Source:http://linkedlifedata.com/resource/pubmed/id/17000644
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2006-12-15
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pubmed:abstractText |
The small ubiquitin-like modifier (SUMO) family in vertebrates includes three different family members that are conjugated as post-translational modifications to target proteins. SUMO-2 and -3 are nearly identical but differ substantially from SUMO-1. We used quantitative proteomics to investigate the target protein preferences of SUMO-1 and SUMO-2. HeLa cells were established that stably express His6-SUMO-1 or His6-SUMO-2. These cell lines and control HeLa cells were labeled with stable arginine isotopes, and His6-SUMOs were enriched from lysates using immobilized metal affinity chromatography. 53 SUMO-conjugated proteins were identified, including 44 novel SUMO targets. 25 proteins were preferentially conjugated to SUMO-1, 19 were preferentially conjugated to SUMO-2, and nine proteins were conjugated to both SUMO-1 and SUMO-2. SART1 was confirmed by immunoblotting to have both SUMO-1- and SUMO-2-linked forms at similar levels. SUMO-1 and SUMO-2 are thus shown to have distinct and overlapping sets of target proteins, indicating that SUMO-1 and SUMO-2 may have both redundant and non-redundant cellular functions. Interestingly, 14 of the 25 SUMO-1-conjugated proteins contain zinc fingers. Although both SUMO family members play roles in many cellular processes, our data show that sumoylation is strongly associated with transcription because nearly one-third of the identified target proteins are putative transcriptional regulators.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO-1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Small Ubiquitin-Related Modifier...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1535-9476
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2298-310
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pubmed:dateRevised |
2007-8-13
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pubmed:meshHeading |
pubmed-meshheading:17000644-Chromatography, Affinity,
pubmed-meshheading:17000644-HeLa Cells,
pubmed-meshheading:17000644-Humans,
pubmed-meshheading:17000644-Multiprotein Complexes,
pubmed-meshheading:17000644-Protein Binding,
pubmed-meshheading:17000644-Protein Processing, Post-Translational,
pubmed-meshheading:17000644-Proteomics,
pubmed-meshheading:17000644-SUMO-1 Protein,
pubmed-meshheading:17000644-Small Ubiquitin-Related Modifier Proteins,
pubmed-meshheading:17000644-Transfection
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pubmed:year |
2006
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pubmed:articleTitle |
Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics.
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pubmed:affiliation |
Department of Molecular Cell Biology, Leiden University Medical Center, 2300 RC Leiden, The Netherlands. vertegaal@lumc.nl
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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