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

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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Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Science
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Acceso en línea:https://doaj.org/article/3681d17d79a54c59a34880abff981baa
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Sumario: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.

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