Journal
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1764, Issue 12, Pages 1940-1947Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2006.09.004
Keywords
mass spectrometry ubiquitin
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Funding
- NIA NIH HHS [AG025688, P50 AG025688] Funding Source: Medline
- NIDDK NIH HHS [DK069580, R21 DK069580] Funding Source: Medline
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Protein modification by ubiquitin is a central regulatory mechanism in eukaryotic cells. Recent proteomics developments in mass spectrometry enable systematic analysis of cellular components in the ubiquitin pathway. Here, we review the advances in analyzing ubiquitinated substrates, determining modified lysine residues, quantifying polyubiquitin chain topologies, as well as profiling deubiquitinating enzymes based on the activity. Moreover, proteomic approaches have been developed for probing the interactome of proteasome and for identifying proteins with ubiquitin-binding domains. Similar strategies have been applied on the studies of the modification by ubiquitin-like proteins as well. These strategies are discussed with respect to their advantages, limitations and potential improvements. While the utilization of current methodologies has rapidly expanded the scope of protein modification by the ubiquitin family, a more active role is anticipated in the functional studies with the emergence of quantitative mass spectrometry. (c) 2006 Elsevier B.V. All rights reserved.
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