Going on a (Membrane) Bender to the F-BAR

Abstract

This study is a personal favorite because it simplified the field and proposed an elegant model of how actin and membranes work together in endocytic trafficking. A group of proteins containing FCH domains (Fes/CIP4 homology) were discovered to have extended homology with the banana-shaped alpha helical BAR domain and renamed F-BAR proteins. F-BAR and BAR proteins bind to and bend curved membrane surfaces and participate in budding and tubulation events. Dynamin, a large GTPase that forms helical cages around tubulated membranes, is the main partner of BAR and F-BAR proteins. The actin cytoskeleton opposes scission of the tubulated membranes pending arrival of an appropriate signal. The idea that dynamin is the most important partner of F-BARs and that the trio of actin, F-BAR, and dynamin sculpt and cut membrane tubules in this elegant way remains important for future research and puts into context the barrage of sometimes disparate studies on these proteins. This PaperPick refers to and the Actin Cytoskeleton Cooperatively Regulate Plasma Membrane Invagination by BAR and F-BAR Proteins by T. Itoh, K.S. Erdmann, A. Roux, B. Habermann, H. Werner, and P. De Camilli, published in December, 2005. F-BAR Proteins: Coordinating the Effects of Actin and Dynamin on Endocytosis Pietro De Camilli discusses how his group came to define the F-BAR domain, its role in endocytosis, and where subsequent work has taken the field.