New Insights into the Role of Ubiquitin Networks in the Regulation of Antiapoptosis Pathways.

International Review of Cell and Molecular Biology
Tomoko Asaoka, Fumiyo Ikeda

Abstract

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.

Citations

May 20, 2017·Critical Reviews in Biochemistry and Molecular Biology·Petra EbnerFumiyo Ikeda
Apr 22, 2018·The FEBS Journal·Lilian M FennellFumiyo Ikeda
Oct 21, 2017·Oncotarget·Sergey A Sinenko
Apr 28, 2017·Open Biology·Katrin Rittinger, Fumiyo Ikeda
Feb 27, 2018·Dose-response : a Publication of International Hormesis Society·Carmel MothersillColin Seymour

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Apoptosis is a specific process that leads to programmed cell death through the activation of an evolutionary conserved intracellular pathway leading to pathognomic cellular changes distinct from cellular necrosis

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