Proteasome inhibitors: valuable new tools for cell biologists.
Abstract
Proteasomes are major sites for protein degradation in eukaryotic cells. The recent identification of selective proteasome inhibitors has allowed a definition of the roles of the ubiquitin-proteasome pathway in various cellular processes, such as antigen presentation and the degradation of regulatory or membrane proteins. This review describes the actions of these inhibitors, how they can be used to investigate cellular responses, the functions of the proteasome demonstrated by such studies and their potential applications in the future.
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MG-132 protects IκB from proteasomal degradation in inflammatory cells.
“MG-132 is known to protect IκB, which inhibits NFκB, from proteasomal degradation in inflammatory cells.”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Lee and Goldberg, 1998
Cites
Potent and selective inhibitors of the proteasome: Dipeptidyl boronic acids
Adams, J., Behnke, M., Chen, S., Cruickshank, A. A., Dick, L. R., Grenier, L., Klunder, J. M., Ma, Y.-T., Plamondon, L., & Stein, R. L. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00029-8 · Cited by 685 · see citing works
Proteasome Inhibitors Activate Stress Kinases and Induce Hsp72
Meriin, A. B., Gabai, V. L., Yaglom, J., Shifrin, V. I., & Sherman, M. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6373 · Cited by 300 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., Abeliovich, H., Acevedo Arozena, A., Adachi, H., Adams, C. M., Adams, P. D., Adeli, K., et al. (2016) · Autophagy · doi:10.1080/15548627.2015.1100356 · Cited by 5,894 · see citing works
Guidelines for the use and interpretation of assays for monitoring autophagy
Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996 · see citing works
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
Self-citationSuppression of Exosomal PD-L1 Induces Systemic Anti-tumor Immunity and Memory
Poggio, M., Hu, T., Pai, C.-C., Chu, B., Belair, C. D., Chang, A., Montabana, E., Lang, U. E., Fu, Q., Fong, L., et al. (2019) · Cell · doi:10.1016/j.cell.2019.02.016 · Cited by 1,376 · see citing works
Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases
Powers, J. C., Asgian, J. L., Ekici, Ö. D., & James, K. E. (2002) · Chemical Reviews · doi:10.1021/cr010182v · Cited by 1,090 · see citing works
Vogiatzi, T., Xilouri, M., Vekrellis, K., & Stefanis, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801992200 · Cited by 683 · see citing works
Nitric Oxide Impairs Normoxic Degradation of HIF-1α by Inhibition of Prolyl Hydroxylases
Metzen, E., Zhou, J., Jelkmann, W., Fandrey, J., & Brüne, B. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0791 · Cited by 414 · see citing works
Wallace, A. D., & Cidlowski, J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106033200 · Cited by 394 · see citing works
P27kip1 Down-Regulation Is Associated with Trastuzumab Resistance in Breast Cancer Cells
Nahta, R., Takahashi, T., Ueno, N. T., Hung, M.-C., & Esteva, F. J. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3900 · Cited by 298 · see citing works
Douar, A.-M., Poulard, K., Stockholm, D., & Danos, O. (2001) · Journal of Virology · doi:10.1128/jvi.75.4.1824-1833.2001 · Cited by 282 · see citing works
Proteolysis Targeting Chimeras (PROTACs) of Anaplastic Lymphoma Kinase (ALK)
Zhang, C., Han, X.-R., Yang, X., Jiang, B., Liu, J., Xiong, Y., & Jin, J. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.03.071 · Cited by 226 · see citing works
Deroo, B. J., Rentsch, C., Sampath, S., Young, J., DeFranco, D. B., & Archer, T. K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4113-4123.2002 · Cited by 164 · see citing works
Kessler, B. M., Tortorella, D., Altun, M., Kisselev, A. F., Fiebiger, E., Hekking, B. G., Ploegh, H. L., & Overkleeft, H. S. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00069-2 · Cited by 163 · see citing works
Roberts, D., Pedmale, U. V., Morrow, J., Sachdev, S., Lechner, E., Tang, X., Zheng, N., Hannink, M., Genschik, P., & Liscum, E. (2011) · The Plant Cell · doi:10.1105/tpc.111.087999 · Cited by 150 · see citing works
Zhang, Y., Mikhael, M., Xu, D., Li, Y., Soe-Lin, S., Ning, B., Li, W., Nie, G., Zhao, Y., & Ponka, P. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3129 · Cited by 120 · see citing works
Regulation of apoptosis by the ubiquitin and proteasome pathway
Wójcik, C. (2002) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2002.tb00309.x · Cited by 118 · see citing works
Proteasome dysfunction induces muscle growth defects and protein aggregation
Kitajima, Y., Tashiro, Y., Suzuki, N., Warita, H., Kato, M., Tateyama, M., Ando, R., Izumi, R., Yamazaki, M., Abe, M., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.150961 · Cited by 79 · see citing works
“might have favored mice with a dystrophin deficiency (Lee and Goldberg, 1998). This was one of our strong motivations to establish a skeletal muscle-specific deletion of the Rpt3 Fig. 6. Autophagy is reduced in the gastrocnemius muscles of Rpt3 mice. (A) Immunoblotting revealed increased levels of p62, LC3, beclin-1 a…”
BackgroundInfluentialBarette, C., Jariel-Encontre, I., Piechaczyk, M., & Piette, J. (2001) · Oncogene · doi:10.1038/sj.onc.1204129 · Cited by 52 · see citing works
Inhibition of NF-κB by MG132 through ER stress-mediated induction of LAP and LIP
Nakajima, S., Kato, H., Takahashi, S., Johno, H., & Kitamura, M. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.047 · Cited by 46 · see citing works
Mozaffari, M., Hoogeveen-Westerveld, M., Kwiatkowski, D., Sampson, J., Ekong, R., Povey, S., den Dunnen, J. T., van den Ouweland, A., Halley, D., & Nellist, M. (2009) · BMC Medical Genetics · doi:10.1186/1471-2350-10-88 · Cited by 36 · see citing works
Ionizing radiation induces ATM-independent degradation of p21Cip1 in transformed cells
Stuart, S. A., & Wang, J. Y. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808810200 · Cited by 28 · see citing works
Carbajosa, N. A. L., Corradi, G., Verrilli, M. A. L., Guil, M. J., Vatta, M. S., & Gironacci, M. M. (2015) · PLOS ONE · doi:10.1371/journal.pone.0116597 · Cited by 27 · see citing works
“MG-132 is an agent substrate analogues and potent transition-state inhibitor primarily of the chymotrypsin-like activity of the proteasome, reversible and with high cell penetration [20].”
BackgroundPerturbation of ubiquitin homeostasis promotes macrophage oxidative defenses
Charbonneau, M.-E., Passalacqua, K. D., Hagen, S. E., Showalter, H. D., Wobus, C. E., & O’Riordan, M. X. D. (2019) · Scientific Reports · doi:10.1038/s41598-019-46526-9 · Cited by 24 · see citing works
Tsao, D. C., Park, N. J., Nag, A., & Martinson, H. G. (2012) · RNA · doi:10.1261/rna.030452.111 · Cited by 8 · see citing works
Modulation of Lonp1 Activity by Small Compounds
Zanini, G., Micheloni, G., Sinigaglia, G., Selleri, V., Mattioli, A. V., Nasi, M., Pierri, C. L., & Pinti, M. (2025) · Biomolecules · doi:10.3390/biom15040553 · Cited by 7 · see citing works
- Authors
- Lee, D. H., & Goldberg, A. L.
- Affiliations
- Harvard University (US)
- Corresponding author
- Goldberg, Alfred L
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 1998-10
- Volume
- 8
- Issue
- 10
- Pages
- 397-403
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W1973963032
- Cited by
- 1,474
- References
- 2
- Citations by year
- 2026: 31 · 2025: 33 · 2024: 33 · 2023: 37 · 2022: 42 · 2021: 48 · 2020: 37 · 2019: 39 · 2018: 39 · 2017: 34 · 2016: 35 · 2015: 36 · 2014: 56 · 2013: 49 · 2012: 69
- FWCI
- 4.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- proteasome inhibitors, proteasome, ubiquitin-proteasome system, protein degradation, antigen presentation, membrane protein degradation, cellular response
- MeSH terms
- Acetylcysteine, Animals, Boron Compounds, Cysteine Endopeptidases, Depression, Chemical, Heat-Shock Proteins, Humans, Leupeptins, Mammals, Multienzyme Complexes, Oligopeptides, Endopeptidases, Protease Inhibitors, Proteins, Sulfones, Ubiquitins, Yeasts, Antigen Presentation, Proteasome Endopeptidase Complex
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