Literature DB >> 34476738

Regulation of topoisomerase II stability and activity by ubiquitination and SUMOylation: clinical implications for cancer chemotherapy.

Ying Ma1,2, Brian J North3, Jianfeng Shu4,5.   

Abstract

DNA topoisomerases II (TOP2) are peculiar enzymes (TOP2α and TOP2β) that modulate the conformation of DNA by momentarily breaking double-stranded DNA to allow another strand to pass through, and then rejoins the DNA phosphodiester backbone. TOP2α and TOP2β play vital roles in nearly all events involving DNA metabolism, including DNA transcription, replication, repair, and chromatin remodeling. Beyond these vital functions, TOP2 enzymes are therapeutic targets for various anticancer drugs, termed TOP2 poisons, such as teniposide, etoposide, and doxorubicin. These drugs exert their antitumor activity by inhibiting the activity of TOP2-DNA cleavage complexes (TOP2ccs) containing DNA double-strand breaks (DSBs), subsequently leading to the degradation of TOP2 by the 26S proteasome, thereby exposing the DSBs and eliciting a DNA damage response. Failure of the DSBs to be appropriately repaired leads to genomic instability. Due to this mechanism, patients treated with TOP2-based drugs have a high incidence of secondary malignancies and cardiotoxicity. While the cytotoxicity associated with TOP2 poisons appears to be TOP2α-dependent, the DNA sequence rearrangements and formation of DSBs appear to be mediated primarily through TOP2β inhibition, likely due to the differential degradation patterns of TOP2α and TOP2β. Research over the past few decades has shown that under various conditions, the ubiquitin-proteasome system (UPS) and the SUMOylation pathway are primarily responsible for regulating the stability and activity of TOP2 and are therefore critical regulators of the therapeutic effect of TOP2-targeting drugs. In this review, we summarize the current progress on the regulation of TOP2α and TOP2β by ubiquitination and SUMOylation. By fully elucidating the basic biology of these essential and complex molecular mechanisms, better strategies may be developed to improve the therapeutic efficacy of TOP2 poisons and minimize the risks of therapy-related secondary malignancy.
© 2021. The Author(s), under exclusive licence to Springer Nature B.V.

Entities:  

Keywords:  SUMOylation; TOP2 poisons; TOP2ccs; Ubiquitination

Mesh:

Substances:

Year:  2021        PMID: 34476738      PMCID: PMC8589089          DOI: 10.1007/s11033-021-06665-7

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.742


  94 in total

1.  26 S proteasome-mediated degradation of topoisomerase II cleavable complexes.

Authors:  Y Mao; S D Desai; C Y Ting; J Hwang; L F Liu
Journal:  J Biol Chem       Date:  2001-08-23       Impact factor: 5.157

2.  The topoisomerase IIbeta circular clamp arrests transcription and signals a 26S proteasome pathway.

Authors:  Hai Xiao; Yong Mao; Shyamal D Desai; Nai Zhou; Chun-Yuan Ting; Jaulang Hwang; Leroy F Liu
Journal:  Proc Natl Acad Sci U S A       Date:  2003-03-10       Impact factor: 11.205

3.  The SUMO pathway is required for selective degradation of DNA topoisomerase IIbeta induced by a catalytic inhibitor ICRF-193(1).

Authors:  Sevim Isik; Kuniaki Sano; Kimiko Tsutsui; Masayuki Seki; Takemi Enomoto; Hisato Saitoh; Ken Tsutsui
Journal:  FEBS Lett       Date:  2003-07-10       Impact factor: 4.124

4.  Synergistic blockade of mitotic exit by two chemical inhibitors of the APC/C.

Authors:  Katharine L Sackton; Nevena Dimova; Xing Zeng; Wei Tian; Mengmeng Zhang; Timothy B Sackton; Johnathan Meaders; Kathleen L Pfaff; Frederic Sigoillot; Hongtao Yu; Xuelian Luo; Randall W King
Journal:  Nature       Date:  2014-08-24       Impact factor: 49.962

5.  Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha.

Authors:  Meelad M Dawlaty; Liviu Malureanu; Karthik B Jeganathan; Esther Kao; Claudio Sustmann; Samuel Tahk; Ke Shuai; Rudolf Grosschedl; Jan M van Deursen
Journal:  Cell       Date:  2008-04-04       Impact factor: 41.582

6.  Conjugation of human topoisomerase 2 alpha with small ubiquitin-like modifiers 2/3 in response to topoisomerase inhibitors: cell cycle stage and chromosome domain specificity.

Authors:  Marta Agostinho; Vera Santos; Fernando Ferreira; Rafael Costa; Joana Cardoso; Inês Pinheiro; José Rino; Ellis Jaffray; Ronald T Hay; João Ferreira
Journal:  Cancer Res       Date:  2008-04-01       Impact factor: 12.701

7.  The retinoblastoma tumor suppressor protein is required for efficient processing and repair of trapped topoisomerase II-DNA-cleavable complexes.

Authors:  Hai Xiao; David W Goodrich
Journal:  Oncogene       Date:  2005-12-08       Impact factor: 9.867

Review 8.  The Ubiquitin-Proteasome System: Potential Therapeutic Targets for Alzheimer's Disease and Spinal Cord Injury.

Authors:  Bing Gong; Miroslav Radulovic; Maria E Figueiredo-Pereira; Christopher Cardozo
Journal:  Front Mol Neurosci       Date:  2016-01-26       Impact factor: 5.639

9.  The E3 ubiquitin-ligase Bmi1/Ring1A controls the proteasomal degradation of Top2alpha cleavage complex - a potentially new drug target.

Authors:  Iris Alchanati; Carmit Teicher; Galit Cohen; Vivian Shemesh; Haim M Barr; Philippe Nakache; Danny Ben-Avraham; Anna Idelevich; Itzchak Angel; Nurit Livnah; Shmuel Tuvia; Yuval Reiss; Daniel Taglicht; Omri Erez
Journal:  PLoS One       Date:  2009-12-01       Impact factor: 3.240

10.  Evaluating the Mechanism and Therapeutic Potential of PTC-028, a Novel Inhibitor of BMI-1 Function in Ovarian Cancer.

Authors:  Anindya Dey; Xunhao Xiong; Aleia Crim; Shailendra Kumar Dhar Dwivedi; Soumyajit Banerjee Mustafi; Priyabrata Mukherjee; Liangxian Cao; Nadiya Sydorenko; Ramil Baiazitov; Young-Choon Moon; Melissa Dumble; Thomas Davis; Resham Bhattacharya
Journal:  Mol Cancer Ther       Date:  2017-11-20       Impact factor: 6.261

View more
  1 in total

Review 1.  Natural Products Against Renal Fibrosis via Modulation of SUMOylation.

Authors:  Peng Liu; Jing Zhang; Yun Wang; Chen Wang; Xinping Qiu; Dan-Qian Chen
Journal:  Front Pharmacol       Date:  2022-03-04       Impact factor: 5.810

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.