Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains (pages 279–284)
Marc Lenoir, Ünal Coskun, Michal Grzybek, Xinwang Cao, Sabine B Buschhorn, Jonathan James, Kai Simons and Michael Overduin
Version of Record online: 19 MAR 2010 | DOI: 10.1038/embor.2010.28
Overduin and colleagues present the NMR structures of free, micelle and PtdIns(4)P-bound FAPP1-PH domain. The micelle-bound structure reveals how its prominent wedge independently tubulates Golgi membranes by leaflet penetration. A hydrophobic element inserts into and bends membranes, and is conserved in pleckstrin homology domains of CERT and OSBP proteins.