Regulation of post-translational modification in breast cancer treatment.

Abstract

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].

• Authors: Kyung-Sun Heo
• Journal: BMB reports (BMB Rep) Vol. 52 Issue 2 Pg. 113-118 (Feb 2019) ISSN: 1976-670X [Electronic] Korea (South)
• PMID: 30638182 (Publication Type: Journal Article, Review)

Chemical References

• Small Ubiquitin-Related Modifier Proteins
• Peptide Hydrolases
• SENP1 protein, human
• Cysteine Endopeptidases
• SENP2 protein, human

Topics

• Breast Neoplasms (genetics, metabolism)
• Cysteine Endopeptidases (metabolism)
• Female
• Humans
• Peptide Hydrolases (metabolism)
• Protein Processing, Post-Translational (genetics, physiology)
• Signal Transduction
• Small Ubiquitin-Related Modifier Proteins (genetics, metabolism)
• Sumoylation (physiology)