The paper:
S. Pankiv et al., “p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy,” J Biol Chem , 282:24131–45, 2007. (Cited in 113 papers)
The finding:
Terje Johansen and his colleagues at the University of Tromsø, Norway, discovered the specific molecule involved in targeting cellular waste for destruction via large double-membrane vesicles called autophagosomes. They found that the protein p62 binds both the ubiquitin-tagged trash and the light chain 3 (LC3) protein on the outside of the autophagosomal membrane. “It was the first paper that showed how directed autophagy might work,” says Vladimir Kirkin of the Johann Wolfgang Goethe University in Frankfurt, Germany.
The bonus:
p62 is also crucial for another process key to cellular cleanup: the clumping together of misfolded proteins before they are engulfed by autophagosomes. Not only does it traffic the aggregate to the right place, “p62 also catalyzes this gluing,” ...
