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: | , , , , , , , , , , , , |
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Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2020
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Subjects: | |
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. |
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