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UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4 - Nature Structural & Molecular Biology

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UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4 - Nature Structural & Molecular Biology

UBR4 is a 574 kDa E3 ligase (E3) of the N-degron pathway with roles in neurodevelopment, age-associated muscular atrophy and cancer. The catalytic module that carries out ubiquitin (Ub) transfer remains unknown. Here we identify and characterize a distinct E3 module within human UBR4 consisting of a 'hemiRING' zinc finger, a helical-rich UBR zinc-finger interacting (UZI) subdomain, and an N-terminal region that can serve as an affinity factor for the E2 conjugating enzyme (E2).

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UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4 - Nature Structural & Molecular Biology

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UBE2A and UBE2B are recruited by an atypical E3 ligase module in UBR4 - Nature Structural & Molecular Biology

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