An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure.

@article{Fujita2008AnAM,
  title={An Atg4B mutant hampers the lipidation of LC3 paralogues and causes defects in autophagosome closure.},
  author={Naonobu Fujita and Mitsuko Hayashi-Nishino and Hiromi Fukumoto and Hiroko Omori and Akitsugu Yamamoto and Takeshi Noda and Tamotsu Yoshimori},
  journal={Molecular biology of the cell},
  year={2008},
  volume={19 11},
  pages={
          4651-9
        }
}
In the process of autophagy, a ubiquitin-like molecule, LC3/Atg8, is conjugated to phosphatidylethanolamine (PE) and associates with forming autophagosomes. In mammalian cells, the existence of multiple Atg8 homologues (referred to as LC3 paralogues) has hampered genetic analysis of the lipidation of LC3 paralogues. Here, we show that overexpression of an inactive mutant of Atg4B, a protease that processes pro-LC3 paralogues, inhibits autophagic degradation and lipidation of LC3 paralogues… CONTINUE READING
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