4.7 Article

ANKRD13a controls early cell-death checkpoint by interacting with RIP1 independent of NF-κB

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CELL DEATH AND DIFFERENTIATION
卷 29, 期 6, 页码 1152-1163

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SPRINGERNATURE
DOI: 10.1038/s41418-021-00906-9

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  1. National Research Foundation of Korea (NRF) - Korea government (MSIT) [2020R1A2C2005317, 2017R1A5A2015385, 2018R1C1B6005332]
  2. National Research Foundation of Korea [2020R1A2C2005317, 2018R1C1B6005332] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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The study shows that ANKRD13a is a novel component in TNF signaling, influencing the threshold of cell death signals and reducing the risk of cell death. Lack of ANKRD13a promotes the formation of complex-II, shifting cell response from survival to death without affecting NF-κB activation.
In TNF signaling, ubiquitination of RIP1 functions as an early cell-death checkpoint, which prevents the spatial transition of the signaling complex from complex-I to death-inducing complex-II. Here, we report that ankyrin repeat domain 13a (ANKRD13a) acts as a novel component of complex-II to set a higher signal threshold for the cytotoxic potential of TNF. ANKRD13a deficiency is sufficient to turn the response to TNF from survival to death by promoting the formation of complex-II without affecting NF-kappa B activation. ANKRD13a binds to ubiquitinated-RIP1 via its UIM, and subsequently limits the association of FADD and caspase-8 with RIP1. Moreover, high ANKRD13a expression is inversely correlated with apoptotic phenotypes in ovarian cancer tissues and is associated with poor prognosis. Our work identifies ANKRD13a as a novel gatekeeper of the early cell-death checkpoint, which may function as part of an escape mechanism from cell death in some cancers.

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