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      Novel insights into the impact of the SUMOylation pathway in hematological malignancies (Review)

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          Abstract

          The small ubiquitin-like modifier (SUMO) system serves an important role in the regulation of protein stability and function. SUMOylation sustains the homeostatic equilibrium of protein function in normal tissues and numerous types of tumor. Accumulating evidence has revealed that SUMO enzymes participate in carcinogenesis via a series of complex cellular or extracellular processes. The present review outlines the physiological characteristics of the SUMOylation pathway and provides examples of SUMOylation participation in different cancer types, including in hematological malignancies (leukemia, lymphoma and myeloma). It has been indicated that the SUMO pathway may influence chromosomal instability, cell cycle progression, apoptosis and chemical drug resistance. The present review also discussed the possible relationship between SUMOylation and carcinogenic mechanisms, and evaluated their potential as biomarkers and therapeutic targets in the diagnosis and treatment of hematological malignancies. Developing and investigating inhibitors of SUMO conjugation in the future may offer promising potential as novel therapeutic strategies.

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          Molecular mechanisms of epithelial-mesenchymal transition.

          Samy Lamouille, Jian Xu, Rik Derynck (2014)
          The transdifferentiation of epithelial cells into motile mesenchymal cells, a process known as epithelial-mesenchymal transition (EMT), is integral in development, wound healing and stem cell behaviour, and contributes pathologically to fibrosis and cancer progression. This switch in cell differentiation and behaviour is mediated by key transcription factors, including SNAIL, zinc-finger E-box-binding (ZEB) and basic helix-loop-helix transcription factors, the functions of which are finely regulated at the transcriptional, translational and post-translational levels. The reprogramming of gene expression during EMT, as well as non-transcriptional changes, are initiated and controlled by signalling pathways that respond to extracellular cues. Among these, transforming growth factor-β (TGFβ) family signalling has a predominant role; however, the convergence of signalling pathways is essential for EMT.
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            Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation.

            K M Sakamoto, K. -B. Kim, A Kumagai … (2001)
            The intracellular levels of many proteins are regulated by ubiquitin-dependent proteolysis. One of the best-characterized enzymes that catalyzes the attachment of ubiquitin to proteins is a ubiquitin ligase complex, Skp1-Cullin-F box complex containing Hrt1 (SCF). We sought to artificially target a protein to the SCF complex for ubiquitination and degradation. To this end, we tested methionine aminopeptidase-2 (MetAP-2), which covalently binds the angiogenesis inhibitor ovalicin. A chimeric compound, protein-targeting chimeric molecule 1 (Protac-1), was synthesized to recruit MetAP-2 to SCF. One domain of Protac-1 contains the I kappa B alpha phosphopeptide that is recognized by the F-box protein beta-TRCP, whereas the other domain is composed of ovalicin. We show that MetAP-2 can be tethered to SCF(beta-TRCP), ubiquitinated, and degraded in a Protac-1-dependent manner. In the future, this approach may be useful for conditional inactivation of proteins, and for targeting disease-causing proteins for destruction.
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              Fusion protein linkers: property, design and functionality.

              Xiaoying Chen, Jennica Zaro, Wei-Chiang Shen (2013)
              As an indispensable component of recombinant fusion proteins, linkers have shown increasing importance in the construction of stable, bioactive fusion proteins. This review covers the current knowledge of fusion protein linkers and summarizes examples for their design and application. The general properties of linkers derived from naturally-occurring multi-domain proteins can be considered as the foundation in linker design. Empirical linkers designed by researchers are generally classified into 3 categories according to their structures: flexible linkers, rigid linkers, and in vivo cleavable linkers. Besides the basic role in linking the functional domains together (as in flexible and rigid linkers) or releasing the free functional domain in vivo (as in in vivo cleavable linkers), linkers may offer many other advantages for the production of fusion proteins, such as improving biological activity, increasing expression yield, and achieving desirable pharmacokinetic profiles. Copyright © 2012 Elsevier B.V. All rights reserved.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Oncol
                Journal ID (iso-abbrev): Int J Oncol
                Journal ID (publisher-id): IJO
                Title: International Journal of Oncology
                Publisher: D.A. Spandidos
                ISSN (Print): 1019-6439
                ISSN (Electronic): 1791-2423
                Publication date Collection: September 2021
                Publication date (Electronic): 06 August 2021
                Publication date PMC-release: 06 August 2021
                Volume: 59
                Issue: 3
                Electronic Location Identifier: 73
                Affiliations
                [1 ]Nanjing Hospital of Chinese Medicine Affiliated to Nanjing University of Chinese Medicine, Nanjing, Jiangsu 210022, P.R. China
                [2 ]School of Medicine and Holistic Integrative Medicine, Nanjing University of Chinese Medicine, Nanjing, Jiangsu 210023, P.R. China
                Author notes
                Correspondence to: Professor Chunyan Gu or Professor Ye Yang, School of Medicine and Holistic Integrative Medicine, Nanjing University of Chinese Medicine, 138 Xianlin Road, Nanjing, Jiangsu 210023, P.R. China, E-mail: guchunyan@ 123456njucm.edu.cn , E-mail: yangye876@ 123456sina.com
                [*]

                Contributed equally

                Article
                Publisher ID: ijo-59-03-05253
                DOI: 10.3892/ijo.2021.5253
                PMC ID: 8360622
                PubMed ID: 34368858
                SO-VID: 7b37bb48-8ce4-45e1-95d5-b6ff641b5899
                Copyright © Copyright: © Wang et al.
                License:

                This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

                History
                Date received : 29 April 2021
                Date accepted : 26 July 2021
                Funding
                Funded by: National Natural Science Foundation of China
                Award ID: 81970196
                Award ID: 82073885
                Funded by: Natural Science Foundation of Jiangsu Province
                Award ID: BK20200097
                This work was supported by the National Natural Science Foundation of China (grant nos. 81970196 and 82073885), the Natural Science Foundation of Jiangsu Province (grant no. BK20200097), and a project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions (Integration of Chinese and Western Medicine).
                Categories
                Subject: Articles

                Keywords: sumoylation,sumo enzymes,hematological malignancies,multiple myeloma
                Data availability:
                Keywords: sumoylation, sumo enzymes, hematological malignancies, multiple myeloma

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