Sorkin Lab
Welcome!
We are interested in life processes that involve deformation and remodeling of membranes, such as viral infection, cell-cell fusion in fertilization, and cell-cell communication by vesicles such as migrasomes. In order to gain insight into membrane remodeling in such processes, we use mechanical single-molecule techniques: Optical Tweezers in combination with confocal fluorescence microscopy and Atomic Force Microscopy (AFM). Our research is highly multidisciplinary, combining Biology, Chemistry, Physics and some engineering to modify our tools according to the experimental needs, and we also work in close collaboration with biologists and theorists. Our tools allow us to measure membrane mechanical properties and to explore the interactions between membranes and proteins in bio-mimetic model systems and cells. By such quantitative measurements, we hope to contribute to the understanding of biological processes in which membranes play a central role.
We published two review papers:
Biophysical Aspects of Migrasome Organelle Formation and their Diverse Cellular Functions, Dharan R., Sorkin R., BioEssays, (2024), https://doi.org/10.1002/bies.202400051
Tetraspanin proteins in membrane remodeling processes, Dharan R., Sorkin R., Journal of Cell Science, J Cell Sci (2024) 137 (14): jcs261532, (2024) https://doi.org/10.1242/jcs.261532,
New Paper! Congratulations, Raviv and Alisa!
Tetraspanin 4 is a protein that can detect membrane curvature and accumulate in highly curved membranes. We studied how different parts of this protein contribute to its ability to sense curvature. We found that a specific part of the protein - the second extracellular loop - plays a crucial role. When we removed this loop, the protein's ability to detect curved membranes and interact with other proteins was significantly reduced. This suggests that EC2 is crucial for modulating TSPANs' biological functions, given that their mode of action is closely tied to molecular interactions and membrane domain formation.
New Paper! Congratulations, Alisa and Alon!
We studied the interaction between the activated fusion protein of Ebola and a target membrane using optical tweezers and single-particle tracking. We showed very strong, receptor-independent binding likely resulting from the interaction between the glycoprotein (GP) fusion loop and the membrane’s hydrophobic core. This approach offers a powerful toolkit for studying other protein−membrane interactions, and can be used to enhance our understanding of protein-mediated membrane fusion events.