A quantitative proteomics design for systematic identification of protease cleavage events.

Molecular & Cellular Proteomics : MCP
Francis ImpensKris Gevaert

Abstract

We present here a novel proteomics design for systematic identification of protease cleavage events by quantitative N-terminal proteomics, circumventing the need for time-consuming manual validation. We bypass the singleton detection problem of protease-generated neo-N-terminal peptides by introducing differential isotopic proteome labeling such that these substrate reporter peptides are readily distinguished from all other N-terminal peptides. Our approach was validated using the canonical human caspase-3 protease and further applied to mouse cathepsin D and E substrate processing in a mouse dendritic cell proteome, identifying the largest set of protein protease substrates ever reported and gaining novel insight into substrate specificity differences of these cathepsins.

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Citations

Oct 2, 2012·Nature Methods·Anthony J O'DonoghueCharles S Craik
Oct 15, 2010·Molecular & Cellular Proteomics : MCP·Paul W BowyerMatthew Bogyo
Oct 9, 2012·Molecular & Cellular Proteomics : MCP·Håvard FoynThomas Arnesen
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Jan 8, 2013·Current Opinion in Chemical Biology·Kim PlasmanKris Gevaert
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Jun 18, 2015·Molecular & Cellular Proteomics : MCP·Barbara SobotičMarko Fonović
May 6, 2016·Biological Chemistry·Anthony J O'DonoghueCharles S Craik
Jul 11, 2019·Proteomics. Clinical Applications·Marija GrozdanićMarko Fonović
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Dec 5, 2018·Journal of Proteome Research·Andrea ArgentiniLennart Martens

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