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How protein droplets change the efficiency of cellular cleanup

How does a protein-rich droplet become easier or harder to break down?

Scientific context

How it works

Inside cells, proteins sometimes gather into droplet-like groups. These groups can remain fluid, like a liquid, or become more gel-like and less mobile. We study how such physical changes affect the removal of unwanted material.

A protein called p62 helps collect proteins marked for degradation and forms these droplet-like assemblies. A 2026 study showed that adding a phosphate group to part of p62 can turn relatively large, fluid assemblies into smaller, more gel-like ones.

This change makes the assemblies interact more effectively with the membrane that surrounds material for recycling, helping unwanted proteins be broken down. The assemblies are therefore not simply storage sites: their physical state helps control cellular cleanup.

Evidence & open questions

What we want to learn next

Published research

We want to understand in greater detail how a small chemical change in p62 affects the stiffness of an entire assembly and how strongly it associates with membranes.

Literature

Related publications & press releases

EMBO Journal (2026)Phosphorylation tunes p62 condensates to drive autophagic degradation of ubiquitinated proteins

Phosphorylation changes the properties of p62 condensates and affects how unwanted proteins are removed.