Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins

Yingming Zhao, Sung Won Kwon, Anthony Anselmo, Kiran Kaur, Michael A. White

Research output: Contribution to journalArticle

116 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)20999-21002
Number of pages4
JournalJournal of Biological Chemistry
Volume279
Issue number20
DOIs
StatePublished - May 14 2004

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Small Ubiquitin-Related Modifier Proteins
Sumoylation
Ubiquitin
Substrates
Proteins
High pressure liquid chromatography
HEK293 Cells
Affinity chromatography
Tandem Mass Spectrometry
Affinity Chromatography
Chromatin
Gene expression
High Pressure Liquid Chromatography
Machinery
Mass spectrometry
Gene Expression

ASJC Scopus subject areas

  • Biochemistry

Cite this

Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins. / Zhao, Yingming; Kwon, Sung Won; Anselmo, Anthony; Kaur, Kiran; White, Michael A.

In: Journal of Biological Chemistry, Vol. 279, No. 20, 14.05.2004, p. 20999-21002.

Research output: Contribution to journalArticle

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