Defective prelamin A processing promotes unconventional necroptosis driven by nuclear RIPK1-Reference-Cited by-同舟云学术

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Defective prelamin A processing promotes unconventional necroptosis driven by nuclear RIPK1

Published:2024-03-27 Issue:4 Volume:26 Page:567-580
ISSN:1465-7392
Container-title:Nature Cell Biology
language:en
Short-container-title:Nat Cell Biol

Author:

Yang Yuanxin^ORCID,Zhang Jian^ORCID,lv Mingming^ORCID,Cui Na,Shan Bing,Sun Qi,Yan Lingjie,Zhang Mengmeng,Zou Chengyu,Yuan Junying^ORCID,Xu Daichao^ORCID

Publisher

Springer Science and Business Media LLC

Link

https://www.nature.com/articles/s41556-024-01374-2.pdf

Reference84 articles.

1. Barrowman, J. & Michaelis, S. ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders. Biol. Chem. 390, 761–773 (2009).

2. Spear, E. D. et al. ZMPSTE24 missense mutations that cause progeroid diseases decrease prelamin A cleavage activity and/or protein stability. Dis. Model Mech. 11, dmm033670 (2018).

3. Corrigan, D. P. et al. Prelamin A endoproteolytic processing in vitro by recombinant Zmpste24. Biochem. J. 387, 129–138 (2005).

4. Dittmer, T. A. & Misteli, T. The lamin protein family. Genome Biol. 12, 222 (2011).

5. Gruenbaum, Y. & Foisner, R. Lamins: nuclear intermediate filament proteins with fundamental functions in nuclear mechanics and genome regulation. Annu. Rev. Biochem. 84, 131–164 (2015).

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1. RIPK1 and necroptosis role in premature ageing;Nature Cell Biology;2024-03-27

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