Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 279, Issue 20, Pages 20999-21002Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M401541200
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Funding
- NCI NIH HHS [CA 71443, CA 85146] Funding Source: Medline
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Reversible covalent modification of proteins with a small ubiquitin-related modifier ( SUMO) is emerging as an important system contributing to dynamic regulation of protein function. To enhance our understanding of the cell regulatory systems impacted by sumoylation, we used affinity chromatography-coupled high pressure liquid chromatography/tandem mass spectrometry for unbiased identification of candidate cellular SUMO substrate proteins. Here we describe the identification of 21 candidate sumoylated proteins from whole-cell lysates of HEK-293 cells. The nature of the proteins identified is consistent with a role for sumoylation in diverse cell regulatory systems but highlights regulation of chromatin organization and gene expression as major systems targeted by the sumoylation machinery.
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