REGULATION OF MEMBRANE TRAFFICKING BY BAR/F-BAR DOMAIN-CONTAINING PROTEINS

Cornell University, Ithaca NY

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Abstract

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The ability of cells to maintain and change the shapes of their membranes is vital for many cellular processes. Peripheral and membrane-spanning proteins have been identified as membrane remodelers involved in endocytosis and in shaping organellar structures, and mutations in these proteins have been linked to various neurological and developmental disease states. The formation of vesicles at the plasma membrane is mediated by proteins that sense or induce membrane curvature, enzymes such as Dynamin that catalyze the final fission step, and the actin cytoskeleton. A major class of membrane curvature sensing and inducing proteins contain BAR domains or related folds (e.g. F-BAR). In vitro and in cells, these proteins facilitate the tubulation of membranes, and are involved in endocytosis and membrane trafficking. We study the structure and function of BAR and F-BAR containing proteins using a combination of X-ray crystallography, small angle X-Ray scattering and other biophysical approaches. The results will shed light on the specific functions and mode of regulation of these proteins.