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Overexpression and purification of the c-terminal domain of SH2D3C in escherichia coli

Protein-protein interactions are crucial for many cellular processes and their research allows us to understand these processes from a biochemical point of view. Since changes in the regulation of signaling pathways in the cell often lead to the development of various diseases, studying protein- protein interactions can help us better understand their origin, development and impact on human health. SH2D3C acts as an adapter protein in signaling pathways involved in cell adhesion and migration, tissue organization, and regulation of the immune response. The protein contains a Ras GEF-like C-terminal domain that has no significant GEF activity, but may interact with other proteins. Analysis of the cellular proteome by SILAC-MS revealed a potential interaction of SH2D3C with dipeptidyl peptidase III (DPP III) involved in the regulation of oxidative stress by competitively binding to the KEAP1 protein which is a key participant in the Nrf2/KEAP1 signaling pathway. This would mean that their interaction represents a possible link between the Nrf2/KEAP1 signaling pathway and cell migration regulation. To confirm the interaction by other methods such as micro-scale thermophoresis (MST), the C- terminal domain of SH2D3C was overexpressed and purified in E. coli with two different tags, GST and MBP.

SH2D3C, DPP3, protein expression

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