Phosphorylation tunes p62 condensates to drive autophagic degradation of ubiquitinated proteins.
Overview
- Department of Physiology, Juntendo University Graduate School of Medicine, Tokyo, Japan
- Department of Cell Biology and Neuroscience, Juntendo University Graduate School of Medicine, Tokyo, Japan
- Laboratory of Morphology and Image Analysis, Biomedical Research Core Facilities, Juntendo University Graduate School of Medicine, Tokyo, Japan
- Autophagy Research Center, Juntendo University Graduate School of Medicine, Tokyo, Japan
- Frontier Research Center for Advanced Material and Life Science, Graduate School of Life Science and Faculty of Advanced Life Science, Hokkaido University, Sapporo, Japan
- Graduate School of Nanobioscience, Yokohama City University, Yokohama, Japan
- Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan
- Department of Life Science Frontiers Center for iPS Cell Research and Application (CiRA), Kyoto University, Kyoto, Japan
- Graduate School of Engineering, Department of Chemical Engineering, Kyoto University, Kyoto, Japan
- Department of Animal Model Development, Brain Research Institute, Niigata University, Niigata, Japan
- Department of Molecular Cell Biology, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan
Abstract
p62/
Reproduced under the paper's license (CC BY), from the paper cited above.
Code
The paper links to its data, not to its authors' code: see the Data section.
Tracing map
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Data
Data links
- ebi.ac.uk/
biostudies/ , EMBL-EBI; found in the text, “Author contributions”sourcedata
Data availability
The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD074538 (https://
The source data of this paper are collected in the following database record: biostudies:S-SCDT-10_103
Reproduced under the paper's license (CC BY), from the paper cited above.
Versions
The history of this record: each version stored by the harvester or made by a correction of its authors or of the maintainers of its code, and what changed in its facts. The texts of the paper (its abstract, its availability statements) are not part of it; versions that changed only those are not listed.
Version 1, 28 September 2026: the first record
Recorded: type, language, journal, volume, issue, pages, dates, 19 authors, 2 keywords, 9 MeSH terms, 7 funders, 61 references, 37 RRIDs.
Cite
This paper
Komatsu-Hirota, S., Tabata, K., Sou, Y.-s., Kakuta, S., Sakamaki, J.-i., Tsuchiya, H., Li, J., Kumeta, H., Sakai, Y., Fujioka, Y., Noshiro, D., Shimobayashi, S. F., Kurimura, T., Taniguchi, T., Abe, M., Koike, M., Morishita, H., Noda, N. N., & Komatsu, M. (2026). Phosphorylation tunes p62 condensates to drive autophagic degradation of ubiquitinated proteins. The EMBO journal, 45(12), 4061-4093. https://
BibTeX
@article{komatsuhirota20
author = {Komatsu-Hirota, Satoko and Tabata, Keisuke and Sou, Yu-shin and Kakuta, Soichiro and Sakamaki, Jun-ichi and Tsuchiya, Hikaru and Li, Jiachen and Kumeta, Hiroyuki and Sakai, Yuji and Fujioka, Yuko and Noshiro, Daisuke and Shimobayashi, Shunsuke F and Kurimura, Tomo and Taniguchi, Takashi and Abe, Manabu and Koike, Masato and Morishita, Hideaki and Noda, Nobuo N and Komatsu, Masaaki},
title = {{Phosphorylation tunes p62 condensates to drive autophagic degradation of ubiquitinated proteins}},
journal = {The EMBO journal},
year = {2026},
month = may,
volume = {45},
number = {12},
pages = {4061--4093},
publisher = {Nature Publishing Group},
issn = {0261-4189},
doi = {10.1038/
url = {https://
pmid = {42086857},
pmcid = {PMC13270050}
}
RIS
TY - JOUR
AU - Komatsu-Hirota, Satoko
AU - Tabata, Keisuke
AU - Sou, Yu-shin
AU - Kakuta, Soichiro
AU - Sakamaki, Jun-ichi
AU - Tsuchiya, Hikaru
AU - Li, Jiachen
AU - Kumeta, Hiroyuki
AU - Sakai, Yuji
AU - Fujioka, Yuko
AU - Noshiro, Daisuke
AU - Shimobayashi, Shunsuke F
AU - Kurimura, Tomo
AU - Taniguchi, Takashi
AU - Abe, Manabu
AU - Koike, Masato
AU - Morishita, Hideaki
AU - Noda, Nobuo N
AU - Komatsu, Masaaki
TI - Phosphorylation tunes p62 condensates to drive autophagic degradation of ubiquitinated proteins
T2 - The EMBO journal
J2 - EMBO J
PY - 2026
DA - 2026/
VL - 45
IS - 12
SP - 4061
EP - 4093
SN - 0261-4189
PB - Nature Publishing Group
DO - 10.1038/
UR - https://
LA - en
ER -
CSL-JSON
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