulopoiesis and neonatal lethality in lκB-α deficient mice. Genes Dev 1995, 9:2736-2746. Demonstrates the importance of lκB-α in inhibiting NF-κB in lymphoid cells. Implicates aberrant activation of NF-κB in diseases.
    • (1995) Genes Dev , vol.9 , pp. 2736-2746
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Baltimore, D.4
  • 57
    • 0028916254 scopus 로고
    • Cactus protein degradation mediates Drosophila dorsal-ventral signalling
    • Belvin MP, Jin Y, Anderson KV: Cactus protein degradation mediates Drosophila dorsal-ventral signalling. Genes Dev 1995, 9:783-793.
    • (1995) Genes Dev , vol.9 , pp. 783-793
    • Belvin, M.P.1    Jin, Y.2    Anderson, K.V.3
  • 58
    • 0028991691 scopus 로고
    • The role of notch in lateral inhibition and cell fate specification
    • Chitnis AB: The role of notch in lateral inhibition and cell fate specification. Mol Cell Neurosci 1995, 6:311-321.
    • (1995) Mol Cell Neurosci , vol.6 , pp. 311-321
    • Chitnis, A.B.1
  • 60
    • 0027083415 scopus 로고
    • Two mammalian helix-loop-helix factors structurally related to Drosophila hairy and enhancer of split
    • Sasai Y, Kageyama R, Tagawa Y, Shigemoto R, Nakanishi S: Two mammalian helix-loop-helix factors structurally related to Drosophila hairy and enhancer of split Genes Dev 1992, 6:2620-2634.
    • (1992) Genes Dev , vol.6 , pp. 2620-2634
    • Sasai, Y.1    Kageyama, R.2    Tagawa, Y.3    Shigemoto, R.4    Nakanishi, S.5
  • 61
    • 0030003538 scopus 로고    scopus 로고
    • Signal transduction by activated Notch: Importance of proteolytic processing and its regulation by the extracellular domain
    • Kopan R, Schroeter EH, Weintraub H, Nye JS: Signal transduction by activated Notch: importance of proteolytic processing and its regulation by the extracellular domain. Proc Natl Acad Sci USA 1996, 93:1683-1688.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1683-1688
    • Kopan, R.1    Schroeter, E.H.2    Weintraub, H.3    Nye, J.S.4
  • 62
    • 0029085935 scopus 로고
    • Signalling downstream of activated mammalian Notch
    • Jarriault S, Brou C, Logeat F, Schroeter EH, Kopan R, Israël A: •• Signalling downstream of activated mammalian Notch. Nature 1995, 377:355-358. Demonstrates that the cytoplasmic domain of Notch can act as a transcrip-tional activator by interacting with the transcription factor KBF2/RBP-Jκ in the nucleus. Its ankyrin repeats are required for this activity.
    • (1995) Nature , vol.377 , pp. 355-358
    • Jarriault, S.1    Brou, C.2    Logeat, F.3    Schroeter, E.H.4    Kopan, R.5    Israël, A.6
  • 63
    • 0027446955 scopus 로고
    • The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers
    • Bours V, Franzoso G, Azarenko V, Park S, Kanno T, Brown K, Siebenlist U: The oncoprotein Bcl-3 directly transactivates through kappa B motifs via association with DNA-binding p50B homodimers. Cell 1993, 72:729-739.
    • (1993) Cell , vol.72 , pp. 729-739
    • Bours, V.1    Franzoso, G.2    Azarenko, V.3    Park, S.4    Kanno, T.5    Brown, K.6    Siebenlist, U.7
  • 64
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS, Goldstein JL: A receptor-mediated pathway for cholesterol homeostasis. Science 1986, 232:34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 65
    • 0027190308 scopus 로고
    • Nuclear protein that binds sterol regulatory element of LDL receptor promoter. I. Identification of the protein and delineation of its target nucleotide sequence
    • Briggs MR, Yokoyama C, Wang X, Brown MS, Goldstein JL: Nuclear protein that binds sterol regulatory element of LDL receptor promoter. I. Identification of the protein and delineation of its target nucleotide sequence. J Biol Chem 1993, 268:14490-14496.
    • (1993) J Biol Chem , vol.268 , pp. 14490-14496
    • Briggs, M.R.1    Yokoyama, C.2    Wang, X.3    Brown, M.S.4    Goldstein, J.L.5
  • 66
    • 0024203810 scopus 로고
    • Multiple sterol regulatory elements in promoter for hamster 3-hydroxy-3-methylglutaryl coenzyme a synthase
    • Smith JR, Osborne TF, Brown MS, Goldstein JL, Gil G: Multiple sterol regulatory elements In promoter for hamster 3-hydroxy-3-methylglutaryl coenzyme A synthase. J Biol Chem 1988, 263:18480-18487.
    • (1988) J Biol Chem , vol.263 , pp. 18480-18487
    • Smith, J.R.1    Osborne, T.F.2    Brown, M.S.3    Goldstein, J.L.4    Gil, G.5
  • 67
    • 0027167918 scopus 로고
    • Nuclear protein that binds sterol regulatory element of LDL receptor promoter. II. Purification and characterization
    • Wang X, Briggs MR, Hua X, Yokoyama C, Goldstein JL, Brown MS: Nuclear protein that binds sterol regulatory element of LDL receptor promoter. II. Purification and characterization. J Biol Chem 1993, 268:14497-14504.
    • (1993) J Biol Chem , vol.268 , pp. 14497-14504
    • Wang, X.1    Briggs, M.R.2    Hua, X.3    Yokoyama, C.4    Goldstein, J.L.5    Brown, M.S.6
  • 68
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • Wang X, Sato R, Brown MS, Hua X, Goldstein JL: SREBP-1, •• a membrane-bound transcription factor released by sterol-regulated proteolysis. Cell 1994, 77:53-62. Shows that SREBP-1 is synthesized as an ER membrane bound precursor protein which is cleaved upon sterol depletion to release an active transcription factor. The clipping of SREBP and its translocation from the ER membrane to the nucleus constitute a new signal transduction pathway in addition to a novel form of transcription factor activation.
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 69
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the degradation of the yeast MATα2 repressor
    • Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M: Multiple ubiquitin-conjugating enzymes participate in the degradation of the yeast MATα2 repressor. Cell 1993, 74:357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 70
    • 0028170682 scopus 로고
    • Degradation of the yeast MATα2 transcriptional regulator is mediated by the proteasome
    • Richter-Ruoff B, Wolf DH, Hochstrasser M: Degradation of the • yeast MATα2 transcriptional regulator is mediated by the proteasome. FEBS Lett 1994, 354:50-52. Direct evidence that MATα2 is degraded via the proteasome pathway, as it is stable in yeast mutants which are defective in proteasome function.
    • (1994) FEBS Lett , vol.354 , pp. 50-52
    • Richter-Ruoff, B.1    Wolf, D.H.2    Hochstrasser, M.3


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