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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains.
EMBO Rep. 11, 279-284 (2010)
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
Language
english
Publication Year
2010
HGF-reported in Year
0
ISSN (print) / ISBN
1469-221X
e-ISSN
1469-3178
Journal
EMBO Reports
Quellenangaben
Volume: 11,
Issue: 4,
Pages: 279-284
Publisher
EMBO Press
Reviewing status
Peer reviewed
Institute(s)
Institute of Pancreatic Islet Research (IPI)
PubMed ID
20300118
Erfassungsdatum
2010-12-31