p47 Protein: Protecting Cells against Mechanical Stress

In September 2025, a groundbreaking study by researchers at the S. N. Bose National Centre for Basic Sciences (SNBNCBS), an autonomous institute under the Department of Science and Technology, has revealed the protective role of a lesser-known protein, p47, in maintaining protein stability under mechanical stress.

Key Points

Mechanical Chaperone Role: p47, previously known as an accessory to the cellular machine p97, was found to act independently as a “mechanical chaperone,” stabilizing proteins exposed to physical stress.
Unique Activity: Unlike its traditional role in protein trafficking, degradation, and membrane fusion, p47 directly binds to mechanically stretched proteins and enhances their ability to refold under continuous pulling forces.
Experimental Approach: Using single-molecule magnetic tweezers, the research team simulated cellular mechanical stress and demonstrated p47’s autonomous, force-dependent protective activity.
Foldase-like Function: This activity mirrors canonical chaperones, highlighting p47 as the first cofactor protein shown to possess single-molecule evidence of such behavior.
Therapeutic Potential: Targeting mechanical cofactors like p47 could provide novel strategies for treating diseases linked to protein instability under mechanical strain.