Regulation of apoptosis by the ubiquitin and proteasome pathway
Open accessAbstract
Regulated proteolysis plays important roles in cell physiology as well as in pathological conditions. In most of the cases, regulated proteolysis is carried out by the ubiquitin‐ and proteasome‐dependent proteolytic system, which is also in charge of the bulk of cytoplasmic proteolysis. However, apoptosis or the process of programmed cell death is regulated by a different proteolytic system, i.e. by caspases, a family of specialized cysteine proteases. Nevertheless, there is plenty of evidence of a crosstalk between the apoptotic pathways and the ubiquitin and proteasome system, whose function in apoptosis appears to be very complex. Proteasome inhibitors induce apoptosis in multiple cell types, while in other they are relatively harmless or even prevent apoptosis induced by other stimuli. Proteasomes degrade specific proteins during apoptosis, but on the other hand some components of the proteasome system are degraded by caspases. The knowledge about the involvement of the ubiquitin‐ and proteasome‐dependent system in apoptosis is already clinically exploited, since proteasome inhibitors are being tested as experimental drugs in the treatment of cancer and other pathological conditions, where manipulation of apoptosis is desirable.
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Proteasome inhibitors induce apoptosis in several cell lines.
“As proteasome inhibitors induce apoptosis in several cell lines [26–28]”
From PSMC5 insufficiency and P320R mutation impair proteasome function (2024) · cites this paper as [28]
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PSMC5 insufficiency and P320R mutation impair proteasome function
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“As proteasome inhibitors induce apoptosis in several cell lines [26–28], we investigated whether apoptosis is induced in PSMC5-knockdown HeLa and SH-SY5Y cells.”
- Authors
- Wójcik, C.
- Affiliations
- Medical University of Warsaw (PL)
- Corresponding author
- Wójcik, Cezary
- ORCID
- Wójcik, Cezary
- Venue
- Journal of Cellular and Molecular Medicine
- Publisher
- Wiley
- Published
- 2002-01
- Volume
- 6
- Issue
- 1
- Pages
- 25-48
- ISSN
- 1582-1838 (ISSN-L)
- 1582-4934
- PMC
- PMC6740140
- OpenAlex
- W1992588869
- Cited by
- 118
- References
- 194
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 5 · 2023: 4 · 2022: 3 · 2021: 1 · 2020: 3 · 2018: 5 · 2017: 5 · 2016: 5 · 2015: 7 · 2014: 4 · 2013: 6 · 2012: 4
- FWCI
- 0.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Cellular and Molecular Medicine (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- apoptosis, ubiquitin-proteasome system, proteasome inhibitors, caspases, regulated proteolysis, programmed cell death, proteasomal degradation, cancer therapy
- MeSH terms
- Animals, Cell Differentiation, Cysteine Endopeptidases, Enzyme Inhibitors, Heat-Shock Proteins, Humans, Models, Biological, Multienzyme Complexes, Neoplasms, Molecular Structure, Apoptosis, Protein Folding, Caspases, Ubiquitin, Proteasome Endopeptidase Complex
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