Abstract
Dynamin, the prototypical member of the dynamin-superfamily of membrane-remodelling proteins, catalyses membrane fission during clathrin-mediated endocytosis. Understanding dynamin polymerization is crucial for our understanding of protein-catalysed membrane fission and its deregulation in various diseases. Existing cryo-EM reconstructions of dynamin polymers provide a limited understanding of the underlying dynamics and the regulatory mechanisms of dynamin polymerization. Here we combine mass photometry (MP) based mass measurement with dynamic mass photometry (DMP) derived mass and diffusion estimation on membranes, to study dynamin polymerization and its regulation.
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