 |
PDBsum entry 2kcj
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
2kcj
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis of wedging the golgi membrane by fapp pleckstrin homology domains.
|
|
|
Authors
|
|
M.Lenoir,
U.Coskun,
M.Grzybek,
X.Cao,
S.B.Buschhorn,
J.James,
K.Simons,
M.Overduin.
|
|
|
Ref.
|
|
Embo Rep, 2010,
11,
279-284.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
