The human GID complex engages two independent modules for substrate recruitment

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A new paper by the Peter group of the ETH Zurich's Institute of Biochemistry (IBC) finds that the human GID E3 ubiquitin ligase forms a tetrameric complex with two distinct substrate-recruitment modules, namely WDR26-RanBP9 and GID4-ARMC8a. Although the shorter ARMC8b isoform stably assembles into the hGID complex, it lacks the ability to recruit the GID4 substrate-receptor.

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