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@ARTICLE{Sachse:868420,
author = {Sachse, Carsten},
title = {{S}tructural basis of p62/{SQSTM}1 helical filaments and
their role in cellular cargo uptake},
journal = {Nature Communications},
volume = {11},
issn = {2041-1723},
address = {[London]},
publisher = {Nature Publishing Group UK},
reportid = {FZJ-2020-00023},
pages = {440},
year = {2020},
abstract = {p62/SQSTM1 is an autophagy receptor and signaling adaptor
with an N-terminal PB1 domain that forms the scaffold of
phase-separated p62 bodies in the cell. The molecular
determinants that govern PB1 domain filament formation in
vitro remain to be determined and the role of p62 filaments
inside the cell is currently unclear. We here determine four
high-resolution cryo-EM structures of different human and
Arabidopsis PB1 domain assemblies and observed a filamentous
ultrastructure of p62/SQSTM1 bodies using correlative
cellular EM. We show that oligomerization or polymerization,
driven by a double arginine finger in the PB1 domain, is a
general requirement for lysosomal targeting of p62.
Furthermore, the filamentous assembly state of p62 is
required for autophagosomal processing of the p62-specific
cargo KEAP1. Our results show that using such mechanisms,
p62 filaments can be critical for cargo uptake in autophagy
and are an integral part of phase-separated p62 bodies.},
cin = {ER-C-3},
ddc = {500},
cid = {I:(DE-Juel1)ER-C-3-20170113},
pnm = {5352 - Understanding the Functionality of Soft Matter and
Biomolecular Systems (POF4-535)},
pid = {G:(DE-HGF)POF4-5352},
typ = {PUB:(DE-HGF)16},
pubmed = {31974402},
UT = {WOS:000558877100009},
doi = {10.1038/s41467-020-14343-8},
url = {https://juser.fz-juelich.de/record/868420},
}