Journal
CELL
Volume 134, Issue 4, Pages 679-691Publisher
CELL PRESS
DOI: 10.1016/j.cell.2008.06.038
Keywords
-
Categories
Funding
- National Institutes of Health [CA087660]
- ARCS Foundation
- Koshland Graduate Fellowship
- Skaggs Institute for Chemical Biology
Ask authors/readers for more resources
Proteolysis is a key regulatory process that promotes the (in) activation, translocation, and/or degradation of proteins. As such, there is considerable interest in methods to comprehensively characterize proteolytic pathways in biological systems. Here, we describe a robust and versatile proteomic platform that enables direct visualization of the topography and magnitude of proteolytic events on a global scale. We use this method to generate a proteome-wide map of proteolytic events induced by the intrinsic apoptotic pathway. This profile contained 91 characterized caspase substrates as well as 170 additional proteins not previously known to be cleaved during apoptosis. Surprisingly, the vast majority of proteolyzed proteins, regardless of the extent of cleavage, yielded persistent fragments that correspond to discrete protein domains, suggesting that the generation of active effector proteins may be a principal function of apoptotic proteolytic cascades.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available