The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations
Open accessAbstract
The death-inducing signaling complex (DISC) formed by the death receptor Fas, the adaptor protein FADD and caspase-8 mediates the extrinsic apoptotic program. Mutations in Fas that disrupt the DISC cause autoimmune lymphoproliferative syndrome (ALPS). Here we show that the Fas–FADD death domain (DD) complex forms an asymmetric oligomeric structure composed of 5–7 Fas DD and 5 FADD DD, whose interfaces harbor ALPS-associated mutations. Structure-based mutations disrupt the Fas–FADD interaction in vitro and in living cells; the severity of a mutation correlates with the number of occurrences of a particular interaction in the structure. The highly oligomeric structure explains the requirement for hexameric or membrane-bound FasL in Fas signaling. It also predicts strong dominant negative effects from Fas mutations, which are confirmed by signaling assays. The structure optimally positions the FADD death effector domain (DED) to interact with the caspase-8 DED for caspase recruitment and higher-order aggregation.
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Cites
Helical Assembly in the MyD88-IRAK4-IRAK2 Complex in TLR/IL-1R Signalling
Lin, S.-C., Lo, Y.-C., & Wu, H. (2010) · Nature · doi:10.1038/nature09121 · Cited by 1,111
Self-citationThe Fas Signaling Pathway: More Than a Paradigm
Wajant, H. (2002) · Science · doi:10.1126/science.1071553 · Cited by 957
Interpreting flow cytometry data: a guide for the perplexed
Herzenberg, L. A., Tung, J., Moore, W. A., Herzenberg, L. A., & Parks, D. R. (2006) · Nature Immunology · doi:10.1038/ni0706-681 · Cited by 464
Membrane-bound Fas ligand only is essential for Fas-induced apoptosis
O’ Reilly, L. A., Tai, L., Lee, L., Kruse, E. A., Grabow, S., Fairlie, W. D., Haynes, N. M., Tarlinton, D. M., Zhang, J.-G., Belz, G. T., et al. (2009) · Nature · doi:10.1038/nature08402 · Cited by 400
The Fas–FADD death domain complex structure unravels signalling by receptor clustering
Scott, F. L., Stec, B., Pop, C., Dobaczewska, M. K., Lee, J. J., Monosov, E., Robinson, H., Salvesen, G. S., Schwarzenbacher, R., & Riedl, S. J. (2009) · Nature · doi:10.1038/nature07606 · Cited by 384
Cited by
Li, J., McQuade, T., Siemer, A. B., Napetschnig, J., Moriwaki, K., Hsiao, Y.-S., Damko, E., Moquin, D., Walz, T., McDermott, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.019 · Cited by 1,222
Self-citationFundamental 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
MyD88: a central player in innate immune signaling
Deguine, J., & Barton, G. M. (2014) · F1000Prime Reports · doi:10.12703/p6-97 · Cited by 692
Interferon-induced RIP1/RIP3-mediated necrosis requires PKR and is licensed by FADD and caspases
Thapa, R. J., Nogusa, S., Chen, P., Maki, J. L., Lerro, A., Andrake, M., Rall, G. F., Degterev, A., & Balachandran, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301218110 · Cited by 355
Dickens, L. S., Boyd, R. S., Jukes-Jones, R., Hughes, M. A., Robinson, G. L., Fairall, L., Schwabe, J. W. R., Cain, K., & MacFarlane, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.004 · Cited by 349
Metadata
- Authors
- Wang, L., Yang, J. K., Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Y., Yin, Q., Damko, E., Jang, S. B., Raunser, S., Robinson, C. V., Siegel, R. M., Walz, T., & Wu, H.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-10-10
- Volume
- 17
- Issue
- 11
- Pages
- 1324-1329
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2137615450
- Cited by
- 276
- References
- 5
- FWCI
- 7.92
- Type
- journal article
- Language
- en
- Open access
- green
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- Wang, L., Yang, J. K., Kabaleeswaran, V., Rice, A. J., Cruz, A. C., Park, A. Y., Yin, Q., Damko, E., Jang, S. B., Raunser, S., Robinson, C. V., Siegel, R. M., Walz, T., & Wu, H. (2010). The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1920
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