期刊
MOLECULAR & CELLULAR PROTEOMICS
卷 5, 期 12, 页码 2298-2310出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M600212-MCP200
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资金
- Biotechnology and Biological Sciences Research Council [BBS/B/11974/2] Funding Source: Medline
- Medical Research Council [G0301131] Funding Source: Medline
- Wellcome Trust [073980] Funding Source: Medline
- MRC [G0301131] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BBS/B/11974/2] Funding Source: researchfish
- Medical Research Council [G0301131] Funding Source: researchfish
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 His 6-SUMO-1 or His 6-SUMO-2. These cell lines and control HeLa cells were labeled with stable arginine isotopes, and His 6-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 immuno-blotting 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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