Quality control e3 ubiquitin ligases suppress overload of abnormal protein aggregation: emerging role in neurodegeneration and ageing
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1
Department of Biology, Indian Institute of Technology Jodhpur, Cellular and Molecular Neurobiology Unit, India
Cells avoid misfolded protein aggregation under different metabolic states and stress conditions. Several lines of evidence indicate that the failure of proteostasis mechanism has been linked with neurodegeneration and ageing. Ubiquitin proteasome system (UPS) specifically targets misfolded proteins for their degradation with the help of E3 ubiquitin ligases. Chaperones assist protein folding and quality control (QC) E3 ubiquitin ligases provide major selective clearance of aberrant proteinaceous inclusions to maintain proper cellular health and fitness. Perhaps few E3 ubiquitin ligases generate specific capacity to recognize abnormal proteins but how their loss of function aggravate cellular pathology is not well understood. We demonstrated that MGRN1, ITCH and E6-AP E3 ubiquitin ligases offer the first line of defense against accumulation of misfolded proteotoxic aggregates in cells. Loss of function of these defenders reveals common signatures of neuro-pathobiological traits concomitant with misfolding protein aggregation. These studies suggest that probably differential interaction of QC E3 ubiquitin ligases can improve the misfolded protein degradation capacity of the cell to an extent capable of ameliorating molecular components of cells linked with neurodegeneration and ageing.
Keywords:
Ubiquitin,
Ageing,
proteostasis,
proteotoxicity,
neurodegeneration
Conference:
14th Meeting of the Asian-Pacific Society for Neurochemistry, Kuala Lumpur, Malaysia, 27 Aug - 30 Aug, 2016.
Presentation Type:
YIC04: Young Investigator Colloquium 4
Topic:
14th Meeting of the Asian-Pacific Society for Neurochemistry
Citation:
Mishra
A
(2016). Quality control e3 ubiquitin ligases suppress overload of abnormal protein aggregation: emerging role in neurodegeneration and ageing.
Conference Abstract:
14th Meeting of the Asian-Pacific Society for Neurochemistry.
doi: 10.3389/conf.fncel.2016.36.00066
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Received:
04 Aug 2016;
Published Online:
11 Aug 2016.
*
Correspondence:
Dr. Amit Mishra, Department of Biology, Indian Institute of Technology Jodhpur, Cellular and Molecular Neurobiology Unit, Jodhpur, Rajasthan, India, amit@iitj.ac.in