Researchers from the Shanghai Institute of Materia Medica, Chinese Academy of Sciences confirmed in a new study that O-GlcNAc glycosylation (O-GlcNAcylation) of the actin-binding protein Cofilin promotes breast cancer cell invasion. Related research papers were published in the Journal of Biochemistry (JBC) on November 8.
Researcher Jian Ding, academician of the Chinese Academy of Engineering, director of the Shanghai Institute of Materia Medica, and researcher Meiyu Geng, deputy director, are co-corresponding authors of this paper. Academician Ding's main research directions include tumor neovascularization inhibitors; kinase inhibitors; PI3K-mTOR inhibitors; anti-tumor metastasis studies; epigenetics; tumor biomarkers. The research directions of Geng Meiyu's research group include receptor tyrosine kinases c-Met, ALK, FGFR inhibitors; tumor metabolism; microenvironment, EMT and tumor metastasis; tumor biomarkers.
Breast cancer is the malignant tumor with the highest morbidity and mortality among women worldwide. Nearly 1.3 million women suffer from breast cancer each year, and more than 400,000 women die due to the recurrence of breast cancer. Exploring the molecular mechanism of breast cancer invasion and metastasis can not only predict the high-risk factors for breast cancer recurrence and metastasis, but also may guide the individualized treatment of breast cancer and provide a theoretical basis for the development of targeted therapeutic drugs.
Proteins are the executive bodies of life activities. The functions of many proteins in cells are achieved through dynamic post-translational modification of proteins. There are more than 20 kinds of post-translational modification processes in eukaryotic animal cells, common ones include ubiquitination, phosphorylation, glycosylation, lipidation, methylation and acetylation. O-GlcNAc glycosylation modification, as a special post-translational modification of protein, is an important regulator of many cellular processes such as signal transduction, transcription and proteasome degradation, and participates in the regulation of proliferation, differentiation, adhesion and apoptosis. Multiple biological functions.
Cofilin is an actin-binding protein that is ubiquitous in eukaryotic cells. The basic function of Cofilin is to bind and depolymerize F-actin (F-actin) in cells, and its activity can be adjusted by phosphorylation, dephosphorylation, phosphoinositide, pH change, etc. Cofilin mediates intracellular signaling pathways, thereby regulating the reorganization of the actin skeleton, plays an important role in cell migration, and is closely related to cancer metastasis. In a variety of cancer cells, Cofilin is subject to complex regulation.
In this article, the researchers confirmed that O-GlcNAc glycosyltransferase (O-GlcNAc transferase, OGT) can glycosylate cofilin O-GlcNAc, and cofilin mediates changes in cell movement related to OGT. Cofilin's Ser108 site O-GlcNAc glycosylation is a necessary condition for the proper function of cofilin in the invasion of breast cancer cell leading edge invadopodia during cell invasion. Cofilin does not undergo O-GlcNAc glycosylation modification, which will cause the invasive pseudopod to lose stability and damage cancer cell invasion.
New research reveals a post-translational modification mechanism of cofilin function, confirming that the abnormal O-GlcNAc glycosylation of cofilin has an important effect on cancer metastasis.
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