ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8.

@article{Rasmussen2017ATG4BCA,
  title={ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8.},
  author={Mads Skytte Rasmussen and St{\'e}phane Mouilleron and Birendra Kumar Shrestha and Martina Wirth and Rebecca J. Lee and Kenneth Bowitz Larsen and Yakubu Abudu Princely and Nicola J O'Reilly and Eva Sj\ottem and Sharon A Tooze and Trond Lamark and Terje Johansen},
  journal={Autophagy},
  year={2017},
  volume={13 5},
  pages={834-853}
}
The cysteine protease ATG4B cleaves off one or more C-terminal residues of the inactive proform of proteins of the ortholog and paralog LC3 and GABARAP subfamilies of yeast Atg8 to expose a C-terminal glycine that is conjugated to phosphatidylethanolamine during autophagosome formation. We show that ATG4B contains a C-terminal LC3-interacting region (LIR) motif important for efficient binding to and cleavage of LC3 and GABARAP proteins. We solved the crystal structures of the GABARAPL1-ATG4B C… CONTINUE READING
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