Abstract：
: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.
journal_name
Celljournal_title
Cellauthors
Dix MM,Simon GM,Cravatt BFdoi
10.1016/j.cell.2008.06.038subject
Has Abstractpub_date
2008-08-22 00:00:00pages
679-91issue
4eissn
0092-8674issn
1097-4172pii
S0092-8674(08)00825-8journal_volume
134pub_type
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