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  Detecting endogenous SUMO targets in mammalian cells and tissues.

Becker, J., Barysch, S. V., Karaca, S., Dittmer, C., Hsiao, H. H., Diaz, M. B., et al. (2013). Detecting endogenous SUMO targets in mammalian cells and tissues. Nature Structural and Molecular Biology, 20(4), 525-531. doi:10.1038/nsmb.2526.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-FBF3-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-1DEB-A
Genre: Journal Article

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 Creators:
Becker , J., Author
Barysch, S. V., Author
Karaca, S.1, Author              
Dittmer, C., Author
Hsiao, H. H.1, Author              
Diaz , M. B., Author
Herzig, S., Author
Urlaub, H.1, Author              
Melchior, F., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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 Abstract: SUMOylation is an essential modification that regulates hundreds of proteins in eukaryotic cells. Owing to its dynamic nature and low steady-state levels, endogenous SUMOylation is challenging to detect. Here, we present a method that allows efficient enrichment and identification of endogenous targets of SUMO1 and the nearly identical SUMO2 and 3 (SUMO 2/3) from vertebrate cells and complex organ tissue. Using monoclonal antibodies for which we mapped the epitope, we enriched SUMOylated proteins by immunoprecipitation and peptide elution. We used this approach in combination with MS to identify SUMOylated proteins, which resulted in the first direct comparison of the endogenous SUMO1- and SUMO2/3-modified proteome in mammalian cells, to our knowledge. This protocol provides an affordable and feasible tool to investigate endogenous SUMOylation in primary cells, tissues and organs, and it will facilitate understanding of SUMO's role in physiology and disease.

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Language(s): eng - English
 Dates: 2013-03-172013-04
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/nsmb.2526
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 20 (4) Sequence Number: - Start / End Page: 525 - 531 Identifier: -