BMB Reports 2019; 52(2): 113-118
Regulation of post-translational modification in breast cancer treatment
Kyung-Sun Heo*
College of Pharmacy and Institute of Drug Research and Development, Chungnam National University, Daejeon 34134, Korea
Correspondence to: Tel: +82-42-821-5927; Fax: +82-42-822-5343; E-mail:
Received: November 1, 2018; Published online: February 28, 2019.
© Korean Society for Biochemistry and Molecular Biology. All rights reserved.

cc This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
The small ubiquitin-related modification molecule (SUMO), one of the post-translational modification molecules, is involved in a variety of cellular functions where it regulates protein activity and stability, transcription, and cell cycling. Modulation of protein SUMOylation or deSUMOylation modification has been associated with regulation of carcinogenesis in breast cancer. In the dynamic processes of SUMOylation and deSUMOylation in a variety of cancers, SUMO proteases (SENPs), reverse SUMOylation by isopeptidase activity and SENPs are mostly elevated, and are related to poor patient prognosis. Although underlying mechanisms have been suggested for how SENPs participate in breast cancer tumorigenesis, such as through regulation of target protein transactivation, cancer cell survival, cell cycle, or other post-translational modification-related machinery recruitment, the effect of SENP isoform-specific inhibitors on the progression of breast cancer have not been well evaluated. This review will introduce the functions of SENP1 and SENP2 and the underlying signaling pathways in breast cancer for use in discovery of new biomarkers for diagnosis or therapeutic targets for treatment.
Keywords: Breast cancer, Post-translational modification, SENP, SUMOylation
Fig. 1. The scheme of SUMOylation and deSUMOylation pathway. (A) Protein SUMOylation is associated with a recycling system
consisting of conjugation and deconjugation pathways. Both conjugation and deconjugation enzymes mediate the dynamic and reversible process of SUMOylation. The protein SUMOylation alters protein activation, transcriptional activity, stability, and localization change. (B) SUMO proteins covalently modify certain residues of specific target substrates and change the function of these substrates. The conjugation pathway is mediated by SUMO E1, E2, E3 enzymes, whereas the deconjugation pathway is mediated by SUMOisopeptidase, SENPs.

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