4bne

Pacsin2 Interacts with Membranes and Actin-Filaments

spinqualitylabelsall models 4bne, resolution 2.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bne is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.57Å Ligands: PGE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PACN2_CHICK Publication Abstract from PubMed Two mechanisms have emerged as major regulators of membrane shape: BAR domain-containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes. While a large body of information exists on interactions of BAR proteins with membranes and regulatory proteins of the cytoskeleton, little is known about connections between these two processes. Here, we show that the F-BAR domain protein pacsin2 is able to associate with actin filaments using the same concave surface employed to bind to membranes, while some other tested N-BAR and F-BAR proteins (endophilin, CIP4 and FCHO2) do not associate with actin. This finding reveals a new level of complexity in membrane remodeling processes. Direct interaction of actin filaments with F-BAR protein pacsin2.,Kostan J, Salzer U, Orlova A, Toro I, Hodnik V, Senju Y, Zou J, Schreiner C, Steiner J, Merilainen J, Nikki M, Virtanen I, Carugo O, Rappsilber J, Lappalainen P, Lehto VP, Anderluh G, Egelman EH, Djinovic-Carugo K EMBO Rep. 2014 Sep 12. pii: e201439267. PMID:25216944 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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