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The C-terminal tail of the RBR E3 ligase RNF14 defines branched K6/K48 polyubiquitin specificity in ribosomal quality control

Molecular Cell · By Sarah J. Trevelyan, Jenny Riedel, Yeh Huei Tong, Hao Dong, Jenny Jiou, Erin N.S. McGowan, Xiangyi S. Wang, Simon A. Cobbold, Rebecca Feltham & Bernhard C. Lechtenberg ·

The Brief

  • Trevelyan et al. report that the E3 ubiquitin ligase RNF14 forms branched K6/K48 polyubiquitin.
  • The study identifies the C-terminal tail of RNF14 as a critical component for its chain-type and branching activity.
  • The work is framed as relevant to ribosomal quality control.

Why it matters

It clarifies how a specific E3 ligase builds a particular branched ubiquitin chain, a step that could matter for understanding how damaged ribosomal translation is handled in cells.

Who’s affected

  • researchers studying ubiquitin signalling and protein quality control
  • structural and molecular biologists working on E3 ligases
  • #ubiquitin
  • #e3 ligase
  • #ribosomal quality control
  • #rnf14
  • #polyubiquitin

Trevelyan et al. report that the E3 ubiquitin ligase RNF14 forms branched K6/K48 polyubiquitin and identify RNF14’s C-terminal tail as a critical component for its chain-type and branching activity. This work opens research avenues for branched K6/K48 ubiquitin in ribosomal…

Timeline

  1. Study published in Molecular Cell

  2. cell.com

    The C-terminal tail of the RBR E3 ligase RNF14 defines branched K6/K48 polyubiquitin specificity in ribosomal quality control

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