By acting as containment structures and dividing the intracellular region from the external environment, cell membranes serve a crucial role. Proteins having unique functional units are essential for promoting interactions between proteins and membranes. For instance, proteins with “Bin-Amphiphysin-Rvs” (“BAR”) domains are important in controlling the curvature of cell membranes. Endocytosis and cell motility are two biologically significant processes that are made possible by the physical bending of cell membranes. Although BAR proteins form highly organized oligomeric units that cause membrane curvature, the exact mechanism that controls this behavior is still completely unclear.
Recently, a study conducted by scientists in Japan identified the mechanism governing the oligomeric assembly of a protein with a BAR domain on membrane surfaces. Shiro Suetsugu served as the study’s principal investigator, and WanNhung Thi Hong Nguyen and Nurul Izzati Wan Mohamad Noor are both scientists of the Nara Institute of Science and Technology (NAIST).
Suetsugu comments on the work, saying, “It is challenging to evaluate the assembly of the relatively few oligomeric BAR domains on thin membrane tubules. Because oligomeric GAS7 protein assembles into larger than the others, we used fluorescence resonance energy transfer monitoring to study the oligomeric assembly of the protein.
Fluorescence resonance energy transfer, or FRET, was used by the researchers to clarify the process underlying the assembly of GAS7 on membrane surfaces. In order to track the scope and time of GAS7 assembly, the researchers used fluorescent protein tags to designate GAS7b units. Fluorescence emission was seen, which showed that GAS7 had assembled on lipid.