Functional Interplay between Caspase Cleavage and Phosphorylation Sculpts the Apoptotic Proteome (2012)
Global Mapping of the Topography and Magnitude of Proteolytic Events in Apoptosis (2008)
PROTOMAP is a recently developed technique to map in vivo substrates of proteolytic events. PROTOMAP uses 1D SDS-PAGE and mass spectrometry to globally identify shifts in gel-migration and corresponding changes in the topography of proteolytic fragments. In 2008, PROTOMAP was used to study the intrinsic apoptosis pathway in Jurkat T-cells, and these experiments identified many proteins known to be cleaved during apoptosis, as well as hundreds of novel caspase substrates. More-recently, an advanced quantitative variant of PROTOMAP was developed that utilizes SILAC for precise quantitation, and incorporates detected sites-of-phosphorylation into the topographical maps of proteins (peptographs). This new method, called quantitative phosphoPROTOMAP (or qP-PROTOMAP) permits the isoform-specific identification and quantification of phosphorylation sites and provided the first global picture of phosphorylation dynamics during apoptosis.
The purpose of this website is to make the entirety of the proteomic data generated for the aforementioned apoptosis studies available for public browsing. Six datasets are currently available, four utilizing traditional PROTOMAP as well as two qP-PROTOMAP datasets. Use the search form below to search for proteins-of-interest by keyword or accession number (IPI and Ensembl acession numbers are supported), or use the peptide-search function at the bottom of the page to search by sequence. Additionally, protocols and software-downloads are provided to facilitate PROTOMAP analyses by other labs. Please use the menu-bar on the left to navigate and if you have any questions don't hesitate to contact us.