# Wuhan researchers: VHL keeps p62 condensates liquid, and a chimeric peptide curbs tumorigenesis

- Published: 2026-11-05 23:37 UTC
- Section: Life & Health › Biology & biochemistry
- Tags: Von Hippel-Lindau protein, p62 condensates, condensate liquidity, aggrephagy, protein aggregation, proteotoxic stress, VHL IDR2 mutations, chimeric peptide, KEAP1 NRF2, tumor suppression
- URL: https://realtech.media/news/rt-498d576588b88ecc7381532b_wuhan_researchers_vhl/

**Authors from Wuhan University showed that VHL tunes the liquidity of p62 condensates under proteotoxic stress. A chimeric peptide reproduced this effect and suppressed tumorigenesis in their experiments.**

![Wuhan researchers: VHL keeps p62 condensates liquid, and a chimeric peptide curbs tumorigenesis](https://sgzwpqqelzmajkcubgkl.supabase.co/storage/v1/object/public/rt-media/2026/11/9454a720359ce8b1.jpg)
*Korinna, Wikimedia Commons, CC BY 4.0*

A team from Zhongnan Hospital and the School of Basic Medical Sciences of Wuhan University, with colleagues from Dalian Medical University and the General Hospital of Central Theater Command, has reported how the Von Hippel-Lindau protein (VHL) regulates protein aggregation. The work was published on 4 November 2026 in Nature Communications [1]. The authors studied how cells coordinate two linked processes: the aggregation of proteins when proteostasis is lost, and aggrephagy, the autophagic removal of those aggregates [1].

The authors note that the coordination of these processes has remained unclear. They showed that p62 condensates change from a gel-like to a more liquid-like state in response to proteotoxic stress [1].

## How VHL changes the state of p62 condensates

According to the authors, VHL is recruited to aggresomes and colocalizes with p62 there [1]. This is crucial for p62 to perform its distinct functions in aggresome formation and in autophagic degradation [1].

Mechanistically, VHL binds to p62 through its IDR1 region. It increases the liquid-like properties of the condensates through its IDR2 region [1].

## Consequences of VHL loss and the chimeric peptide

VHL depletion, or disease-associated mutations in IDR2, impaired the dynamics of p62 condensates [1]. This led to excessive accumulation of aggregated proteins. It was accompanied by sequestration of KEAP1 and stabilization of NRF2 [1].

The researchers also built a chimeric peptide that links the p62 PB1 domain to VHL IDR2. The peptide recapitulated the fluidity-promoting activity of VHL. The authors report that it suppressed tumorigenesis and protein aggregation [1].

The authors conclude that the data point to an HIF-independent tumor-suppressive role of VHL in regulating proteostasis. They suggest that targeting condensate dynamics could serve as a new approach to cancer treatment [1]. The abstract does not describe clinical testing of the peptide.

## Sources

1. [Nature Communications](https://doi.org/10.1038/s41467-026-79256-4)

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Source: RealTech, realtech.media — https://realtech.media/news/rt-498d576588b88ecc7381532b_wuhan_researchers_vhl/