inside the cells to take control of most of the major and minor cellular pathways (Nakayama and Nakayama, 2006). Roles of E3 ligases have been recognized in creation, fostering, as well as in destroying the components of the cells. Creation stands for the roles played by E3s in developmental processes, including, cell division, stem cell differentiation and organogenesis etc. (Nakayama and Nakayama, 2006; Stegmuller and Bonni, 2010; Yokomizo and Dzierzak, 2008). Fostering responsibilities include, cell signaling, metabolism, transcriptional control, protein sorting, trafficking, cell to cell communication and modulation of inflammatory responses as well (Acconcia et al., 2009; Hampton and Garza, 2009; Huang, 2010; Liu, 2004; Polo, 2012; Weake and Workman, 2008). Destroying capacity of E3 ligases is associated with maintenance of cellular proteostasis by regulating the turnover of cellular proteins, using degradatory pathways of autophagy and proteasome (Kuang et
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It may lead either to a functional modulation of a substrate protein, or it may also be treated as death signals, depending upon the way, ubiquitin molecules are attached (Komander and Rape, 2012; Woelk et al., 2007). First of all, by forming a thioester bond between C-terminus glycine residue of ubiquitin and a cysteine residue present on E1 enzyme activates ubiquitin in an ATP-dependent manner (Haas and Rose, 1982). Thereafter, the activated ubiquitin is transferred to another cysteine residue, present on another class of enzymes, called E2, through transesterification (Ciechanover, 1994; Hershko and Ciechanover, 1992). Afterward, transfer of ubiquitin to the substrate is mediated by a large group of another set of enzymes, known as E3 ubiquitin
It may lead either to a functional modulation of a substrate protein, or it may also be treated as death signals, depending upon the way, ubiquitin molecules are attached (Komander and Rape, 2012; Woelk et al., 2007). First of all, by forming a thioester bond between C-terminus glycine residue of ubiquitin and a cysteine residue present on E1 enzyme activates ubiquitin in an ATP-dependent manner (Haas and Rose, 1982). Thereafter, the activated ubiquitin is transferred to another cysteine residue, present on another class of enzymes, called E2, through transesterification (Ciechanover, 1994; Hershko and Ciechanover, 1992). Afterward, transfer of ubiquitin to the substrate is mediated by a large group of another set of enzymes, known as E3 ubiquitin