Accumulation of protein aggregates is a hallmark of neurodegenerative diseases. For therapeutic interventions of neurodegenerative diseases, it is important to understand the mechanism involved in the formation and degradation of protein aggregates.
At the Institute of Life Sciences (ILS) Scientsts led led by Dr. Santosh Chuahan, have unrevealed mechanisms by which the protein aggregates are formed and degraded. They found that a protein named, TRIM16 governs the cell stress machineries to safely dispose the protein aggregates which otherwise could be cytotoxic. The work suggests that pharmacological activation of TRIM16 could be a useful strategy for therapeutic interventions of neurodegenerative diseases. This work is published in the recent issue of “The EMBO Journal”.
The study showed that the cancer cells can highjack the TRIM16 governed cell stress machinery so that they can survive under harsh cellular stress conditions including oxidative stress. They found that knocking out this protein in cancer cells make them vulnerable and cannot tolerate the oxidative stress succumbing them to death. Hence, the pharmacological down-regulation of TRIM16 could have direct implication in cancer therapy. The study was financially supported by DBT and The Wellcome Trust/DBT India Alliance.