The emerging role of SPOP protein in tumorigenesis and cancer therapy

被引：0
作者：
Yizuo Song
Yichi Xu
Chunyu Pan
Linzhi Yan
Zhi-wei Wang
Xueqiong Zhu
机构：
[1] The Second Affiliated Hospital of Wenzhou Medical University,Department of Obstetrics and Gynecology
[2] The Second Affiliated Hospital of Wenzhou Medical University,Center of Scientific Research
[3] Beth Israel Deaconess Medical Center,Department of Pathology
[4] Harvard Medical School,undefined
来源：
Molecular Cancer | / 19卷
关键词：
SPOP; Oncoprotein; Tumor suppressor; Cancer; Therapy;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The nuclear speckle-type pox virus and zinc finger (POZ) protein (SPOP), a representative substrate-recognition subunit of the cullin-RING E3 ligase, has been characterized to play a dual role in tumorigenesis and cancer progression. Numerous studies have determined that SPOP suppresses tumorigenesis in a variety of human malignancies such as prostate, lung, colon, gastric, and liver cancers. However, several studies revealed that SPOP exhibited oncogenic function in kidney cancer, suggesting that SPOP could exert its biological function in a cancer type-specific manner. The role of SPOP in thyroid, cervical, ovarian, bone and neurologic cancers has yet to be determined. In this review article, we describe the structure and regulation of SPOP in human cancer. Moreover, we highlight the critical role of SPOP in tumorigenesis based on three major categories: physiological evidence (animal models), pathological evidence (human cancer specimens) and biochemical evidence (downstream ubiquitin substrates). Furthermore, we note that SPOP could be a promising therapeutic target for cancer treatment.
引用
收藏
相关论文
共 959 条
[1]  
Christianson JC(2014)Cleaning up in the endoplasmic reticulum: ubiquitin in charge Nat Struct Mol Biol 21 325-335
[2]  
Ye Y(2013)Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting Bioorg Med Chem 21 3400-3410
[3]  
Ciechanover A(2014)Roles of F-box proteins in cancer Nat Rev Cancer 14 233-247
[4]  
Wang Z(2016)Cullin 3 ubiquitin ligases in Cancer biology: functions and therapeutic implications Front Oncol 6 113-903
[5]  
Liu P(2014)SCF ubiquitin ligase-targeted therapies Nat Rev Drug Discov 13 889-690
[6]  
Inuzuka H(2008)Diversity of degradation signals in the ubiquitin-proteasome system Nat Rev Mol Cell Biol 9 679-46
[7]  
Wei W(2011)Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets Nat Rev Drug Discov 10 29-620
[8]  
Chen HY(2011)The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation Nat Rev Mol Cell Biol 12 605-20
[9]  
Chen RH(2008)Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling PLoS One 3 9-434
[10]  
Skaar JR(2005)Function and regulation of cullin-RING ubiquitin ligases Nat Rev Mol Cell Biol 6 399-642
12345678910