4.8 Article

Complementary positional proteomics for screening substrates of endo- and exoproteases

Journal

NATURE METHODS
Volume 7, Issue 7, Pages 512-U39

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.1469

Keywords

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Funding

  1. Research Foundation, Flanders (FWO-Vlaanderen)
  2. Institute for the Promotion of Innovation through Science and Technology in Flanders (IWT-Vlaanderen)
  3. Fund for Scientific Research, Flanders (Belgium) [G.0156.05, G.0077.06, G.0042.07]
  4. Ghent University [BOF07/GOA/012]
  5. Interuniversity Attraction Poles [IUAP06]
  6. EC [LSH6-2006-018830-CAMP]
  7. Ministerio de Ciencia y Innovacion, Spain [BIO2007-68046]

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We describe a positional proteomics approach to simultaneously analyze N- and C-terminal peptides and used it to screen for human protein substrates of granzyme B and carboxypeptidase A4 in human cell lysates. This approach allowed comprehensive proteome studies, and we report the identification of 965 database-annotated protein C termini, 334 neo-C termini resulting from granzyme B processing and 16 neo-C termini resulting from carboxypeptidase A4 processing.

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