Molecular Neurobiology

, Volume 45, Issue 3, pp 571–585

E3 Ubiquitin Ligases in Protein Quality Control Mechanism

  • Deepak Chhangani
  • Ajay Prakash Joshi
  • Amit Mishra
Article

DOI: 10.1007/s12035-012-8273-x

Cite this article as:
Chhangani, D., Joshi, A.P. & Mishra, A. Mol Neurobiol (2012) 45: 571. doi:10.1007/s12035-012-8273-x

Abstract

In living cells, polypeptide chains emerging from ribosomes and preexisting polypeptide chains face constant threat of misfolding and aggregation. To prevent protein aggregation and to fulfill their biological activity, generally, protein must fold into its proper three-dimensional structure throughout their lifetimes. Eukaryotic cell possesses a quality control (QC) system to contend the problem of protein misfolding and aggregation. Cells achieve this functional QC system with the help of molecular chaperones and ubiquitin–proteasome system (UPS). The well-conserved UPS regulates the stability of various proteins and maintains all essential cellular function through intracellular protein degradation. E3 ubiquitin ligase enzyme determines specificity for degradation of certain substrates via UPS. New emerging evidences have provided considerable information that various E3 ubiquitin ligases play a major role in cellular QC mechanism and principally designated as QC E3 ubiquitin ligases. Nevertheless, very little is known about how E3 ubiquitin ligase maintains QC mechanism against abnormal proteins under various stress conditions. Here in this review, we highlight and discuss the functions of various E3 ubiquitin ligases implicated in protein QC mechanism. Improving our knowledge about such processes may provide opportunities to modulate protein QC mechanism in age-of-onset diseases that are caused by protein aggregation.

Keywords

E3 ubiquitin ligase Protein misfolding Aggregation Ubiquitin–proteasome system Cellular quality control 

Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  • Deepak Chhangani
    • 1
  • Ajay Prakash Joshi
    • 2
  • Amit Mishra
    • 1
  1. 1.Biology Laboratory, Indian Institute of Technology RajasthanJodhpurIndia
  2. 2.Centre for Converging TechnologiesUniversity of RajasthanJaipurIndia

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