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TAK1 衔接蛋白 TAB2 和 TAB3 的稳定对于最佳 NF-κB 激活至关重要。

Stabilization of the TAK1 adaptor proteins TAB2 and TAB3 is critical for optimal NF-κB activation.

机构信息

Department of Biomedical Molecular Biology, Ghent University, Belgium.

Unit of Molecular Signal Transduction in Inflammation, VIB-UGent Center for Inflammation Research, VIB, Ghent, Belgium.

出版信息

FEBS J. 2020 Aug;287(15):3161-3164. doi: 10.1111/febs.15210. Epub 2020 Jan 29.

DOI:10.1111/febs.15210

PMID:31997570

Abstract

TAB2 and TAB3 bind to K63-linked polyubiquitin chains and recruit the critical kinase MAP3K7 (TAK1). The polyubiquitin-recruited TAK1/TAB2/TAB3 complex comes in close proximity with the IKK (IKKα/IKKβ/IKKγ) complex, which is recruited to M1-linked polyubiquitin chains via the IKKγ (NEMO) component. Together, the two complexes activate the NF-κB family of transcription factors. NF-κB transcription factors are critical mediators of pro-inflammatory signals and must be tightly regulated at multiple levels. Recently, it was discovered that one such point of regulation occurs at the level of TAB2 and TAB3 protein stability by the deubiquitinase USP15. Comment on: https://doi.org/10.1111/febs.15202.

摘要

TAB2 和 TAB3 与 K63 连接的多泛素链结合，并招募关键激酶 MAP3K7（TAK1）。多泛素募集的 TAK1/TAB2/TAB3 复合物与 IKK（IKKα/IKKβ/IKKγ）复合物接近，后者通过 IKKγ（NEMO）组件被招募到 M1 连接的多泛素链上。这两个复合物共同激活 NF-κB 转录因子家族。NF-κB 转录因子是促炎信号的关键介质，必须在多个水平上进行严格调控。最近发现，这种调节之一发生在去泛素酶 USP15 对 TAB2 和 TAB3 蛋白稳定性的水平上。评论见：https://doi.org/10.1111/febs.15202。