Article abstract
Nature Structural & Molecular Biology 14, 138 - 146 (2007)
Published online: 14 January 2007 | doi:10.1038/nsmb1194
A general amphipathic 
-helical motif for sensing membrane curvature
Guillaume Drin1, Jean-François Casella1, Romain Gautier1, Thomas Boehmer2, Thomas U Schwartz2 & Bruno Antonny1
Abstract
The Golgi-associated protein ArfGAP1 has an unusual membrane-adsorbing amphipathic 
-helix: its polar face is weakly charged, containing mainly serine and threonine residues. We show that this feature explains the specificity of ArfGAP1 for curved versus flat lipid membranes. We built an algorithm to identify other potential amphipathic -helices rich in serine and threonine residues in protein databases. Among the identified sequences, we show that three act as membrane curvature sensors. In the golgin GMAP-210, the sensor may serve to trap small vesicles at the end of a long coiled coil. In Osh4p/Kes1p, which transports sterol between membranes, the sensor controls access to the sterol-binding pocket. In the nucleoporin Nup133, the sensor corresponds to an exposed loop of a 
-propeller structure. Ser/Thr-rich amphipathic helices thus define a general motif used by proteins of various functions for sensing membrane curvature.
- Centre National de la Recherche Scientifique (CNRS), Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis, 06560 Valbonne, France.
- Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Ave, Cambridge, Massachusetts 02139, USA.
Correspondence to: Bruno Antonny1 e-mail: antonny@ipmc.cnrs.fr
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