32
Views
8
CrossRef citations to date
0
Altmetric
Review

Ubiquitin- and proteasome-dependent pathway of protein degradation as an emerging therapeutic target

Pages 89-111 | Published online: 25 Feb 2005

Bibliography

  • ROCK KL, GRAMM C, ROTHSTEIN L et al.: Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell (1994) 78:761–771.
  • ••Demonstration that the bulk of cell proteins are degraded bythe proteasome pathway and that MHC class I associated peptides are also generated by the proteasomes.
  • LEE DH, TANAKA K, TAMURA T, CHUNG CH, ICHIHARA A: PRS3 encoding an essential subunit of yeast protea-somes homologous to mammalian proteasome subunit C5. Biochem. Biophys. Res. Comm. (1992) 182:452–460.
  • OHBA M: A 70-kDa heat shock cognate protein suppresses the defects caused by a proteasome mutation in Saccharomyces cerevisiae. FEBSLett. (1994) 351:263-266.
  • WOJCIK C: Proteasomes in apoptosis-guardians or villains? Cell. Mol. Life Sci. (1999) (In Press).
  • •Good review on the role of proteasomes in apoptosis.
  • GLAS R, BOGYO M, MCMASTER JS, GACZYNSKA M, PLOEGH HL: A proteolytic system that compensates for loss of proteasome function. Nature (1998) 392:618-622. Report on proteases which can compensate proteasome inhibition.
  • GEIER E, PFEIFER G, WILM M et al.: A giant protease with potential to substitute for some functions of the proteasome. Science (1999) 283:978–981.
  • •Report on proteases which can compensate proteasome inhibition.
  • NEUFELD EF: Lysosomal storage diseases. Ann. Rev. Biochem. (1991) 60:257–280.
  • SCHWARTZ AL, CIECHANOVER A: The ubiquitin-proteasome pathway and pathogenesis of human diseases. Ann. Rev. Med. (1999) 50:57–74.
  • ••Good review on the basic functions of the ubiquitin-andproteasome-dependent proteolytic system and its involve-ment in the pathogenesis of some diseases.
  • ANDRE P, GROETTRUP M, KLENERMAN P et al: An inhibitor of 11IV-1 protease modulates proteasome activity, antigen presentation, and T cell responses. Proc. Natl. Acad. Sci. USA (1998) 95:13120–13124.
  • RAO S, PORTER DC, CHEN X et al: Lovastatin-mediated G1 arrest is through inhibition of the proteasome, independent of hydroxymethyl glutaryl-CoA reductase. Proc. Natl. Acad. Sci. USA (1999) 96:7797–7802.
  • CIECHANOVER A, HOD Y, HERSHKO A: A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem. Biophys. Res. Commun. (1978) 81:1100–1105.
  • •First report on ubiquitin.
  • OZKAYNAK E, FINLEY D, VARSHAVSKY A: The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein. Nature (1984) 312:663–666.
  • HERSHKOA CIECHANOVER A: The ubiquitin system. Ann. Rev. Biochem. (1998) 67:425–479.
  • ••An excellent review of different aspects of the ubiquitinsystem, mainly the ubiquitination cascade enzymes.
  • CIECHANOVER A, BREITSCHOPF K, HATOUM OA, BENGAL E: Degradation of MyoD by the ubiquitin pathway: regulation by specific DNA-binding and identification of a novel site for ubiquitination. Mol Biol. Rep. (1999) 26:59–64.
  • WU RS, KOHN KW, BONNER WM: Metabolism of ubiquitinated histones. J. Biol. Chem. (1 9 8 1) 256:5916-5920.
  • STROUS GJ, GOVERS R: The ubiquitin-proteasome system and endocytosis. j CellSci. (1999) 112:1417–1423.
  • FINLEY D, BARTEL B, VARSHAVSKY A: The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature (1989) 338:394–401.
  • ANDREA AD, PELLMAN D: Deubiquitinating enzymes: a new class of biological regulators. Grit. Rev. Biochem. Mol. Biol. (1998) 33:337–352.
  • WILKINSON KD: Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEBJ (1997) 11:1245–1256.
  • RUBIN DM, FINLEY D: Proteolysis. The proteasome: a protein-degrading organelle? Curr. Biol. (1995) 5:854–858.
  • HENDIL KB: The 19 S multicatalytic `prosome' proteinase is a constitutive enzyme in HeLa cells. Biochem. Intl. (1988) 17:471–477.
  • BOCHTLER M, DITZEL L, GROLL M, HARTMANN C, HUBER R: The proteasome. Ann. Rev. Biophys. Biomol Struct. (1999) 28:295–317.
  • ••An excellent review of the ultrastructure of the proteasome, its associated regulators and related proteases.
  • DEMARTINO GN, SLAUGHTER CA: The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. (1999) 274: 22123–22126.
  • ••A recent, short and complete review of the proteasomesystem.
  • GROLL M, DITZEL L, LOWE J et al.: Structure of 20S proteasome from yeast at 2.4 A resolution. Nature (1997) 386:463–471.
  • ••A great paper describing details of the ultrastructure of theyeast proteasome at a very low resolution.
  • WILK S, ORLOWSKI M: Cation-sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary enzyme. J. Neurochem. (1980) 35:1172–1182.
  • •First report on the proteasome.
  • WILK S, ORLOWSKI M: Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex. J. Neurochem. (1983) 40:842–849.
  • PUHLER G, WEINKAUF S, BACHMANN L et al: Subunit stoichiometry and three-dimensional arrangement in proteasomes from Therm oplasma acidophilum. EMBO (1992) 11:1607–1616.
  • LOWE J, STOCK D, JAP B et al: Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science (1995) 268:533–539.
  • KOPP F, HENDIL KB, DAHLMANN B et al.: Subunit arrangement in the human 20S proteasome. Proc. Natl. Acad. ScL USA (1997) 94:2939–2944.
  • FRUH K, GOSSEN M, WANG K et al.: Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. EMBO J (1994) 13:3236–3244.
  • •One of the first reports showing the importance of the proteasome in the antigen presentation.
  • FRUH K, YANG Y: Antigen presentation by MHC class I and its regulation by interferon gamma. Curr. Opin. Immunol. (1999) 11:76–81.
  • KLOETZEL PM, SOZA A, STOHVVASSER R: The role of the proteasome system and the proteasome activator PA28 complex in the cellular immune response. Biol. Chem. (1999) 380:293–297.
  • ••Good review on the role of the proteasome system in thepresentation of antigens associated with MHC class I molecules.
  • DEMARTINO GN, PROSKE RJ, MOOMAW CR et al.: Identi-fication, purification, and characterization of a PA700-dependent activator of the proteasome. J. Biol. Chem. (1996) 271:3112–3118.
  • GLICKMAN MH, RUBIN DM, FRIED VA, FINLEY D: The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. (1998) 18:3149–3162.
  • GLICKMAN MH, RUBIN DM, COUX O et al.: A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell (1998) 94:615–623.
  • •Characterisation of two different parts of the PA700-the lid and the base.
  • DUBIEL W, PRATT G, FERRELL K, RECHSTEINER M: Purifi-cation of an 11 S regulator of the multicatalytic proteinase. J. Biol. Chem. (1992) 267:22369–22377.
  • MA CP, SLAUGHTER CA, DEMARTINO GN Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain). J. Biol. Chem. (1992) 267:10515–10523.
  • TANAHASHI N, YOKOTA K, AHN JY et al.: Molecular properties of the proteasome activator PA28 family proteins and gamma-interferon regulation. Genes Cells (1997) 2:195–211.
  • ••Great paper discussing different aspects of the PA28regulator.
  • TOJO T, KABURAKI M, HAYAKAWA T et al: Precipitatingantibody to a soluble nuclear antigen `KIC with specificity for systemic lupus erythematosus. Ryumachi (1981) 21 (Suppl.):129–134.
  • CHU-PING M, SLAUGHTER CA, DEMARTINO GN: Purifi-cation and characterization of a protein inhibitor of the 20S proteasome (macropain). Biochim. Biophys. Acta (1992) 1119:303–311.
  • SCHMID HP, AKHAYAT O, MARTINS DE SAC et al.: The prosome: an ubiquitous morphologically distinct RNP particle associated with repressed mRNPs and containing specific ScRNA and a characteristic set of proteins. EMBO J (1984) 3:29–34.
  • SCHERRER K: Prosomes, subcomplexes of untranslated mRNP. Mol. Biol. Rep. (1990) 14:1–9.
  • •A different view of the proteasome: the prosome.
  • ARRIGO AP, TANAKA K, GOLDBERG AL, WELCH WJ: Identity of the 19S `prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature (1988) 331:192–194.
  • PAMNANI V, HAAS B, PUHLER G, SANGER HL, BAUMEISTER W: Proteasome-associated RNAs are non-specific. Eur. J. Biochem. (1994) 225:511–519.
  • PETIT F, JARROUSSE AS, DAHLMANN B et al.: Involve-ment of proteasomal subunits zeta and iota in RNA degradation. Biochem. J. (1997) 326:93–98.
  • PETIT F, JARROUSSE AS, BOISSONNET G et al.: Protea-some (prosome) associated endonuclease activity. Mol. Biol. Rep. (1997) 24:113–117.
  • NOTHWANG HG, COUX O, KEITH G, SILVA-PEREIRA I, SCHERRER K: The major RNA in prosomes of HeLa cells and duck erythroblasts is tRNA(Lys, 3). Nucleic Acids Res. (1992) 20:1959–1965.
  • JARROUSSE AS, PETIT F, KREUTZER-SCHMID C, GAEDIGK R, SCHMID HP: Possible involvement of proteasomes (prosomes) in AUCUA-mediated mRNA decay. J. Biol. Chem. (1999) 274:5925–5930.
  • OMURA S, FUJIMOTO T, OTOGURO K et al.: Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J. AntibioL (1991) 44:113–116.
  • FENTEANY G, STANDAERT RF, LANE WS et al.: Inhibitionof proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science (1995) 268:726–731.
  • SEEMULLER E, LUPAS A, STOCK D et al.: Proteasomefrom Thermoplasma acidophilum: a threonine protease. Science (1995) 268:579–582.
  • ARENDT CS, HOCHSTRASSER M: Identification of theyeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proc. Nati Acad. ScL USA (1997) 94:7156–7161.
  • LEE DH, GOLDBERG AL: Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. (1998) 8:397–403.
  • ••Good review of some proteasome inhibitors.
  • WOJCIK C: Inhibition of the proteasome as a therapeutic approach. Drug Discov. Today (1999) 4:188–192.
  • ••A different review of some proteasome inhibitors and theirpotential use in therapy.
  • ORLOWSKI M: The multicatalytic proteinase complex, a major extralysosomal proteolytic system. Biochem-istry (1990) 29:10289–10297.
  • 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.
  • SPALTENSTEIN A, LEBAN JJ, HUANG JJ et al.: Design and synthesis of novel protease inhibitors. Tripeptide a', 9'-epoxyketones as nanomolar inactivators of the proteasome. Tetrahedron Lett. (1996) 37:1343–1346.
  • IQBAL M, CHATTERJEE S, KAUER JC et al.: Potent inhibi-tors of proteasome. J. Med. Chem. (1995) 38:2276–2277.
  • LUM RT, KERWAR SS, MEYER SM et al.: A new class ofproteasome inhibitors that prevent NFkB activation. Biochem. Pharmacol. (1998) 55:1391–1397.
  • BOGY° M, SHINS, MCMASTER JS, PLOEGH HL: Substratebinding and sequence preference of the proteasome revealed by active-site-directed affinity probes. Chem. Biol. (1998) 5:307–320.
  • ADAMS J, BEHNKE M, CHEN S et al.: Potent and selectiveinhibitors of the proteasome: dipeptidyl boronic acids. Bioorg. Med. Chem. Lett. (1998) 8:333–338.
  • LOIDL G, GROLL M, MUSIOL HJ et al.: Bifunctional inhibitors of the trypsin-like activity of eukaryotic proteasomes. Chem. Biol. (1999) 6:197–204.
  • MENG L, MOHAN R, KWOK BH et al: Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo anti-inflammatory activity. Proc. Natl. Acad. Sci. USA (1999) 96:10403–10408.
  • SIN N, KIM KB, ELOFSSON M et al.: Total synthesis of the potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology. Bioorg. Med. Chem. Lett. (1999) 9:2283–2288.
  • MENG L, KWOK BH, SIN N, CREWS CM: Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. (1999) 59:2798–2801.
  • KROLL M, ARENZANA-SEISDEDOS F, BACHELERIE F et al:The secondary fungal metabolite gliotoxin targets proteolytic activities of the proteasome. Chem. Biol. (1999) 6:689–698.
  • LOIDL G, GROLL M, MUSIOL HJ, HUBER R, MORODER L:Bivalency as a principle for proteasome inhibition. Proc. Natl. Acad. Sci. USA (1999) 96:5418–5422.
  • •Design of novel proteasome inhibitors based on the crystal-lographic structure of the enzyme.
  • ISOE T, NAITO M, SHIRAI A, HIRAI R, TSURUO T: Inhibi-tion of different steps of the ubiquitin system by cisplatin and aclarubicin. Biochim. Biophys. Acta (1992) 1117:131–135.
  • ISOE T, NAITO M, HIRAI R, TSURUO T: Inhibition ofubiquitin-ATP-dependent proteolysis and ubiquitina-tion by cisplatin. AntiCancer Res. (1991) 11:1905–1909.
  • FIGUEIREDO-PEREIRA ME, CHEN WE, LI J, JOHDO 0: Theantitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome. J. Biol. Chem. (1996) 271:16455–16459.
  • KIYOMIYA K, MATSUO S, KUREBE M: Proteasome is a carrier to translocate doxorubicin from cytoplasm into nucleus. Life Sci. (1998) 62:1853–1860.
  • WILK S, CHEN WE: Synthetic peptide-based activators of the proteasome. Mol. Biol. Rep. (1997) 24:119–124.
  • •The only known reports on synthetic activators of the proteasome.
  • WILK S, CHEN WE, MAGNUSSON RP: Modulation of the PA28alpha-205 proteasome interaction by a peptidyl alcohol. Arch. Biochem. Biophys. (1999) 362:283–290.
  • OBIN M, MESCO E, GONG X et al.: Neurite outgrowth in PC12 cells. Distinguishing the roles of ubiquitylation and ubiquitin-dependent proteolysis. J. Biol. Chem. (1999) 274:11789–11795.
  • SONODA H, OMI K, HOJO K et al.: Suppression of oncogenic transformation by hypothemycin associ-ated with accelerated cyclin Di degradation through ubiquitin-proteasome pathway. Life Sci. (1999) 65:381–394.
  • WANG X, OMURA S, SZWEDA LI et al.: Rapamycin inhibits proteasome activator expression and protea-some activity. Eur. j Immunol (1997) 27:2781–2786.
  • VASILEVSKAYA IA, PJ OD: Effects of geldanamycin onsignaling through activator-protein 1 in hypoxic 11T29 human colon adenocarcinoma cells. Cancer Res. (1999) 59:3935–3940.
  • ADAMS J, STEIN R: Novel inhibitors of the proteasomeand their therapeutic use in inflammation. Ann. Rep. Med. Chem. (1996) 31:279–288.
  • PALOMBELLA VJ, RANDO 0J, GOLDBERG AL, MANIATIS T: The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell (1994) 78:773–785.
  • ORIAN A, WHITESIDE S, ISRAEL A et al.: Ubiquitin-mediated processing of NF-kappa B transcriptional activator precursor p105. Reconstitution of a cell-free system and identification of the ubiquitin-carrier protein, E2, and a novel ubiquitin-protein ligase, E3, involved in conjugation. J. Biol. Chem. (1995) 270:21707–21714.
  • UN L, GHOSH S: A glycine-rich region in NF-kappaB p105 functions as a processing signal for the genera-tion of the p50 subunit. Mol. Cell. Biol. (1996) 16:2248–2254.
  • ORIAN A, SCHWARTZ AL, ISRAEL A et al.: Structural motifs involved in ubiquitin-mediated processing of the NF-kappaB precursor p105: roles of the glycine-rich region and a downstream ubiquitination domain. Mol. Cell. Biol. (1999) 19:3664–3673.
  • TRAENCKNER EB, PAHL HL, HENKEL T et al.: Phosphory-lation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli. EMBOJ (1995) 14:2876–2883.
  • TRAENCKNER EB, WILK S, BAEUERLE PA: A proteasomeinhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B. EMBOJ (1994) 13:5433–5441.
  • CONNER EM, BRAND S, DAVIS JM et al.: Proteasomeinhibition attenuates nitric oxide synthase expres-sion, VCAM-1 transcription and the development of chronic colitis. J. Pharm. Exp. Therap. (1997) 282:1615–1622.
  • PALOMBELLA VJ, CONNER EM, FUSELER JW et al.: Role ofthe proteasome and NF-kappaB in streptococcal cell wall-induced polyarthritis. Proc. Natl Acad. Sci. USA (1998) 95:15671–15676.
  • BRAND SJ, MORISE Z, TAGERUD S et al.: Role of theproteasome in rat indomethacin-induced gastropathy [see comments]. Gastroenterology (1999) 116:865–873.
  • ELLIOTT PJ, PIEN CS, MCCORMACK TA, CHAPMAN ID, ADAMS J: Proteasome inhibition: a novel mechanism to combat asthma. J. Allergy Clin. Immunol. (1999) 104:294–300.
  • LUPAS A, ZUHL F, TAMURA T et al.: Eubacterial protea-somes. Molec. Biol. Rep. (1997) 24:125–131.
  • •A nice review on different proteasomes and proteasome-like enzymes in eubacteria.
  • NAGY I, TAMURA T, VANDERLEYDEN J, BAUMEISTER W, DE MOT R: The 20S proteasome of Streptomyces coelicolor. j Bacteriol. (1998) 180:5448–5453.
  • DE MOT R, NAGY I, WALZ J, BAUMEISTER W: Protea-somes and other self-compartmentalizing proteases in prokaryotes. Trends Microbic)]. (1999) 7:88–92.
  • •A recent review on proteasome-like systems in prokaryotes.
  • CHUANG SE, BURLAND V, PLUNKETT GD, DANIELS DL, BLATTNER FR: Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hs1VU operons in Escherichia coli. Gene (1993) 134:1–6.
  • ROHRWILD M, COUX O, HUANG HC et al.: Hs1V-Hs1U: Anovel ATP-dependent protease complex in Escheri-chia coli related to the eukaryotic proteasome. Proc. Natl. Acad. ScL USA (1996) 93:5808–5813.
  • LEVITSKAYA J, SHARIPO A, LEONCHIKS A, CIECHANOVER A, MASUCCI MG: Inhibition of ubiquitin/proteasome-dependent protein degrada-tion by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl. Acad. ScL USA (1997) 94:12616–12621.
  • GILBERT MJ, RIDDELL SR, PLACHTER B, GREENBERG PD: Cytomegalovirus selectively blocks antigen processing and presentation of its immediate-early gene product. Nature (1996) 383:720–722.
  • MILLER DM, SEDMAK DD: Viral effects on antigen processing. Curr. Opin. Immunol. (1999) 11:94–99.
  • SAMANIEGO LA, NEIDERHISER L, DELUCA NA: Persis-tence and expression of the herpes simplex virus genome in the absence of immediate-early proteins. J. Virol. (1998) 72:3307–3320.
  • EVERETT RD: A surprising role for the proteasome inthe regulation of herpesvirus infection. Trends Biochem. Sci. (1999) 24:293–295.
  • EVERETT RD, FREEMONT P, SAITOH H et al.: The disrup-tion of ND10 during herpes simplex virus infection correlates with the Vmw110-and proteasome-dependent loss of several PMI, isoforms. j Virol. (1998) 72:6581–6591.
  • CHELBI-ALIX MK, DE THE H: Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene (1999) 18:935–941.
  • EVERETT RD, ORR A, PRESTON CM: A viral activator of gene expression functions via the ubiquitin-proteasome pathway. EMBO J (1998) 17:7161–7169.
  • ISHOV AM, STENBERG RM, MAUL GG: Human cytomega-lovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J. Cell Biol. (1997) 138:5–16.
  • DOUCAS V, ISHOV AM, ROMO A et al.: Adenovirus replication is coupled with the dynamic properties of the PMI, nuclear structure. Genes Dev. (1996) 10:196–207.
  • EMERMAN M, MALIM MH: HIV-1 regulatory/accessory genes: keys to unraveling viral and host cell biology. Science (1998) 5371:1880–1884.
  • SCHUBERT U, ANTON LC, BACIK I et al.: CD4 glycopro-tein degradation induced by human immunodefi-ciency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. (1998) 3:2280–2288.
  • MARGOTTIN F, BOUR SP, DURAND H et al.: A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell (1998) 4:565–574.
  • DIECKMANN T, WITHERS-WARD ES, JAROSINSKI MA, LIU CF, CHEN IS, FEIGON J: Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr. Nature Struct. Biol (1998) 12:1042–1047.
  • JARROUSSE AS, GAUTIER K, APCHER S et al.: Relation-ships between proteasomes and viral gene products. Mol. Biol. Rep. (1999) 1–2:113–117.
  • NAKAMURA T, TANAKA T, NAGANO T, YONEDA T, TAKAGI H, SATO M: Distribution of mRNA encoding Tat-binding protein-I (TBP-1), a component of 26S proteasome, in the rat brain. Brain Res. Mol. Brain Res. (1998) 1–2:321–327.
  • SEEGER M, FERRELL K, FRANK R, DUBIEL W: 11IV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. J. Biol. Chem. (1997) 13:8145–8148.
  • ROSSI F, EVSTAFIEVA A, PEDRALI-NOY G, GALLINA A, MILANESI. G: HsN3 proteasomal subunit as a target for human immunodeficiency virus type 1 Nef protein. Virology (1997) 1:33–45.
  • SCHWARTZ O, MARECHAL V, FRIGUET B, ARENZANA-SEISDEDOS F, HEARD JM: Antiviral activity of the proteasome on incoming human immunodeficiency virus type 1../. Virol. (1998) 5:3845–3850.
  • TANG G, LEPPLA SH: Proteasome activity is required for anthrax lethal toxin to kill macrophages. Infect. Immun. (1999) 67:3055–3060.
  • MAKSYMOWYCH WP, IKAWA T, YAMAGUCHI A et al.: Invasion by Salmonella typhimurium induces increased expression of the LMP, MECL, and PA28 proteasome genes and changes in the peptide repertoire of HLA-B27. Infect. Immun. (1998) 66:4624–4632.
  • GANTT SM, MYUNG JM, BRIONES MR et al.: Proteasome inhibitors block development of Plasmodium spp. Antimicrob. Agents Chemother. (1998) 42:2731–2738.
  • GONZALEZ J, RAMALHO-PINTO FJ, FREVERT U et al.: Proteasome activity is required for the stage-specific transformation of a protozoan parasite. J. Exp. Med. (1996) 184:1909–1918.
  • MUTOMBA MC, TO WY, HYUN WC, WANG CC: Inhibi-tion of proteasome activity blocks cell cycle progres-sion at specific phase boundaries in African trypanosomes. Molec. Biochem. ParasitoL (1997) 90:491–504.
  • GONZALEZ J, BAT G, FREVERT U, COREY EJ, EICHINGER D: Proteasome-dependent cyst formation and stage-specific ubiquitin mRNA accumulation in Entamoeba invadens. Eur. J. Biochem. (1999) 264:897–904.
  • FEATHERSTONE C: Proteasome inhibitors in develop-ment for malaria [news]. Molec. Med. Today(1997) 3: 367.
  • TAKAOKA M, OKAMOTO H, ITO M et al.: Antihyperten-sive effect of a proteasome inhibitor in DOCA-salt hypertensive rats. Life Sci. (1998) 63:PL65–70.
  • STAUB O, GAUTSCHI I, ISHIKAWA T et al.: Regulation of stability and function of the epithelial Na+ channel (ENaC) by ubiquitination. EMBOJ (1997) 16:6325–6336.
  • LOWE J, BLANCHARD A, MORRELL K et al.: Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease. J. Pathol (1988) 155:9–15.
  • LENNOX G, LOWE J, MORRELL K, LANDON M, MAYER RJ: Ubiquitin is a component of neurofibrillary tangles in a variety of neurodegenerative diseases. Neurosci. Lett. (1988) 94:211–217.
  • KUZUHARA S, MORI H, IZUMIYAMA N, YOSHIMURA M, IHARA Y: Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study. Acta Neuropathol. (1988) 75:345–353.
  • LEIGH PN, ANDERTON BH, DODSON A et al.: Ubiquitin deposits in anterior horn cells in motor neurone disease. Neurosci. Lett. (1988) 93:197–203.
  • SUENAGA T, HIRANO A, LLENA JF et al.: Ubiquitin immunoreactivity in kuru plaques in Creutzfeldt Jakob disease. Ann. Neurol. (1990) 28:174–177.
  • PERRY G, FRIEDMAN R, SHAW G, CHAU V: Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer's disease brains. Proc. Natl. Acad. Sci. USA (1987) 84:3033–3036.
  • COLE GM, TIMIRAS PS: Ubiquitin-protein conjugates in Alzheimer's lesions. Neurosci. Lett. (1987) 79:207–212.
  • MORI H, KONDO J, IHARA Y: Ubiquitin is a component of paired helical filaments in Alzheimer's disease. Science (1987) 235:1641–1644.
  • LOWE J, MAYER RJ, LANDON M: Ubiquitin in neurode-generative diseases. Brain Pathol (1993) 3:55–65.
  • •A review of the reports showing the presence of ubiquitin in different neuropathological findings.
  • II K, ITO H, TANAKA K, HIRANO A: Immunocyto-chemical co-localization of the proteasome in ubiquiti-hated structures in neurodegenerative diseases and the elderly. J. Neuropathol. Exp. Neurol. (1997) 56:125–131.
  • MORANDI A, LOS B, OSOFSKY L, AUTILIO-GAMBETTI L, GAMBETTI P: Ubiquitin and heat shock proteins in cultured nervous tissue after different stress conditions. Prog. Clin. Biol. Res. (1989) 317:819–827.
  • WOJCIK C, SCHROETER D, WILK S, LAMPRECHT J, PAWELETZ N: Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur. J. Cell Biol. (1996) 71:311–318.
  • •First report on 'aggresome' or proteolytic centre.
  • JOHNSTON JA, WARD CL, KOPITO RR: Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. (1998) 143:1883–1898.
  • FIGUEIREDO-PEREIRA ME, COHEN G: The ubiquitin/proteasome pathway: friend or foe in zinc-, cadmium-, and 11202-induced neuronal oxidative stress. Mol. Biol. Rep. (1999) 26:65–69.
  • GARCIA-MATA R, BEBOK Z, SORSCHER EJ, SZTUL ES: Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera. J. Cell Biol. (1999) 146:1239–1254.
  • NOTTERPEK L, RYAN MC, TOBLER AR, SHOOTER EM: PMP22 Accumulation in aggresomes: implications for CMT1A pathology. Neurobiol. Dis. (1999) 6:450–460.
  • MCKEON-O'MALLEY C, SAUNDERS AJ, BUSH Al, TANZI RE: Potential therapeutic targets for Alzheimer's disease. Emerging Therapeutic Targets (1998) 2:157–179.
  • GLENNER GG, WONG CW: Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. (1984) 120:885–890.
  • ISHIURA S, TSUKAHARA T, TABIRA T, SUGITA H: Putative N-terminal splitting enzyme of amyloid A4 peptides is the multicatalytic proteinase, ingensin, which is widely distributed in mammalian cells. FEBS Lett. (1989) 257:388–392.
  • KOJIMA S, OMORI M: Two-way cleavage of beta-amyloid protein precursor by multicatalytic proteinase. FEBS Lett. (1992) 304:57–60.
  • MARAMBAUD P, CHEVALLIER N, BARELLI H, WILK S, CHECLER F: Proteasome contributes to the alpha-secretase pathway of amyloid precursor protein in human cells. J. Neurochem. (1997) 68:698–703.
  • HIGAKI J, QUON D, ZHONG Z, CORDELL B: Inhibition of beta-amyloid formation identifies proteolytic precur-sors and subcellular site of catabolism. Neuron (1995) 14:651–659.
  • ALLSOP D, CHRISTIE G, GRAY C et al.: Studies on inhibi-tion of b-amyloid formation in APP751-transfected IIVIR-32 cells and SPA4CT-transfected SHSY5Y cells. In: Alzheimer's Disease: Biology, Diagnostics and Therapeutics. Iqbal K, Winblad B, Nishimura T, Takeda M, Wisniewski HM (Eds.), John Wiley, New York, USA (1997):717–727.
  • KLAFKI H, ABRAMOWSKI D, SWOBODA R, PAGANETTI PA, STAUFENBIEL M: The carboxyl termini of beta-amyloid peptides 1-40 and 1-42 are generated by distinct gamma-secretase activities. J. Biol. Chem. (1996) 271:28655–28659.
  • KLAFKI HW, PAGANETTI PA, SOMMER B, STAUFENBIEL M: Calpain inhibitor I decreases beta A4 secretion from human embryonal kidney cells expressing beta-amyloid precursor protein carrying the APP670/671 double mutation. Neurosci. Lett. (1995) 201:29–32.
  • CHRISTIE G, MARKWELL RE, GRAY CW et al: Alzheimer's disease: correlation of the suppression of beta-amyloid peptide secretion from cultured cells with inhibition of the chymotrypsin-like activity of the proteasome. j Neurochem. (1999) 73:195–204.
  • •This report show a close relationship between the activity of the proteasome system and 13-amyloid secretion.
  • GREGORI L, FUCHS C, FIGUEIREDO-PEREIRA ME, VAN NOSTRAND WE, GOLDGABER D: Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro. J. Biol. Chem. (1995) 270:19702–19708.
  • ALZHEIMER'S DISEASE COLLABORATIVE GROUP: The structure of the presenilin 1 (S182) gene and identifi-cation of six novel mutations in early onset AD families. Nature Genet. (1995) 11:219–222.
  • LEVY-LAHAD E, WIJSMAN EM, NEMENS E et al: A familial Alzheimer's disease locus on chromosome 1 [see comments]. Science (1995) 269:970–973.
  • STEINER H, CAPELL A, PESOLD B et al.: Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J. Biol. Chem. (1998) 273:32322–32331.
  • HONDA T, YASUTAKE K, NIHONMATSU N et al: Dual roles of proteasome in the metabolism of presenilin 1. Am. J. Physiol (1999) 276:L9–L19.
  • MARAMBAUD P, ANCOLIO K, LOPEZ-PEREZ E, CHECLER F: Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and potentiate A beta 42 recovery from human cells. Molec. Med. (1998) 4:147–157.
  • ADAMS J, PALOMBELLA VJ, SAUSVILLE EA et al.: Protea-some inhibitors: a novel class of potent and effective antitumor agents. Cancer. Res. (1999) 59:2615–2622.
  • •A short but concrete report on antitumour effects of PS-341 proteasome inhibitor, also including toxicological and pharmacological studies.
  • FENTEANY G, SCHREIBER SL: Specific inhibition of the chymotrypsin-like activity of the proteasome induces a bipolar morphology in neuroblastoma cells. Chem. Biol. (1996) 3:905–912.
  • WILK S, CHEN WE, MAGNUSSON RP: Modulators of the activation of the proteasome by PA28 (11S reg). Mol Biol. Rep. (1999) 26:39–44.
  • ATTAIX D, AUROUSSEAU E, COMBARET L et al.: Ubiquitin-proteasome dependent proteolysis in skelet al muscle. Reprod. Nutr. Dev. (1998) 38:153–165.
  • ••An exhausting report on the role of the ubiquitin-andproteasome-dependent proteolytic system in different wasting conditions.
  • FURUNO K, GOODMAN MN, GOLDBERG AL: Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J. Biol. Chem. (1990) 265:8550–8557.
  • MYKLES DL: Lobster muscle proteasome and the degradation of myofibrillar proteins. Enzyme Protein (1993) 47:220–231.
  • EBLE DM, SPRAGIA ML, FERGUSON AG, SAMAREL AM: Sarcomeric myosin heavy chain is degraded by the proteasome. Cell Tissue Res. (1999) 296:541–548.
  • MITCH WE, GOLDBERG AL: Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. New Engl. J. Med. (1996) 335:1897–1905.
  • HASSELGREN PO: Glucocorticoids and muscle catabo-lism. Curr. Opin. Clin. Nutr. Metab. Care (1999) 2:201–205.
  • GRIZARD J, DARDEVET D, BALAGE M et al.: Insulin action on skelet al muscle protein metabolism during catabolic states. Reprod. Nutr. Dev. (1999) 39:61–74.
  • TAWA NE, JR., ODESSEY R, GOLDBERG AL: Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skelet al muscles. J. Clin. Invest. (1997) 100:197–203.
  • LECKER SH, SOLOMON V, MITCH WE, GOLDBERG AL: Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J. Nutr. (1999) 129:243S–246S.
  • COMBARET L, RALLIERE C, TAILLANDIER D, TANAKA K, ATTAIX D: Manipulation of the ubiquitin-proteasome pathway in cachexia: pentoxifylline suppresses the activation of 20S and 26S proteasomes in muscles from tumor-bearing rats. Mol. Biol. Rep. (1999) 26:95–101.
  • LAZARUS DD, DESTREE AT, MAZZOLA LM et al: A new model of cancer cachexia: contribution of the ubiquitin-proteasome pathway. Am. J. Physiol. (1999) 277:E332–E341.
  • HOBLER SC, TIAO G, FISCHER JE, MONACO J, HASSEL-GREN PO: Sepsis-induced increase in muscle proteolysis is blocked by specific proteasome inhibi-tors. Am. J. Physiol. (1998) 274:R30–R37.
  • ATTAIX D, COMBARET L, TILIGNAC T, TAILLANDIER D: Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia. Mol. Biol. Rep. (1999) 26:77–82.
  • COMBARET L, TAILLANDIER D, VOISIN L et al.: No altera-tion in gene expression of components of the ubiquitin-proteasome proteolytic pathway in dystrophin-deficient muscles. FEBS Lett. (1996) 393:292–296.
  • GLOTZER M, MURRAY AW, KIRSCHNER MW: Cyclin is degraded by the ubiquitin pathway. Nature (1991) 349:132–138.
  • •This paper boosted studies of the proteasome system in cancer cells.
  • ROLFE M, CHIU MI, PAGANO M: The ubiquitin-mediated proteolytic pathway as a therapeutic area. J. Molec. Med. (1997) 75:5–17.
  • HERSHKO A: Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. (1997) 9:788–799.
  • ••A good review of the role of the ubiquitin-and proteasome-dependent proteolytic pathway in the cell cycle regulation.
  • ELLEDGE SJ, HARPER JW: The role of protein stability in the cell cycle and cancer. Biochim. Biophys. Acta (1998) 1377:M61–M70.
  • ••A good review of the role of the ubiquitin-and proteasome-dependent proteolytic pathway in cancer.
  • WADA M, KOSAKA M, SAITO S et al.: Serum concentra-tion and localization in tumor cells of proteasomes in patients with hematologic malignancy and their pathophysiologic significance [see comments]. J. Lab. Clin. Med. (1993) 121:215–223.
  • DIETRICH C, BARTSCH T, SCHANZ F, OESCH F, WIESER RJ: p53-dependent cell cycle arrest induced by N-acetyl-L-leucinyl-L-leucinyl-L-norleucinal in platelet-derived growth factor-stimulated human fibroblasts. Proc. Natl. Acad. Sci. USA (1996) 93:10815–10819.
  • WOJCIK C, SCHROETER D, STOEHR M, WILK S, PAWELETZ N An inhibitor of the chymotrypsin-like activity of the multicatalytic proteinase complex (20S proteasome) induces arrest in G2-phase and metaphase in HeLa cells. Eur. J. Cell Biol. (1996) 70:172–178.
  • IMAJOH-OHMI S, KAWAGUCHI T, SUGIYAMA S et al: Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem. Biophys. Res. Comm. (1995) 217:1070–1077.
  • WOJCIK C, STOKLOSA T, GIERMASZ A et al: Apoptosis induced in L1210 leukemia cells by an inhibitor of the chymotryp sin-like activity of the proteasome. Apoptosis (1997) 2:455–462.
  • SADOUL R, FERNANDEZ PA, QUIQUEREZ AL et al.: Involvement of the proteasome in the programmed cell death of NGF-deprived sympathetic neurons. EMBO J (1996) 15:3845–3852.
  • GRIMM LM, GOLDBERG AL, POIRIER GG, SCHWARTZ LM, OSBORNE BA: Proteasomes play an essential role in thymocyte apoptosis. EMBO J (1996) 15:3835–3844.
  • WOJCIK C, MLYNARCZUK I, HOSER G et al.: A combina-tion of retinoic acid and proteasome inhibitors for the treatment of leukemias is potentially dangerous [letter]. Blood (1999) 94:1827–1828.
  • LIN KI, BARABAN JM, RATAN RR: Inhibition versus induction of apoptosis by proteasome inhibitors depends on concentration. Cell Death Differ. (1998) 5:577–583.
  • GRIMM LM, OSBORNE BA: Apoptosis and the protea-some. Results Probl. Cell. Differ. (1999) 23:209–228.
  • •A recent review on the role of the ubiquitin-and proteasome-dependent proteolytic pathway in apoptosis.
  • ORLOWSKI RZ: The role of the ubiquitin-proteasome pathway in apoptosis. Cell Death Differ. (1999) 6:303–313.
  • •A different review of the ubiquitin-and proteasome-dependent proteolytic pathway in apoptosis.
  • DELIC J, MASDEHORS P, OMURA S et al.: The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo-and radioresistant human chronic lympho-cytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis. Br. J. Canc. (1998) 77:1103–1107.
  • OIKAWA T, SASAKI T, NAKAMURA M et al.: The protea-some is involved in angiogenesis. Biochem. Biophys. Res. Commun. (1998) 246:243–248.
  • STOKLOSA T, GOLAB J, WOJCIK C et al.: Antitumor effect of proteasome inhibitor dependent on p53 induction and angiogenesis inhibition. Third Workshop on Protea-somes. (1999) Clermont-Ferrand, France.
  • OIKAWA T, HASEGAWA M, SHIMAMURA M et al.: Eponemycin, a novel antibiotic, is a highly powerful angiogenesis inhibitor. Biochem. Biophys. Res. Commun. (1991) 181:1070–1076.
  • ORLOWSKI RZ, ESWARA JR, LAFOND-WALKER A et al.: Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res. (1998) 58:4342–4348.
  • •First published report on antitumour effects of a proteasome inhibitor in vivo.
  • HANADA M, SUGAWARA K, KANETA K et al.: Epoxomicin, a new antitumor agent of microbial origin. J. Antibiot. (1992) 45:1746–1752.
  • SUGAWARA K, HATORI M, NISHIYAMA Y et al.: Eponemycin, a new antibiotic active against B16 melanoma. I. Production, isolation, structure and biological activity. J. Ant/blot. (1990) 43:8–18.
  • TEICHER BA, ARA G, HERBST R, PALOMBELLA VJ, ADAMS J: The proteasome inhibitor PS-341 in cancer therapy. Clin. Cancer Res. (1999) 5:2638–2645.
  • SPATARO V, NORBURY C, HARRIS AL: The ubiquitin-proteasome pathway in cancer. Br. J. Canc. (1998) 77:448–455.
  • RAY K, HARRIS H: Purification of neutral lens endopep-tidase: close similarity to a neutral proteinase in pituitary. Proc. NatL Acad. ScL USA (1985) 82:7545–7549.
  • TAYLOR A, DAVIES KJ: Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens. Free Radic. Blol. Med. (1987) 3:371–377.
  • MURAKAMI K, JAHNGEN JH, LIN SW, DAVIES KJ, TAYLOR A: Lens proteasome shows enhanced rates of degrada-tion of hydroxyl radical modified alpha-crystallin. Free Radic. Biol. Merl. (1990) 8:217–222.
  • SHANG F, GONG X, PALMER HJ, NOWELL TR, JR., TAYLOR A: Age-related decline in ubiquitin conjugation in response to oxidative stress in the lens. Exp. Eye Res. (1997) 64:21–30.
  • ANDERSSON M, SJOSTRAND J, KARLSSON J: Proteolytic cleavage of N-Succ-Leu-Leu-Val-Tyr-AMC by the protea-some in lens epithelium from clear and cataractous human lenses. Exp. Eye Res. (1998) 67:231–236.
  • WARD CL, OMURA S, KOPITO RR: Degradation of CFTR by the ubiquitin-proteasome pathway. Cell (1995) 83:121–127.
  • •This paper links the ubiquitin-and proteasome-dependent proteolytic pathway to the degradation of ER proteins.
  • XIONG X, CHONG E, SKACH WR: Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane. J. Nutr. (1999) 129:227S–237S.
  • KOPITO RR: Biosynthesis and degradation of CFTR. Physic)]. Rev. (1999) 79:S167–5173.
  • WIGLEY WC, FABUNMI RP, LEE MG et al: Dynamic association of proteasomal machinery with the centrosome. J. Cell Biol. (1999) 145:481–490.
  • SUTCLIFFE JS, JIANG YH, GALIJAARD RJ et al.: The E6-Ap ubiquitin-protein ligase (UBE3A) gene is localized within a narrowed Angelman syndrome critical region [letter]. Genome Res. (1997) 7:368–377.
  • FANG P, LEV-LEHMAN E, TSAI TF et al: The spectrum of mutations in UBE3A causing Angelman syndrome. Hum. Molec. Genet. (1999) 8:129–135.
  • ALBRECHT U, SUTCLIFFE JS, CATTANACH BM et al.: Imprinted expression of the murine Angelman syndrome gene, Ube3a, in hippocampal and Purkinje neurons. Nature Genet. (1997) 17:75–78.
  • ROEST HP, VAN KLAVEREN J, DE WIT J et al.: Inactivation of the HR6B ubiquitin-conjugating DNA repair enzyme in mice causes male sterility associated with chromatin modification. Cell (1996) 86:799-810.4
  • BAARENDS WM, ROEST HP, GROOTEGOED JA: The ubiquitin system in gametogenesis. Mol. Cell Endocrinol. (1999) 151:5–16.
  • PERRY WL, HUSTAD CM, SWING DA et al.: The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a1811 mice [see comments]. Nature Genet. (1998) 18:143–146.
  • ARRIBAS J, LUZ RODRIGUEZ M, ALVAREZ-DO FORNO R, CASTANO JG: Autoantibodies against the multicatalytic proteinase in patients with systemic lupus erythema-tosus. J. Exp. Merl. (1991) 173:423–427.
  • FEIST E, DORNER T, KUCKELKORN U et al: Proteasome alpha-type subunit C9 is a primary target of autoanti-bodies in sera of patients with myositis and systemic lupus erythematosus. J. Exp. Merl. (1996) 184:1313–1318.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.