Abstract
Mammalian cells contain proteins that function as endogenous inhibitors of apoptosis (IAPs) and that act, at least in part, by inhibiting caspases, proteases that mediate signals leading to cell death. In thymocytes, inhibitors of the proteasome, a protein complex that mediates proteolysis of ubiquitin-tagged proteins, can block apoptosis. Yang et al. find that the IAPs have ubiquitin ligase activity and that they appear to catalyze auto-ubiquitination. This activity increases in response to apoptotic stimuli, indicating that regulated proteolysis of IAPs contributes to the control of cell death in thymocytes. Yang, Y., Fang, S., Jensen, J.P., Weissman, A.M., and Ashwell, J.D. (2000) Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288 : 874-877. [Abstract] [Full Text]
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
