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Abstract:
The integrative structural, biochemical, and cell biology data revealed mechanistic
principles of substrate targeting by evolutionarily conserved GID/CTLH E3 ubiquitin
ligases. The pliable substrate receptors adapt their conformations to recognize various
N-terminal peptide/degron sequences, whereas the chelator-like supramolecular
assembly of a catalytically active E3 ligase core configures multi-pronged targeting of
oligomeric substrates. The revealed principles provide a conceptual framework for
understanding the emerging complexity of the GID E3 ligase family.
