The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis
Open accessAbstract
Omi/HtrA2 is a mitochondrial serine protease that is released into the cytosol during apoptosis to antagonize inhibitors of apoptosis (IAPs) and contribute to caspase-independent cell death. Here, we demonstrate that Omi/HtrA2 directly cleaves various IAPs in vitro, and the cleavage efficiency is determined by its IAP-binding motif, AVPS. Cleavage of IAPs such as c-IAP1 substantially reduces its ability to inhibit and ubiquitylate caspases. In contrast to the stoichiometric anti-IAP activity by Smac/DIABLO, Omi/HtrA2 cleavage of c-IAP1 is catalytic and irreversible, thereby more efficiently inactivating IAPs and promoting caspase activity. Elimination of endogenous Omi by RNA interference abolishes c-IAP1 cleavage and desensitizes cells to apoptosis induced by TRAIL. In addition, overexpression of cleavage-site mutant c-IAP1 makes cells more resistant to TRAIL-induced caspase activation. This IAP cleavage by Omi is independent of caspase. Taken together, these results indicate that unlike Smac/DIABLO, Omi/HtrA2's catalytic cleavage of IAPs is a key mechanism for it to irreversibly inactivate IAPs and promote apoptosis.
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Cites
IAP proteins: blocking the road to death's door
Salvesen, G. S., & Duckett, C. S. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm830 · Cited by 1,756
The N-end rule: functions, mysteries, uses
Varshavsky, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12142 · Cited by 859
Cited by
Galluzzi, L., Vitale, I., Abrams, J. M., Alnemri, E. S., Baehrecke, E. H., Blagosklonny, M. V., Dawson, T. M., Dawson, V. L., El-Deiry, W. S., Fulda, S., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.96 · Cited by 2,421
The Role of Mitochondria in Apoptosis
Wang, C., & Youle, R. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102108-134850 · Cited by 1,987
Fundamental Mechanisms of Regulated Cell Death and Implications for Heart Disease
Del Re, D. P., Amgalan, D., Linkermann, A., Liu, Q., & Kitsis, R. N. (2019) · Physiological Reviews · doi:10.1152/physrev.00022.2018 · Cited by 961
Cell Death in the Pathogenesis of Heart Disease: Mechanisms and Significance
Whelan, R. S., Kaplinskiy, V., & Kitsis, R. N. (2010) · Annual Review of Physiology · doi:10.1146/annurev.physiol.010908.163111 · Cited by 759
Mustafa, M., Ahmad, R., Tantry, I. Q., Ahmad, W., Siddiqui, S., Alam, M., Abbas, K., Moinuddin, Hassan, M. I., Habib, S., et al. (2024) · Cells · doi:10.3390/cells13221838 · Cited by 595
Metadata
- Authors
- Yang, Q.-H., Church-Hajduk, R., Ren, J., Newton, M. L., & Du, C.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2003-06-15
- Volume
- 17
- Issue
- 12
- Pages
- 1487-1496
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2110075925
- Cited by
- 335
- References
- 2
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Yang, Q.-H., Church-Hajduk, R., Ren, J., Newton, M. L., & Du, C. (2003). Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis. Genes & Development. https://doi.org/10.1101/gad.1097903
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