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Curr Opin Chem Biol. 2009 Dec;13(5-6):503-9. doi: 10.1016/j.cbpa.2009.07.026. Epub 2009 Sep 2.

Methods for the proteomic identification of protease substrates.

Author information

1
Department of Pharmaceutical Chemistry, University of California, San Francisco, UCSF MC 2552, 1700 4th St, San Francisco, CA 94158, United States of America.

Abstract

Proteolysis is a key regulatory post-translational modification in diverse cellular processes including programed cell death, immune function, and development. Tracking proteolytic events has become a focus of researchers assessing the downstream consequences of protease activation. In this review we summarize unbiased methods for identifying protease substrates and tracking the extent of cleavage, a field termed 'degradomics'. These include one-dimensional and two-dimensional gel-based methods for identifying protease substrates, N-terminal peptide identification methods for simultaneously identifying substrates and cleavage sites, and approaches for the quantitation of cleavage events during endogenous proteolysis. Individual methods have identified more than 300 caspase-cleaved targets during apoptosis suggesting broad future applications for these technologies.

PMID:
19729334
PMCID:
PMC2787889
DOI:
10.1016/j.cbpa.2009.07.026
[Indexed for MEDLINE]
Free PMC Article

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