Regulatory roles of an atypical ubiquitin ligase UBE2O in orphans of multi-protein complexes for degradation

Turkish Journal of Biology

article

LV, YI¹  XING, FEIYUE¹ 

[1]Department of Immunobiology, Institute of Tissue Transplantation and Immunology, Jinan University

关键词: UBE2O;    SMAD6;    TRAF6;    BAP1;    AMPKa2;    MLL;   

DOI  :  10.55730/1300-0152.2585

学科分类：生物科学（综合）

来源: Scientific and Technical Research Council of Turkey - TUBITAK

【 摘 要 】

UBE2O as an atypical ubiquitin-conjugating enzyme possesses an E2-E3 hybrid enzyme activity. It can regulate substrate levels or transcriptional activities by cooperating with other E3 ubiquitin ligases or forming homomeric complexes displaying intrinsic E2 and E3 activities. UBE2O controls the quality of cell proteome including protein degradation, modification, transport and location. Recent studies reveal that UBE2O plays a vital role in intracellular protein ubiquitination processes by regulating BMP/SMAD, TRAF/ NF-κB, mTOR/HIF1a and IL-1ß/IRAK4 signaling pathways, c-Maf stability and BAP1 subcellular location, which is proposed as a quality control supervisor of multiprotein complexes for degradation. Its abnormality leads to a variety of physical activity disorders and even occurrence of cancer. UBE2O is entirely distinct in molecular structure and functions from other E2 ubiquitin ligase. Exploring and elucidating regulatory mechanism of UBE2O may identify novel crucial molecular targets so as to pave therapeutic approaches for ubiquitination-associated metabolic disorders and diseases. Here, we particularly feature regulatory pathways of UBE2O in orphans of multiprotein complexes for degradation and its potential application.

【 授权许可】

Unknown