Volume 1 | Issue 4 | DOI: https://doi.org/10.33696/Signaling.1.023
A Novel Regulatory Mechanism to Regulate the Deubiquitinating Activity of USP25 by Oligomerization
- 1Institut de Biotecnologia i de Biomedicina. Departament de Bioquimica i Biologia Molecular, Universitat Autonoma de Barcelona, 08193 Barcelona, Bellaterra, Spain
David Reverter, email@example.com
Received Date: August 24, 2020
Accepted Date: September 18, 2020
Li Y, Liu B, Reverter D. A Novel Regulatory Mechanism to Regulate the Deubiquitinating Activity of USP25 by Oligomerization. J Cell Signal 2020;1(4):151-154.
Copyright: © 2020 Li Y, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Apoptosis is a physiological response in development and homeostasis of metazoans. Apoptosis is triggered during pathological events as a means to renew affected tissues and eliminate cancer cells. The immune system regulates the extrinsic pathway of apoptosis, where signals such as TNFα or displayed ligands on the surface of immune cells trigger signal cascades by death receptors present on targeted cells.
Protein ubiquitination is a major post-translational mechanism that regulates fate and function of many proteins in the cell, either by regulating their abundance by the 26S-proteasome-ubiquitin system or by modulating protein activity by the attachment of the ubiquitin modifier