Cleavage of sequestosome 1/p62 by an enteroviral protease results in disrupted selective autophagy and impaired NFKB signaling.

@article{Shi2013CleavageOS,
  title={Cleavage of sequestosome 1/p62 by an enteroviral protease results in disrupted selective autophagy and impaired NFKB signaling.},
  author={Junyan Shi and Jerry Wong and Paulina Piesik and Gabriel Fung and Jingchun Zhang and Julienne M. Jagdeo and Xiaotao Li and Eric Jan and Honglin Luo},
  journal={Autophagy},
  year={2013},
  volume={9 10},
  pages={1591-603}
}
The adaptor protein, sequestosome 1 (SQSTM1)/p62, plays an essential role in mediating selective autophagy. It serves as an autophagy receptor targeting ubiquitinated proteins to autophagosomes for degradation. In addition, it functions as a scaffold protein to regulate signaling pathways. Here we explored the interplay between coxsackievirus B3 (CVB3) and SQSTM1-mediated selective autophagy. We reported that SQSTM1 was cleaved at glycine 241 following CVB3 infection through the activity of… CONTINUE READING
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Structural basis for sorting mechanism of p62 in selective autophagy.

The Journal of biological chemistry • 2008
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