期刊
CANCER RESEARCH
卷 77, 期 7, 页码 1542-1547出版社
AMER ASSOC CANCER RESEARCH
DOI: 10.1158/0008-5472.CAN-16-2958
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资金
- CDMRP LCRP grant [LC110229]
- CPRIT [RP140672, RP160652]
- UT Southwestern Friends of the Comprehensive Cancer Center
- ACS [13-068-01-TBG]
- Gibson Foundation
- Texas 4000
- Lymphoma Research Foundation
- Cancer Center support grant [2P30 CA142543-06]
- [R01CA137195]
- [NCI5P50 CA70907-15]
SUMOylation modifies the interactome, localization, activity, and lifespan of its target proteins. This process regulates several cellular machineries, including transcription, DNA damage repair, cell-cycle progression, and apoptosis. Accordingly, SUMOylation is critical in maintaining cellular homeostasis, and its deregulation leads to the corruption of a plethora of cellular processes that contribute to disease states. Among the proteins involved in SUMOylation, the protein inhibitor of activated STAT (PIAS) E3-ligases were initially described as transcriptional coregulators. Recent findings also indicate that they have a role in regulating protein stability and signaling transduction pathways. PIAS proteins interact with up to 60 cellular partners affecting several cellular processes, most notably immune regulation and DNA repair, but also cellular proliferation and survival. Here, we summarize the current knowledge about their role in tumorigenesis and cancer-related processes.
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