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Physiological Reviews, Vol. 82, No. 2, April 2002, pp. 373-428; 10.1152/physrev.00027.2001.
Copyright ©2002 by the American Physiological Society
Faculty of Biology and the Institute for Catalysis Science and Technology, and Department of Biochemistry, Bruce Rappaport Faculty of Medicine, Technion-Israel Institute of Technology, Haifa, Israel
Glickman, Michael H. and
Aaron Ciechanover.
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction
for the Sake of Construction. Physiol. Rev. 82: 373-428, 2002.
Between the 1960s and 1980s, most life
scientists focused their attention on studies of nucleic acids and the
translation of the coded information. Protein degradation was a
neglected area, considered to be a nonspecific, dead-end process.
Although it was known that proteins do turn over, the large extent and high specificity of the process, whereby distinct proteins have half-lives that range from a few minutes to several days, was not
appreciated. The discovery of the lysosome by Christian de Duve did not
significantly change this view, because it became clear that this
organelle is involved mostly in the degradation of extracellular
proteins, and their proteases cannot be substrate specific. The
discovery of the complex cascade of the ubiquitin pathway
revolutionized the field. It is clear now that degradation of cellular
proteins is a highly complex, temporally controlled, and tightly
regulated process that plays major roles in a variety of basic pathways
during cell life and death as well as in health and disease. With the
multitude of substrates targeted and the myriad processes involved, it
is not surprising that aberrations in the pathway are implicated in the
pathogenesis of many diseases, certain malignancies, and
neurodegeneration among them. Degradation of a protein via the
ubiquitin/proteasome pathway involves two successive steps:
1) conjugation of multiple ubiquitin moieties to the
substrate and 2) degradation of the tagged protein by the downstream 26S proteasome complex. Despite intensive research, the
unknown still exceeds what we currently know on intracellular protein
degradation, and major key questions have remained unsolved. Among
these are the modes of specific and timed recognition for the
degradation of the many substrates and the mechanisms that underlie
aberrations in the system that lead to pathogenesis of diseases.
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 J. T. Lei and M. Martinez-Moczygemba Separate endocytic pathways regulate IL-5 receptor internalization and signaling J. Leukoc. Biol., August 1, 2008; 84(2): 499 - 509. [Abstract] [Full Text] [PDF]
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E. J. Birks, N. Latif, K. Enesa, T. Folkvang, L. A. Luong, P. Sarathchandra, M. Khan, H. Ovaa, C. M. Terracciano, P. J.R. Barton, et al. Elevated p53 expression is associated with dysregulation of the ubiquitin-proteasome system in dilated cardiomyopathy Cardiovasc Res, August 1, 2008; 79(3): 472 - 480. [Abstract] [Full Text] [PDF]
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A. F. Fernandes, J. Zhou, X. Zhang, Q. Bian, J. Sparrow, A. Taylor, P. Pereira, and F. Shang Oxidative Inactivation of the Proteasome in Retinal Pigment Epithelial Cells: A POTENTIAL LINK BETWEEN OXIDATIVE STRESS AND UP-REGULATION OF INTERLEUKIN-8 J. Biol. Chem., July 25, 2008; 283(30): 20745 - 20753. [Abstract] [Full Text] [PDF]
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N.-Y. Zhang, Z. Tang, and C.-W. Liu {alpha}-Synuclein Protofibrils Inhibit 26 S Proteasome-mediated Protein Degradation: UNDERSTANDING THE CYTOTOXICITY OF PROTEIN PROTOFIBRILS IN NEURODEGENERATIVE DISEASE PATHOGENESIS J. Biol. Chem., July 18, 2008; 283(29): 20288 - 20298. [Abstract] [Full Text] [PDF]
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 B. Sehat, S. Andersson, L. Girnita, and O. Larsson Identification of c-Cbl as a New Ligase for Insulin-like Growth Factor-I Receptor with Distinct Roles from Mdm2 in Receptor Ubiquitination and Endocytosis Cancer Res., July 15, 2008; 68(14): 5669 - 5677. [Abstract] [Full Text] [PDF]
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R. S. Saliba, M. Pangalos, and S. J. Moss The Ubiquitin-like Protein Plic-1 Enhances the Membrane Insertion of GABAA Receptors by Increasing Their Stability within the Endoplasmic Reticulum J. Biol. Chem., July 4, 2008; 283(27): 18538 - 18544. [Abstract] [Full Text] [PDF]
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K. Enesa, K. Ito, L. A. Luong, I. Thorbjornsen, C. Phua, Y. To, J. Dean, D. O. Haskard, J. Boyle, I. Adcock, et al. Hydrogen Peroxide Prolongs Nuclear Localization of NF-{kappa}B in Activated Cells by Suppressing Negative Regulatory Mechanisms J. Biol. Chem., July 4, 2008; 283(27): 18582 - 18590. [Abstract] [Full Text] [PDF]
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M. Kraus, E. Malenke, J. Gogel, H. Muller, T. Ruckrich, H. Overkleeft, H. Ovaa, E. Koscielniak, J. T. Hartmann, and C. Driessen Ritonavir induces endoplasmic reticulum stress and sensitizes sarcoma cells toward bortezomib-induced apoptosis Mol. Cancer Ther., July 1, 2008; 7(7): 1940 - 1948. [Abstract] [Full Text] [PDF]
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 R. Gonzalez-Fernandez, E. Martinez-Galisteo, F. Gaytan, J. A. Barcena, and J. E. Sanchez-Criado Changes in the Proteome of Functional and Regressing Corpus Luteum During Pregnancy and Lactation in the Rat Biol Reprod, July 1, 2008; 79(1): 100 - 114. [Abstract] [Full Text] [PDF]
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G. Gao, J. Zhang, X. Si, J. Wong, C. Cheung, B. McManus, and H. Luo Proteasome inhibition attenuates coxsackievirus-induced myocardial damage in mice Am J Physiol Heart Circ Physiol, July 1, 2008; 295(1): H401 - H408. [Abstract] [Full Text] [PDF]
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S. Bottcher, C. Maresch, H. Granzow, B. G. Klupp, J. P. Teifke, and T. C. Mettenleiter Mutagenesis of the Active-Site Cysteine in the Ubiquitin-Specific Protease Contained in Large Tegument Protein pUL36 of Pseudorabies Virus Impairs Viral Replication In Vitro and Neuroinvasion In Vivo J. Virol., June 15, 2008; 82(12): 6009 - 6016. [Abstract] [Full Text] [PDF]
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Y. Miyauchi, M. Kato, F. Tokunaga, and K. Iwai The COP9/Signalosome Increases the Efficiency of von Hippel-Lindau Protein Ubiquitin Ligase-mediated Hypoxia-inducible Factor-{alpha} Ubiquitination J. Biol. Chem., June 13, 2008; 283(24): 16622 - 16631. [Abstract] [Full Text] [PDF]
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S. Kohlmann, A. Schafer, and D. H. Wolf Ubiquitin Ligase Hul5 Is Required for Fragment-specific Substrate Degradation in Endoplasmic Reticulum-associated Degradation J. Biol. Chem., June 13, 2008; 283(24): 16374 - 16383. [Abstract] [Full Text] [PDF]
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 S. Aoufouchi, A. Faili, C. Zober, O. D'Orlando, S. Weller, J.-C. Weill, and C.-A. Reynaud Proteasomal degradation restricts the nuclear lifespan of AID J. Exp. Med., June 9, 2008; 205(6): 1357 - 1368. [Abstract] [Full Text] [PDF]
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 I. Ferrer, G. Santpere, and F. W. van Leeuwen Argyrophilic grain disease Brain, June 1, 2008; 131(6): 1416 - 1432. [Abstract] [Full Text] [PDF]
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 L. Wang, S. Kumar, B. L. Fridley, K. R. Kalari, I. Moon, L. L. Pelleymounter, M. A.T. Hildebrandt, A. Batzler, B. W. Eckloff, E. D. Wieben, et al. Proteasome {beta} Subunit Pharmacogenomics: Gene Resequencing and Functional Genomics Clin. Cancer Res., June 1, 2008; 14(11): 3503 - 3513. [Abstract] [Full Text] [PDF]
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Y. Zhang, S. Feng, F. Chen, H. Chen, J. Wang, C. McCall, Y. Xiong, and X. W. Deng Arabidopsis DDB1-CUL4 ASSOCIATED FACTOR1 Forms a Nuclear E3 Ubiquitin Ligase with DDB1 and CUL4 That Is Involved in Multiple Plant Developmental Processes PLANT CELL, June 1, 2008; 20(6): 1437 - 1455. [Abstract] [Full Text] [PDF]
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M. M.J. Cohen, G. P. Leboucher, N. Livnat-Levanon, M. H. Glickman, and A. M. Weissman Ubiquitin-Proteasome-dependent Degradation of a Mitofusin, a Critical Regulator of Mitochondrial Fusion Mol. Biol. Cell, June 1, 2008; 19(6): 2457 - 2464. [Abstract] [Full Text] [PDF]
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B. H. Ha, H.-C. Ahn, S. H. Kang, K. Tanaka, C. H. Chung, and E. E. Kim Structural Basis for Ufm1 Processing by UfSP1 J. Biol. Chem., May 23, 2008; 283(21): 14893 - 14900. [Abstract] [Full Text] [PDF]
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K. A. Glenn, R. F. Nelson, H. M. Wen, A. J. Mallinger, and H. L. Paulson Diversity in Tissue Expression, Substrate Binding, and SCF Complex Formation for a Lectin Family of Ubiquitin Ligases J. Biol. Chem., May 9, 2008; 283(19): 12717 - 12729. [Abstract] [Full Text] [PDF]
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O. A. Bazirgan and R. Y. Hampton Cue1p Is an Activator of Ubc7p E2 Activity in Vitro and in Vivo J. Biol. Chem., May 9, 2008; 283(19): 12797 - 12810. [Abstract] [Full Text] [PDF]
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 S. Maezawa, T. Hayano, K. Koiwai, R. Fukushima, K. Kouda, T. Kubota, and O. Koiwai Bood POZ containing gene type 2 is a human counterpart of yeast Btb3p and promotes the degradation of terminal deoxynucleotidyltransferase. Genes Cells, May 1, 2008; 13(5): 439 - 457. [Abstract] [Full Text] [PDF]
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A. O. Manfiolli, A. L. G.C. Maragno, M. M.A. Baqui, S. Yokoo, F. R. Teixeira, E. B. Oliveira, and M. D. Gomes FBXO25-associated Nuclear Domains: A Novel Subnuclear Structure Mol. Biol. Cell, May 1, 2008; 19(5): 1848 - 1861. [Abstract] [Full Text] [PDF]
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P. Rondou, G. Haegeman, P. Vanhoenacker, and K. Van Craenenbroeck BTB Protein KLHL12 Targets the Dopamine D4 Receptor for Ubiquitination by a Cul3-based E3 Ligase J. Biol. Chem., April 25, 2008; 283(17): 11083 - 11096. [Abstract] [Full Text] [PDF]
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 P. M Voorhees, E C. Dees, B. O'Neil, and R. Z Orlowski The Proteasome as a Target for Cancer Therapy Am. Assoc. Cancer Res. Educ. Book, April 12, 2008; 2008(1): 153 - 170. [Abstract] [Full Text] [PDF]
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M. Hayakawa, M. Matsushima, H. Hagiwara, T. Oshima, T. Fujino, K. Ando, K. Kikugawa, H. Tanaka, K. Miyazawa, and M. Kitagawa Novel insights into FGD3, a putative GEF for Cdc42, that undergoes SCF(FWD1/beta-TrCP)-mediated proteasomal degradation analogous to that of its homologue FGD1 but regulates cell morphology and motility differently from FGD1. Genes Cells, April 1, 2008; 13(4): 329 - 342. [Abstract] [Full Text] [PDF]
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 D. M. Lonard and B. W. O'Malley SRC-3 Transcription-Coupled Activation, Degradation, and the Ubiquitin Clock: Is There Enough Coactivator to Go Around in Cells? Sci. Signal., April 1, 2008; 1(13): pe16 - pe16. [Abstract] [Full Text] [PDF]
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 D. E. Goll, G. Neti, S. W. Mares, and V. F. Thompson Myofibrillar protein turnover: The proteasome and the calpains J Anim Sci, April 1, 2008; 86(14_suppl): E19 - E35. [Abstract] [Full Text] [PDF]
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M.-H. Fortier, E. Caron, M.-P. Hardy, G. Voisin, S. Lemieux, C. Perreault, and P. Thibault The MHC class I peptide repertoire is molded by the transcriptome J. Exp. Med., March 17, 2008; 205(3): 595 - 610. [Abstract] [Full Text] [PDF]
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