Journal
MOLECULAR & CELLULAR ONCOLOGY
Volume 5, Issue 6, Pages -Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/23723556.2018.1532251
Keywords
TRIM16; NRF2; NFE2L2; p62/SQSTM1; autophagy; Protein aggregates; cancer; oxidative stress; protein homeostasis; protein quality control; aggrephagy; proteotoxic stress
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Funding
- Wellcome Trust/Department of Biotechnology (DBT) India Alliance fellowship [IA/I/15/2/502071]
- ILS core funding (Department of Biotechnology, India)
- Early Career Reward (SERB) [ECR/2016/000478]
- SERB (NPDF) [PDF/2016/001697]
- DST [SR/WOS-A/LS-9/2016]
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Protein misfolding and protein aggregation are linked to several diseases commonly called as proteinopathies, which include cancer. Understanding the mechanisms of proteostasis could provide newer strategies to combat proteinopathies. We have recently demonstrated a new mechanism where we found that TRIM16 (tripartite motif-containing protein 16) utilizing NRF2-p62 axis and autophagy streamlines the safe disposal of misfolded proteins to maintain protein homeostasis.
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