ISSN: 0974-276X
Marie W. Wooten
Auburn, AL, 36849
Tanzania
Research Article
Defining an Embedded Code for Protein Ubiquitination
Author(s): Trafina Jadhav and Marie W. Wooten
Trafina Jadhav and Marie W. Wooten
It has been more than 30 years since the initial report of the discovery of ubiquitin as an 8.5 kDa protein of unknown function expressed universally in living cells. And still, protein modification by covalent conjugation of the ubiquitin molecule is one of the most dynamic posttranslational modifications studied in terms of biochemistry and cell physiology. Ubiquitination plays a central regulatory role in number of eukaryotic cellular processes such as receptor endocytosis, growth-factor signaling, cell-cycle control, transcription, DNA repair, gene silencing, and stress response. Ubiquitin conjugation is a three step concerted action of the E1-E2-E3 enzymes that produces a modified protein. In this review we investigate studies undertaken to identify both ubiquitin and SUMO (small ubiquitin-related modifier) substrates with the goal of understanding how lysine sel.. View More»
DOI:
10.4172/jpb.1000091