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Functional complementation between FADD and RIP1 in embryos and lymphocytes

Author

Listed:
  • Haibing Zhang

    (Kimmel Cancer Center, Thomas Jefferson University)

  • Xiaohui Zhou

    (Kimmel Cancer Center, Thomas Jefferson University
    Present address: College of Life Science, Wenzhou Medical College, Zhejiang 325035, China.)

  • Thomas McQuade

    (University of Massachusetts Medical School)

  • Jinghe Li

    (Kimmel Cancer Center, Thomas Jefferson University)

  • Francis Ka-Ming Chan

    (University of Massachusetts Medical School)

  • Jianke Zhang

    (Kimmel Cancer Center, Thomas Jefferson University)

Abstract

Shared function of FADD and RIPK1 Regulation of cell death is vital for embryonic development and homeostasis in somatic cells, and the Fas-associated death domain (FADD) is a critical signalling adaptor for extrinsic apoptotic pathways. In a study of potential interactions between FADD and receptor interacting protein kinase-1 (RIP1/RIPK1), double deficiency of FADD and RIPK1 is shown to rescue the defects in embryonic development and lymphocyte proliferation seen in mice with single gene deficiencies. This suggests that FADD (presumably in conjunction with caspase-8 and c-FLIP) keeps necrosis in check by causing cleavage of RIPK1.

Suggested Citation

  • Haibing Zhang & Xiaohui Zhou & Thomas McQuade & Jinghe Li & Francis Ka-Ming Chan & Jianke Zhang, 2011. "Functional complementation between FADD and RIP1 in embryos and lymphocytes," Nature, Nature, vol. 471(7338), pages 373-376, March.
    • Handle: RePEc:nat:nature:v:471:y:2011:i:7338:d:10.1038_nature09878
    DOI: 10.1038/nature09878
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    Cited by:

    1. Xinyu Mei & Yuan Guo & Zhangdan Xie & Yedan Zhong & Xiaofen Wu & Daichao Xu & Ying Li & Nan Liu & Zheng-Jiang Zhu, 2021. "RIPK1 regulates starvation resistance by modulating aspartate catabolism," Nature Communications, Nature, vol. 12(1), pages 1-16, December.

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