Ubiquitin is a small modifier protein that conjugates on lysine (Lys) residues of substrates, and it can be targeted by another ubiquitin molecule to form chains through conjugation on the intrinsic Lys residues and methionine (Met) 1 residue. Ubiquitination of substrates by such chains determines the fate of substrates, thereby influencing various biological processes. In this chapter, we focus on apoptosis with an emphasis on the regulation by ubiquitination. The signal transduction of apoptosis is governed not only by the classical function of ubiquitin, which is proteasome-dependent degradation of substrates, but also by the apoptosis signaling complex formation guided by different types of ubiquitin chains. Ubiquitinations of pro- and antiapoptotic proteins are tightly regulated by particular sets of enzymes, such as ubiquitin E3 ligases and deubiquitinases (DUBs). We further discuss ubiquitination in the tumor necrosis factor (TNF) signaling pathway as an example for the ubiquitin-dependent regulation of apoptosis and cell survival.
|Number of pages||38|
|Journal||International Review of Cell and Molecular Biology|
|Publication status||Published - Jan 1 2015|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology