SUMO proteomics to decipher the SUMO-modified proteome regulated by various diseases.

Published

Journal Article (Review)

Small ubiquitin-like modifier (SUMO1-3) conjugation is a posttranslational protein modification whereby SUMOs are conjugated to lysine residues of target proteins. SUMO conjugation can alter the activity, stability, and function of target proteins, and thereby modulate almost all major cellular pathways. Many diseases are associated with SUMO conjugation, including heart failure, arthritis, cancer, degenerative diseases, and brain ischemia/stroke. It is, therefore, of major interest to characterize the SUMO-modified proteome regulated by these disorders. SUMO proteomics analysis is hampered by low levels of SUMOylated proteins. Several strategies have, therefore, been developed to enrich SUMOylated proteins from cell/tissue extracts. These include proteomics analysis on cells expressing epitope-tagged SUMO isoforms, use of monoclonal SUMO antibodies for immunoprecipitation and epitope-specific peptides for elution, and affinity purification with peptides containing SUMO interaction motifs to specifically enrich polySUMOylated proteins. Recently, two mouse models were generated and characterized that express tagged SUMO isoforms, and allow purification of SUMOylated proteins from complex organ extracts. Ultimately, these new analytical tools will help to decipher the SUMO-modified proteome regulated by various human diseases, and thereby, identify new targets for preventive and therapeutic purposes.

Full Text

Duke Authors

Cited Authors

  • Yang, W; Paschen, W

Published Date

  • March 2015

Published In

Volume / Issue

  • 15 / 5-6

Start / End Page

  • 1181 - 1191

PubMed ID

  • 25236368

Pubmed Central ID

  • 25236368

Electronic International Standard Serial Number (EISSN)

  • 1615-9861

Digital Object Identifier (DOI)

  • 10.1002/pmic.201400298

Language

  • eng

Conference Location

  • Germany