For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
7
views
114
references
 Top references
cited by
45
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      420
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      The emerging role of SPOP protein in tumorigenesis and cancer therapy

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          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.

          Related collections

          Most cited references114

          • Record: found
          • Abstract: found
          • Article: not found

          Mammalian sirtuins: biological insights and disease relevance.

          Marcia Haigis, David A Sinclair (2010)
          Aging is accompanied by a decline in the healthy function of multiple organ systems, leading to increased incidence and mortality from diseases such as type II diabetes mellitus, neurodegenerative diseases, cancer, and cardiovascular disease. Historically, researchers have focused on investigating individual pathways in isolated organs as a strategy to identify the root cause of a disease, with hopes of designing better drugs. Studies of aging in yeast led to the discovery of a family of conserved enzymes known as the sirtuins, which affect multiple pathways that increase the life span and the overall health of organisms. Since the discovery of the first known mammalian sirtuin, SIRT1, 10 years ago, there have been major advances in our understanding of the enzymology of sirtuins, their regulation, and their ability to broadly improve mammalian physiology and health span. This review summarizes and discusses the advances of the past decade and the challenges that will confront the field in the coming years.
          Article 0 comments Cited 651 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.

            Arul M Chinnaiyan, Karen O'Rourke, Muneesh Tewari … (1995)
            Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the lpr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interleukin-1 beta-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.
            Article 0 comments Cited 319 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Diverse somatic mutation patterns and pathway alterations in human cancers.

              Zhengyan Kan, Bijay Jaiswal, Jeremy Stinson … (2010)
              The systematic characterization of somatic mutations in cancer genomes is essential for understanding the disease and for developing targeted therapeutics. Here we report the identification of 2,576 somatic mutations across approximately 1,800 megabases of DNA representing 1,507 coding genes from 441 tumours comprising breast, lung, ovarian and prostate cancer types and subtypes. We found that mutation rates and the sets of mutated genes varied substantially across tumour types and subtypes. Statistical analysis identified 77 significantly mutated genes including protein kinases, G-protein-coupled receptors such as GRM8, BAI3, AGTRL1 (also called APLNR) and LPHN3, and other druggable targets. Integrated analysis of somatic mutations and copy number alterations identified another 35 significantly altered genes including GNAS, indicating an expanded role for galpha subunits in multiple cancer types. Furthermore, our experimental analyses demonstrate the functional roles of mutant GNAO1 (a Galpha subunit) and mutant MAP2K4 (a member of the JNK signalling pathway) in oncogenesis. Our study provides an overview of the mutational spectra across major human cancers and identifies several potential therapeutic targets.
              Article 0 comments Cited 298 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Yizuo Song: Yi_zuo@126.com
                Yichi Xu: xuyichixuyichi@163.com
                Chunyu Pan: panchunyu95@163.com
                Linzhi Yan: ylz204121@hotmail.com
                Zhi-wei Wang:
                ORCID: http://orcid.org/0000-0002-6465-7779
                zwang6@bidmc.harvard.edu
                Xueqiong Zhu: zjwzzxq@163.com
                Journal
                Journal ID (nlm-ta): Mol Cancer
                Journal ID (iso-abbrev): Mol. Cancer
                Title: Molecular Cancer
                Publisher: BioMed Central (London )
                ISSN (Electronic): 1476-4598
                Publication date (Electronic): 4 January 2020
                Publication date PMC-release: 4 January 2020
                Publication date Collection: 2020
                Volume: 19
                Electronic Location Identifier: 2
                Affiliations
                [1 ]ISNI 0000 0004 1764 2632, GRID grid.417384.d, Department of Obstetrics and Gynecology, , The Second Affiliated Hospital of Wenzhou Medical University, ; No. 109 Xueyuan Xi Road, Wenzhou, 325027 Zhejiang China
                [2 ]ISNI 0000 0004 1764 2632, GRID grid.417384.d, Center of Scientific Research, , The Second Affiliated Hospital of Wenzhou Medical University, ; No. 109 Xueyuan Xi Road, Wenzhou, 325027 Zhejiang China
                [3 ]Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA USA
                Author information
                http://orcid.org/0000-0002-6465-7779
                Article
                Publisher ID: 1124
                DOI: 10.1186/s12943-019-1124-x
                PMC ID: 6942384
                PubMed ID: 31901237
                SO-VID: 6d2ca087-db26-4807-8cf1-cb51d0124505
                Copyright © © The Author(s). 2020
                License:

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                Date received : 5 August 2019
                Date accepted : 23 December 2019
                Funding
                Funded by: FundRef http://dx.doi.org/10.13039/501100001809, National Natural Science Foundation of China;
                Award ID: 81572936 and 81773186
                Categories
                Subject: Review
                Custom metadata
                issue-copyright-statement © The Author(s) 2020

                ScienceOpen disciplines: Oncology & Radiotherapy
                Keywords: spop,oncoprotein,tumor suppressor,cancer,therapy
                Data availability:
                ScienceOpen disciplines: Oncology & Radiotherapy
                Keywords: spop, oncoprotein, tumor suppressor, cancer, therapy

                Comments

                Comment on this article

                scite_

                Similar content420

                See all similar

                Cited by45

                See all cited by

                Most referenced authors2,336

                See all reference authors