K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking

Wei Chien Yuan, Yu Ru Lee, Shu Yu Lin, Li Ying Chang, Yen Pei Tan, Chin Chun Hung, Jean Cheng Kuo, Cheng Hsin Liu, Mei Yao Lin, Ming Xu, Zhijian J. Chen, Ruey Hwa Chen

Research output: Contribution to journalArticlepeer-review

109 Scopus citations


Ubiquitin chains are formed as structurally distinct polymers via different linkages, and several chain types including K33-linkage remain uncharacterized. Here, we describe a role for K33-polyubiquitination in protein trafficking. We show that the Cullin 3 (Cul3) substrate adaptor KLHL20 is localized to the trans-Golgi network (TGN) and is important for post-Golgi trafficking by promoting the biogenesis of TGN-derived transport carriers. The Cul3-KLHL20 ubiquitin E3 ligase catalyzes a nondegradable, K33-linked polyubiquitination on coronin 7 (Crn7), which facilitates Crn7 targeting to TGN through a ubiquitin-dependent interaction with Eps15. Blockage of K33-chain formation, Crn7 ubiquitination, or disruption of Crn7-Eps15 interaction impairs TGN-pool F-actin assembly, a process essential for generating transport carriers. Enforced targeting of Crn7 to TGN bypasses the requirement of K33-ubiquitination for TGN-pool F-actin assembly and post-Golgi trafficking. Our study reveals a role of KLHL20-mediated K33-ubiquitination of Crn7 in post-Golgi transport and identifies a cellular recognition mechanism for this ubiquitin chain type.

Original languageEnglish (US)
Pages (from-to)586-600
Number of pages15
JournalMolecular cell
Issue number4
StatePublished - May 22 2014

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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