The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Xk-Related Protein 8 and CED-8 Promote Phosphatidylserine Exposure in Apoptotic Cells
Open accessAbstract
Whence the “Eat Me” Signal?: Cells are surrounded by a lipid bilayer, the composition of which is asymmetrical and serves as a marker of the physiological status of the cell. The phospholipid, phosphatidylserine (PtdSer), is normally found only on the inner leaflet of the membrane, but in dying cells it appears on the cell surface, thus providing the phagocytes tasked with cleaning up such cellular debris with a way to recognize cells undergoing cell death. Such movement of phospholipids within the membrane requires an elusive enzyme known as a scramblase. Suzuki et al. (p. 403 ; published online 11 July) identified an enzyme, Xkr8, which appears to act as a scramblase that promotes exposure of PtdSer on the surface of dying mammalian cells. Consistent with such a role, Xkr8 was activated after cleavage by caspase 3, a key protease that promotes apoptotic cell death. Genetic studies with the homolog of Xkr8 expressed in Caenorhabditis elegans indicated that the protein played a similar role in tagging dead cells in the nematode worm during development.
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Cites
Lethal effect of the anti-Fas antibody in mice
Ogasawara, J., Watanabe-Fukunaga, R., Adachi, M., Matsuzawa, A., Kasugai, T., Kitamura, Y., Itoh, N., Suda, T., & Nagata, S. (1993) · Nature · doi:10.1038/364806a0 · Cited by 1,881
Self-citationIdentification of a factor that links apoptotic cells to phagocytes
Hanayama, R., Tanaka, M., Miwa, K., Shinohara, A., Iwamatsu, A., & Nagata, S. (2002) · Nature · doi:10.1038/417182a · Cited by 1,401
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Cited by
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Self-citationImmunogenic cell stress and death
Kroemer, G., Galassi, C., Zitvogel, L., & Galluzzi, L. (2022) · Nature Immunology · doi:10.1038/s41590-022-01132-2 · Cited by 1,353
Apoptotic cell clearance: basic biology and therapeutic potential
Poon, I. K. H., Lucas, C. D., Rossi, A. G., & Ravichandran, K. S. (2014) · Nature Reviews Immunology · doi:10.1038/nri3607 · Cited by 1,223
Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production
White, M. J., McArthur, K., Metcalf, D., Lane, R. M., Cambier, J. C., Herold, M. J., van Delft, M. F., Bedoui, S., Lessene, G., Ritchie, M. E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.036 · Cited by 983
“, 1998), and PS exposure, which is facilitated by cleavage of Xkr8 (Suzuki et al., 2013), it seems likely that caspase-mediated suppression of IFN-b production (and DAMP signaling generally) is the result of multiple redundant processes.”
Phagocytosis of apoptotic cells in homeostasis
Arandjelovic, S., & Ravichandran, K. S. (2015) · Nature Immunology · doi:10.1038/ni.3253 · Cited by 959
Metadata
- Authors
- Suzuki, J., Denning, D. P., Imanishi, E., Horvitz, H. R., & Nagata, S.
- Venue
- Science
- Published
- 2013-07-26
- Volume
- 341
- Issue
- 6144
- Pages
- 403-406
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2066171290
- Cited by
- 569
- References
- 2
- FWCI
- 18.88
- Type
- journal article
- Language
- en
- Open access
- green
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- Suzuki, J., Denning, D. P., Imanishi, E., Horvitz, H. R., & Nagata, S. (2013). Xk-Related Protein 8 and CED-8 Promote Phosphatidylserine Exposure in Apoptotic Cells. Science. https://doi.org/10.1126/science.1236758
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