Ubiquitination and deubiquitination of MCL1 in cancer: deciphering chemoresistance mechanisms and providing potential therapeutic options.

Cell Death & Disease
Xiaowei WuZhihua Liu

Abstract

MCL1 is an important antiapoptotic member of the BCL-2 family that is distinguishable from other family members based on its relatively short half-life. Emerging studies have revealed the crucial role of MCL1 in the chemoresistance of cancer cells. The antiapoptotic function of MCL1 makes it a popular therapeutic target, although specific inhibitors have begun to emerge only recently. Notably, emerging studies have reported that several E3 ligases and deubiquitinases modulate MCL1 stability, providing an alternate means of targeting MCL1 activity. In addition, the emergence and development of proteolysis-targeting chimeras, the function of which is based on ubiquitination-mediated degradation, has shown great potential. In this review, we provide an overview of the studies investigating the ubiquitination and deubiquitination of MCL1, summarize the latest evidence regarding the development of therapeutic strategies targeting MCL1 in cancer treatment, and discuss the promising future of targeting MCL1 via the ubiquitin-proteasome system in clinical practice.

References

Apr 3, 1992·Cell·G I EvanD C Hancock
Oct 25, 1991·Nucleic Acids Research·M BonfantiM D'Incalci
Apr 15, 1993·Proceedings of the National Academy of Sciences of the United States of America·K M KozopasR W Craig
Aug 28, 1998·Science·D R Green, J C Reed
Oct 6, 1998·Annual Review of Biochemistry·A Hershko, A Ciechanover
Apr 17, 2001·Trends in Microbiology·B T Cookson, M A Brennan
Sep 5, 2002·Nature Reviews. Drug Discovery·Andrew L Hopkins, Colin R Groom
Nov 25, 2003·Genes & Development·Andrea CuconatiEileen White
Dec 12, 2003·Nature·Joseph T OpfermanStanley J Korsmeyer
Mar 5, 2004·Biochimica Et Biophysica Acta·Andrew M PetrosStephen W Fesik
Apr 3, 2004·Nature Reviews. Drug Discovery·Michelle R Arkin, James A Wells
May 4, 2004·Nature Reviews. Molecular Cell Biology·Jessica A Downs, Stephen P Jackson
Feb 19, 2005·Science·Joseph T OpfermanStanley J Korsmeyer
Oct 11, 2005·FEBS Letters·Matthew R WarrGordon C Shore
Nov 18, 2005·Journal of Hepatology·Wolfgang SieghartVolker Wacheck
Jan 13, 2006·Nature Chemical Biology·Alexei DegterevJunying Yuan
Jun 15, 2007·Toxicologic Pathology·Susan Elmore
Sep 8, 2007·The Journal of Biological Chemistry·Marc Germain, Vincent Duronio
May 23, 2008·Molecular Biology of the Cell·Sarwat JamilVincent Duronio
Jun 21, 2008·The Journal of Immunology : Official Journal of the American Association of Immunologists·Ivan DzhagalovYou-Wen He
Dec 17, 2008·Annals of the New York Academy of Sciences·Shaida A AndrabiValina L Dawson
Jan 8, 2009·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Binje VickHenning Schulze-Bergkamen
Jul 25, 2009·Nature Reviews. Molecular Cell Biology·David KomanderSylvie Urbé
Aug 14, 2009·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Hayato HikitaNorio Hayashi
Dec 22, 2009·Nature·Martin SchwickartVishva M Dixit
Jan 16, 2010·Pediatric Research·Kathleen M Sakamoto
Jan 26, 2010·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·Achim WeberHenning Schulze-Bergkamen
Feb 19, 2010·Nature·Rameen BeroukhimMatthew Meyerson
Mar 17, 2010·Nature Cell Biology·Yaron PeregVishva M Dixit
Dec 15, 2010·Biochimica Et Biophysica Acta·Aisha Shamas-DinDavid W Andrews

❮ Previous
Next ❯

Citations

Jan 29, 2021·Cellular Signalling·Shujing LiHuijian Wu
Dec 15, 2020·Journal of Hematology & Oncology·Arnold BolomskyJo Caers
Feb 19, 2021·Biochimica Et Biophysica Acta. Molecular Cell Research·Sarah Kehr, Meike Vogler
Apr 1, 2021·Cell Death and Differentiation·Kirsteen J CampbellStephen W G Tait
Jun 3, 2021·Cells·Meenakshi Basu-ShrivastavaIréna Lassot
Aug 3, 2021·International Journal of Biological Macromolecules·Pooja MittalIndrakant Kumar Singh
Sep 4, 2021·Communications Biology·Hayley Widden, William J Placzek

❮ Previous
Next ❯

Methods Mentioned

BETA
deubiquitinases
ubiquitination
ubiquitinate
deubiquitination
antisense oligonucleotide
xenograft

Related Concepts

Related Feeds

BCL-2 Family Proteins

BLC-2 family proteins are a group that share the same homologous BH domain. They play many different roles including pro-survival signals, mitochondria-mediated apoptosis and removal or damaged cells. They are often regulated by phosphorylation, affecting their catalytic activity. Here is the latest research on BCL-2 family proteins.

Related Papers

OncoTargets and Therapy
Weiguo XiangLongchuan Bai
Journal of Hematology & Oncology
Haolan WangYongheng Chen
Pharmacology & Therapeutics
Johannes Belmar, Stephen W Fesik
© 2021 Meta ULC. All rights reserved