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Global mapping of the topography and magnitude of proteolytic events in apoptosis

Academic Article
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Overview

related to degree

  • Dix, Melissa, Ph.D. in Biology, Scripps Research 2006 - 2012
  • Simon, Gabriel, Ph.D. in Chemistry, Scripps Research 2004 - 2009

authors

  • Dix, Melissa
  • Simon, Gabriel
  • Cravatt, Benjamin

publication date

  • August 2008

journal

  • Cell  Journal

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.

subject areas

  • Apoptosis
  • Humans
  • Jurkat Cells
  • Mass Spectrometry
  • Peptide Hydrolases
  • Proteins
  • Proteomics
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Identity

PubMed Central ID

  • PMC2597167

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2008.06.038

PubMed ID

  • 18724940
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Additional Document Info

start page

  • 679

end page

  • 691

volume

  • 134

issue

  • 4

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