4.8 Editorial Material

K29/K48-branched ubiquitin chains TRIP the alarm fueling neo-substrate degradation via the CRL2VHL

Journal

MOLECULAR CELL
Volume 81, Issue 7, Pages 1363-1365

Publisher

CELL PRESS
DOI: 10.1016/j.molcel.2021.02.030

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Funding

  1. Galbraith Family Charitable Trust

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The study demonstrates that the HECT-type E3 ubiquitin ligase TRIP12 cooperates with CRL complexes to promote PROTAC-induced degradation of neo-substrates by generating K29/K48-branched ubiquitin chains.
In this issue of Molecular Cell, Kaiho-Soma et al. (2021) demonstrate that the HECT-type E3 ubiquitin ligase TRIP12 cooperates with CRL complexes to promote PROTAC-induced degradation of neo-substrates by generating K29/K48-branched ubiquitin chains.

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