Autophagy is one of the cellular adaptive processes that provide protection against many pathological conditions like infection, cancer, neurodegeneration, and aging. Recent evidences suggest that ubiquitination plays an important role in degradation of proteins or defective organelle either through proteasome or autophagy. In this study, we describe the role of TRIM13, ER resident ubiquitin E3 ligase in induction of autophagy and its role during ER stress. The ectopic expression of TRIM13 in HEK-293 cells induces autophagy. Domain mapping showed that coiled-coil (CC) domain is required for induction of autophagy. TRIM13 is stabilized during ER stress, interacts with p62/SQSTM1 and co-localizes with DFCP1. TRIM13 regulates initiation of autophagy during ER stress and decreases the clonogenic ability of the cells. This study for the first time demonstrates the role of TRIM13 in induction of autophagy which may play an important role in regulation of ER stress and may act as tumor suppressor.
|Number of pages||11|
|Journal||Biochimica et Biophysica Acta - Molecular Cell Research|
|State||Published - Feb 2012|
Bibliographical noteFunding Information:
This study was supported by the Program Support to Indian Institute of Advanced Research (IIAR) sponsored by the Department of Biotechnology, Government of India (grant to RS) and grant from the Puri Foundation for Education in India (grant to RS). Dhanendra Tomar received Junior Research Fellowship from the Council of Scientific and Industrial Research (CSIR), Government of India.
- ER stress
- Ubiquitin E3 ligase
- Ubiquitin proteasome system
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology