Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation

@article{Scott2016TwoDT,
  title={Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation},
  author={Daniel A. Yaussy Charles T. Scott and David Y Rhee and David M. Duda and Ian R Kelsall and Jennifer L. Olszewski and Joao A. Paulo and Annemieke de Jong and Huib Ovaa and Arno F. Alpi and J Wade Harper and Brenda A. Schulman},
  journal={Cell},
  year={2016},
  volume={166},
  pages={1198-1214.e24}
}
Hundreds of human cullin-RING E3 ligases (CRLs) modify thousands of proteins with ubiquitin (UB) to achieve vast regulation. Current dogma posits that CRLs first catalyze UB transfer from an E2 to their client substrates and subsequent polyubiquitylation from various linkage-specific E2s. We report an alternative E3-E3 tagging cascade: many cellular NEDD8-modified CRLs associate with a mechanistically distinct thioester-forming RBR-type E3, ARIH1, and rely on ARIH1 to directly add the first UB… CONTINUE READING
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