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Role of SKP1-CUL1-F-Box-Protein (scf) e3 Ubiquitin ligases in Skin Cancer

Journal of Genetics and Genomics 2013年第3期40卷 97-106页

作者： Chuan-Ming Xie Wenyi Wei Yi Sun School of Biomedical Sciences The Chinese University of Hong Kong Shatin New Territories Department of Pathology Beth Israel Deaconess Medical Center Harvard Medical School Division of Radiation and Cancer Biology Department of Radiation Oncology University of Michigan

Many biological processes such as cell proliferation, differentiation, and cell death depend precisely on the timely synthesis and degradation of key regulatory proteins. While protein synthesis can be regulated at multiple levels, protein degradation is mainly controlled by the ubiquitin-proteasome system （UPS）, which consists of two distinct steps：（1） ubiquitylation of targeted protein by e1 ubiquitin-activating enzyme, e2 ubiquitin-conjugating enzyme and e3 ubiquitin ligase, and （2） subsequent degradation by the 26S proteasome. Among all e3 ubiquitin ligases, the scf （SKP1-CUL1-F-box protein） e3 ligases are the largest family and are responsible for the turnover of many key regulatory proteins. Aberrant regulation of scf e3 ligases is associated with various human diseases, such as cancers, including skin cancer. In this review, we provide a comprehensive overview of all currently published data to define a promoting role of scf e3 ligases in the development of skin cancer. The future directions in this area of research are also discussed with an ultimate goal to develop small molecule inhibitors of scf e3 ligases as a novel approach for the treatment of human skin cancer. Furthermore, altered components or substrates of scf e3 ligases may also be developed as the biomarkers for early diagnosis or predicting prognosis.

关键词： Carcinogenesis F-box proteins RING proteins scf e3 ligases Skin Ubiquitin ligases

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Functional characterization of SAG/RBX2/ROC2/RNF7, an antioxidant protein and an e3 ubiquitin ligase

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Protein & Cell 2013年第2期4卷 103-116页

作者： Yi Sun Hua Li Division of Radiation and Cancer Biology Department of Radiation OncologyUniversity of Michigan4424B Medical Science-I1301 Catherine StreetAnn ArborMI 48109USA.

SAG(Sensitive to Apoptosis Gene),also known as RBX2(RING box protein 2),ROC2(Regulator of Cullins 2),or RNF7(RING Finger Protein 7),was originally cloned in our laboratory as a redox inducible antioxi-dant protein and later characterized as the second member of the RBX/ROC RING component of the scf(SKP1-CUL-F-box Proteins)e3 ubiquitin ligase.When acting alone,SAG scavenges oxygen radicals by forming inter-and intra-molecular disulfide bonds,whereas by forming a complex with other components of the scf e3 ligase,SAG promotes ubiquitination and degradation of a number of protein substrates,includ-ing c-JUN,DePTOR,HIF-1α,IκBα,NF1,NOXA,p27,and procaspase-3,thus regulating various signaling path-ways and biological processes.Specifically,SAG pro-tects cells from apoptosis,confers radioresistance,and plays an essential and non-redundant role in mouse embryogenesis and vasculogenesis.Furthermore,stress-inducible SAG is overexpressed in a number of human cancers and SAG overexpression correlates with poor patient prognosis.Finally,SAG transgenic expression in epidermis causes an early stage inhibi-tion,but later stage promotion,of skin tumorigenesis triggered by DMBA/TPA.Given its major role in pro-moting targeted degradation of tumor suppressive proteins,leading to apoptosis suppression and accel-erated tumorigenesis,SAG e3 ligase appears to be an attractive anticancer target.

关键词： antioxidant angiogenesis apoptosis Cullin-RING ligases radiation resistance reactive oxygen species SAG/RBX2/ROC2/RNF7 scf e3 ligases tumori-genesis ubiquitin ligase vasculogenesis

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