Cited by 832Cell death mechanisms and regulationInflammasome and immune disordersUbiquitin and proteasome pathways

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Caspases and their substrates

Open access

Julien, Olivier, Wells, James A·2017·Cell Death & Differentiation

DOI 10.1038/cdd.2017.44PMC PMC5520456

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Abstract

Protease biology is intimately linked to the functional consequences of substrate cleavage events. Human caspases are a family of 12 fate-determining cysteine proteases that are best known for driving cell death, either apoptosis or pyroptosis. More recently, caspases have been shown to be involved in other cellular remodeling events as well including stem cell fate determination, spermatogenesis, and erythroid differentiation. Recent global proteomics methods enable characterization of the substrates that caspases cleave in live cells and cell extracts. The number of substrate targets identified for individual caspases can vary widely ranging from only a (few) dozen targets for caspases-4, -5, -9, and -14 to hundreds of targets for caspases-1, -2, -3, -6, -7, and -8. Proteomic studies characterizing the rates of target cleavage show that each caspase has a preferred substrate cohort that sometimes overlaps between caspases, but whose rates of cleavage vary over 500-fold within each group. Determining the functional consequences of discrete proteolytic events within the global substrate pool is a major challenge for the field. From the handful of individual targets that have been studied in detail, there are only a few so far that whose single cleavage event is capable of sparking apoptosis alone, such as cleavage of caspase-3/-7 and BIM EL, or for pyroptosis, gasdermin D. For the most part, it appears that cleavage events function cooperatively in the cell death process to generate a proteolytic synthetic lethal outcome. In contrast to apoptosis, far less is known about caspase biology in non-apoptotic cellular processes, such as cellular remodeling, including which caspases are activated, the mechanisms of their activation and deactivation, and the key substrate targets. Here we survey the progress made in global identification of caspase substrates using proteomics and the exciting new avenues these studies have opened for understanding the molecular logic of substrate cleavage in apoptotic and non-apoptotic processes.

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Authors: Julien, O., & Wells, J. A.
Affiliations: University of California, San Francisco (US)
Corresponding author: Wells, James A
ORCID: Julien, Olivier
Wells, James A
Venue: Cell Death & Differentiation
Publisher: Springer Science and Business Media LLC
Published: 2017-05-12
Volume: 24
Issue: 8
Pages: 1380-1389
ISSN: 1350-9047 (ISSN-L)
1476-5403
DOI: 10.1038/cdd.2017.44
PMC: PMC5520456
OpenAlex: W2613163105
Cited by: 816
References: 102
Citations by year: 2026: 61 · 2025: 98 · 2024: 108 · 2023: 94 · 2022: 110 · 2021: 117 · 2020: 89 · 2019: 73 · 2018: 47 · 2017: 19
FWCI: 5.79
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Cell Death and Differentiation (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (R01GM081051)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: caspases, caspase substrates, substrate cleavage, apoptosis, pyroptosis, cysteine protease, synthetic lethality, gasdermin D, caspase activation, cellular remodeling, stem cell fate determination, spermatogenesis, erythroid differentiation
MeSH terms: Pyroptosis, Bcl-2-Like Protein 11, Gasdermins, Animals, Cell Differentiation, Eukaryotic Cells, Gene Expression Regulation, Humans, Kinetics, Neoplasm Proteins, Substrate Specificity, Signal Transduction, Caspases, Phosphate-Binding Proteins, Intracellular Signaling Peptides and Proteins, Proteolysis

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