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Lenoir, M.* ; Coskun, Ü.* ; Grzybek, M.* ; Cao, X.* ; Buschhorn, S.B.* ; James, J.* ; Simons, K.* ; Overduin, M.*

Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains.

EMBO Rep. 11, 279-284 (2010)
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Open Access Green as soon as Postprint is submitted to ZB.
The mechanisms underlying Golgi targeting and vesiculation are unknown, although the responsible phosphatidylinositol 4-phosphate (PtdIns(4)P) ligand and four-phosphate-adaptor protein (FAPP) modules have been defined. The micelle-bound structure of the FAPP1 pleckstrin homology domain reveals how its prominent wedge independently tubulates Golgi membranes by leaflet penetration. Mutations compromising the exposed hydrophobicity of full-length FAPP2 abolish lipid monolayer binding and compression. The trafficking process begins with an electrostatic approach, phosphoinositide sampling and perpendicular penetration. Extensive protein contacts with PtdIns(4)P and neighbouring phospholipids reshape the bilayer and initiate tubulation through a conserved wedge with features shared by diverse protein modules.
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Publication type Article: Journal article
Document type Scientific Article
ISSN (print) / ISBN 1469-221X
e-ISSN 1469-3178
Journal EMBO Reports
Quellenangaben Volume: 11, Issue: 4, Pages: 279-284 Article Number: , Supplement: ,
Publisher EMBO Press
Reviewing status Peer reviewed
Institute(s) Institute for Pancreatic Beta Cell Research (IPI)