Evidence map›Paper›PMID 41543905›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Proteasomal proteolysis in p62 condensates directs tumor suppression or growth depending on their subcellular localization.

Chen Lulu-Shimron, Zhiwen Luo, Vera Brekhman, Lina Huang, Ido Livneh, Hidetaka Kosako, Victoria Cohen-Kaplan, Aaron Ciechanover

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Proteasomal proteolysis in p62 condensates directs tumor suppression or growth depending on their subcellular localization.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Chen Lulu-ShimronRappaport-Technion Integrated Cancer Center, The Rappaport Faculty of Medicine and Research Institute, Technion- Israel Institute of Technology, Haifa 3109602, Israel.
Zhiwen LuoNational Cancer Center, National Clinical Research Center for Cancer, Chinese Academy of Medical Sciences, and Peking Union Medical College Cancer Hospital, Beijing, China.ORCID 0000-0003-1400-1437
Vera BrekhmanRappaport-Technion Integrated Cancer Center, The Rappaport Faculty of Medicine and Research Institute, Technion- Israel Institute of Technology, Haifa 3109602, Israel.
Lina HuangRappaport-Technion Integrated Cancer Center, The Rappaport Faculty of Medicine and Research Institute, Technion- Israel Institute of Technology, Haifa 3109602, Israel.
Ido LivnehRappaport-Technion Integrated Cancer Center, The Rappaport Faculty of Medicine and Research Institute, Technion- Israel Institute of Technology, Haifa 3109602, Israel.
Hidetaka KosakoDivision of Cell Signaling, Institute of Advanced Medical Sciences and Laboratory of Proteomics, Institute of Photonics and Human Health Frontier, Tokushima University, Tokushima 770-8503, Japan.ORCID 0000-0003-3228-6368
Victoria Cohen-KaplanRappaport-Technion Integrated Cancer Center, The Rappaport Faculty of Medicine and Research Institute, Technion- Israel Institute of Technology, Haifa 3109602, Israel.
Aaron CiechanoverRappaport-Technion Integrated Cancer Center, The Rappaport Faculty of Medicine and Research Institute, Technion- Israel Institute of Technology, Haifa 3109602, Israel.ORCID 0000-0001-9184-8944

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p62/SQSTM1 generates liquid-liquid phase-separated condensates that participate in diverse processes, including protein quality control (PQC) and autophagy. Nuclear p62 condensates were shown to act as ubiquitin- and proteasome-mediated degradation hubs, whereas the involvement of cytoplasmic condensates in this pathway has remained unclear. Here, we show that cytoplasmic p62 condensates serve as a hub for proteasomal degradation that displays distinct substrate preferences compared with nuclear condensates. Specifically, cytoplasmic condensates mediate accelerated degradation of the tumor suppressor p53 through recruitment MDM2, its E3 ligase, while nuclear condensates are selectively enriched with USP7, a deubiquitinating enzyme (DUB) that stabilizes p53. Immunohistochemical analysis of human tissues reveal that p62 in healthy tissues is largely localized to the nucleus, whereas in the corresponding malignant tissues, it is largely in the cytosol, which is correlated with reduced p53 abundance in tumors. Nuclear p62 condensates also promote the degradation of oncogenic c-Myc, underscoring compartment-specific differences in protein turnover. Experiments in cancer cells and xenografts demonstrate that cytoplasmic p62 condensates drive tumor growth, whereas nuclear p62 condensates suppress it. Moreover, condensate formation rather than p62 expression alone is required for both enhanced proteolytic activity and tumor growth modulation. Proteomic analysis reveals that nuclear p62, unlike its cytosolic counterpart, is linked to enrichment of proteins associated with apoptosis, p53 stabilization, DNA damage response, and cellular senescence-all related to tumor suppression. These findings establish that p62 condensates provide compartment-specific regulation of ubiquitin and proteasomal degradation and suggest that manipulating their localization or affecting their dynamics can offer different therapeutic opportunities.

Indexed as

NeoplasmsProteasome Endopeptidase ComplexSequestosome-1 ProteinAnimalsCell Line, TumorCell NucleusCytoplasmHumansMiceProteolysisProto-Oncogene Proteins c-mdm2Proto-Oncogene Proteins c-mycTumor Suppressor Protein p53Ubiquitin-Specific Peptidase 7MDM2 protein, humanMYC protein, humanProteasome Endopeptidase ComplexProto-Oncogene Proteins c-mdm2Proto-Oncogene Proteins c-mycSequestosome-1 ProteinSQSTM1 protein, humanTP53 protein, humanTumor Suppressor Protein p53Ubiquitin-Specific Peptidase 7cancerc-Mycp53p62 condensatesubiquitin–proteasome system

Identifiers

PMID41543905
PMCPMC12818402

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.