The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
XIAP as a ubiquitin ligase in cellular signaling
Open accessAbstract
The ability of the vertebrate X-linked inhibitor of apoptosis (XIAP) protein to directly suppress apoptotic cell death pathways has been the subject of much research. Studies of this broadly expressed protein have largely focused on the unique interactions between XIAP and caspases – proteases that conduct and participate in the ordered disassembly of the cell during apoptosis. However, relatively less attention has been given to the RING domain of XIAP, which functions as an E3 ligase to catalyze the ubiquitination of substrate proteins. Here, we discuss the evidence implicating the RING domain of XIAP in the ubiquitin-mediated regulation of three, somewhat arbitrarily divided, categories of substrate: XIAP itself, XIAP-interacting proteins involved in apoptosis, and other targets whose physiological roles likely extend beyond cell death. Collectively, these multiple activities of XIAP show that this enigmatic protein participates in a range of cellular activities beyond apoptotic suppression.
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Cites
Integrating cell-signalling pathways with NF-κB and IKK function
Perkins, N. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2083 · Cited by 2,350
Mechanisms of Thrombus Formation
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Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family
Eckelman, B. P., Salvesen, G. S., & Scott, F. L. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400795 · Cited by 813
Cummins, J. M., Kohli, M., Rago, C., Kinzler, K. W., Vogelstein, B., & Bunz, F. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0046 · Cited by 200
Cited by
Ubiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets
Bedford, L., Lowe, J., Dick, L. R., Mayer, R. J., & Brownell, J. E. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3321 · Cited by 563
The Ubiquitin Ligase XIAP Recruits LUBAC for NOD2 Signaling in Inflammation and Innate Immunity
Damgaard, R. B., Nachbur, U., Yabal, M., Wong, W. W.-L., Fiil, B. K., Kastirr, M., Rieser, E., Rickard, J. A., Bankovacki, A., Peschel, C., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.014 · Cited by 375
Würstle, M. L., Laussmann, M. A., & Rehm, M. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.02.013 · Cited by 269
Apoptosis and aging: increased resistance to apoptosis enhances the aging process
Salminen, A., Ojala, J., & Kaarniranta, K. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0597-y · Cited by 158
PD-L1 and IAPs co-operate to protect tumors from cytotoxic lymphocyte-derived TNF
Kearney, C. J., Lalaoui, N., Freeman, A. J., Ramsbottom, K. M., Silke, J., & Oliaro, J. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.94 · Cited by 83
Metadata
- Authors
- Galbán, S., & Duckett, C. S.
- Venue
- Cell Death & Differentiation
- Published
- 2009-07-10
- Volume
- 17
- Issue
- 1
- Pages
- 54-60
- ISSN
- 1350-9047 (ISSN-L)
- 1476-5403
- OpenAlex
- W1998642504
- Cited by
- 215
- References
- 5
- FWCI
- 6.00
- Type
- journal article
- Language
- en
- Open access
- bronze
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