Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake

PB1-mediated oligomerization of p62/SQSTM1 is essential for its function as a selective autophagy receptor. Here the authors present the cryo-EM structures of human and Arabidopsis PB1 domain helical assemblies and find that a conserved double arginine finger in the PB1 domain is important for p62 p...

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Main Authors: Arjen J. Jakobi, Stefan T. Huber, Simon A. Mortensen, Sebastian W. Schultz, Anthimi Palara, Tanja Kuhm, Birendra Kumar Shrestha, Trond Lamark, Wim J. H. Hagen, Matthias Wilmanns, Terje Johansen, Andreas Brech, Carsten Sachse
Format: article
Language:EN
Published: Nature Portfolio 2020
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Online Access:https://doaj.org/article/3681d17d79a54c59a34880abff981baa
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Summary:PB1-mediated oligomerization of p62/SQSTM1 is essential for its function as a selective autophagy receptor. Here the authors present the cryo-EM structures of human and Arabidopsis PB1 domain helical assemblies and find that a conserved double arginine finger in the PB1 domain is important for p62 polymerisation and lysosomal targeting of p62.