PMID- 30638182 OWN - NLM STAT- MEDLINE DCOM- 20190617 LR - 20200225 IS - 1976-670X (Electronic) IS - 1976-6696 (Print) IS - 1976-6696 (Linking) VI - 52 IP - 2 DP - 2019 Feb TI - Regulation of post-translational modification in breast cancer treatment. PG - 113-118 AB - 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. [BMB Reports 2019; 52(2): 113-118]. FAU - Heo, Kyung-Sun AU - Heo KS AD - College of Pharmacy and Institute of Drug Research and Development, Chungnam National University, Daejeon 34134, Korea. LA - eng PT - Journal Article PT - Review PL - Korea (South) TA - BMB Rep JT - BMB reports JID - 101465334 RN - 0 (Small Ubiquitin-Related Modifier Proteins) RN - EC 3.4.- (Peptide Hydrolases) RN - EC 3.4.- (SENP1 protein, human) RN - EC 3.4.22.- (Cysteine Endopeptidases) RN - EC 3.4.22.- (SENP2 protein, human) SB - IM EIN - BMB Rep. 2019 Dec;52(12):728. PMID: 31878989 MH - Breast Neoplasms/*genetics/metabolism MH - Cysteine Endopeptidases/metabolism MH - Female MH - Humans MH - Peptide Hydrolases/metabolism MH - Protein Processing, Post-Translational/genetics/physiology MH - Signal Transduction MH - Small Ubiquitin-Related Modifier Proteins/genetics/metabolism MH - Sumoylation/*physiology PMC - PMC6443327 COIS- CONFLICTS OF INTEREST The authors have no conflicting interests. EDAT- 2019/01/15 06:00 MHDA- 2019/06/18 06:00 PMCR- 2019/03/01 CRDT- 2019/01/15 06:00 PHST- 2018/11/01 00:00 [received] PHST- 2019/01/15 06:00 [pubmed] PHST- 2019/06/18 06:00 [medline] PHST- 2019/01/15 06:00 [entrez] PHST- 2019/03/01 00:00 [pmc-release] AID - 4499 [pii] AID - bmb-52-113 [pii] AID - 10.5483/BMBRep.2019.52.2.017 [doi] PST - ppublish SO - BMB Rep. 2019 Feb;52(2):113-118. doi: 10.5483/BMBRep.2019.52.2.017.