title: A novel twist in membrane dePHormation.
abstract: Bin-Amphiphysin-Rvs (BAR) domain-containing proteins form oligomeric assemblies that aid membrane remodeling. In this issue of Developmental Cell, Pang et al. (2014) show that the BAR domain of ACAP1, although architecturally similar to other BAR domains, cooperates with its neighboring pleckstrin homology domain to deform membranes and facilitate endosomal recycling.
authors.affiliation: Leibniz Institut für Molekulare Pharmakologie (FMP), Robert-Roessle-Straße 10, 13125 Berlin, Germany. Electronic address: krauss@fmp-berlin.de.
authors.forename: Michael
authors.initials: M
authors.lastname: Krauss
authors.affiliation: Leibniz Institut für Molekulare Pharmakologie (FMP), Robert-Roessle-Straße 10, 13125 Berlin, Germany. Electronic address: haucke@fmp-berlin.de.
authors.forename: Volker
authors.initials: V
authors.lastname: Haucke
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D020690:GTPase-Activating Proteins / Q000737:chemistry*; D006801:Humans
chemical_list: C507017:ACAP1 protein, human; D020690:GTPase-Activating Proteins