Professor Suetsugu and his colleagues have been studying protein modules, which are the parts of the structure of protein molecules that have the function of forming the morphogenesis of biological membranes, called the "BAR domain." The BAR domain is a protein domain that regulates the morphology of biological membranes by gathering proteins on the biological membrane and forming a shape that stacks blocks.

　This time, we analyzed the BAR domain contained in the protein "GAS7".As a result, the research group determined the three-dimensional structure of this protein.Furthermore, when we investigated how GAS7 gathers like blocks and functions in phagocytosis cups, we found that they form a planar aggregate suitable for the formation of phagocytosis cups, which occupy a relatively large part of cells. I found it.

　In addition, the research group found that this set can be reconstructed in vitro and that a similar set can be seen in the actual fagocytosis cup, including super-resolution imaging, mathematical model analysis, and biochemistry / cell biology. It was clarified in detail by the analysis.

　This will elucidate a mechanism that was previously unknown as the mechanism of phagocytosis cup formation, and deepen the fundamental understanding of life as well as the immune response mechanism.At the same time, detailed molecular mechanisms will pave the way for future functional manipulation of immune cells and the like.

Paper information:[Nature Communications] Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7