TRIM16 controls turnover of protein aggregates by modulating NRF2, ubiquitin system, and autophagy: implication for tumorigenesis
Autor: | Kautilya Kumar Jena, Srinivasa Prasad Kolapalli, Subhash Mehto, Swati Chauhan, Santosh Chauhan |
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Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: | |
Zdroj: | Molecular & Cellular Oncology, Vol 5, Iss 6 (2018) |
Druh dokumentu: | article |
ISSN: | 2372-3556 23723556 |
DOI: | 10.1080/23723556.2018.1532251 |
Popis: | 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. |
Databáze: | Directory of Open Access Journals |
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