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
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Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/3681d17d79a54c59a34880abff981baa
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spelling oai:doaj.org-article:3681d17d79a54c59a34880abff981baa2021-12-02T15:33:31ZStructural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake10.1038/s41467-020-14343-82041-1723https://doaj.org/article/3681d17d79a54c59a34880abff981baa2020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14343-8https://doaj.org/toc/2041-1723PB1-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.Arjen J. JakobiStefan T. HuberSimon A. MortensenSebastian W. SchultzAnthimi PalaraTanja KuhmBirendra Kumar ShresthaTrond LamarkWim J. H. HagenMatthias WilmannsTerje JohansenAndreas BrechCarsten SachseNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
description 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.
format article
author 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
author_facet 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
author_sort Arjen J. Jakobi
title Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
title_short Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
title_full Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
title_fullStr Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
title_full_unstemmed Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
title_sort structural basis of p62/sqstm1 helical filaments and their role in cellular cargo uptake
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/3681d17d79a54c59a34880abff981baa
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