4BNE
Pacsin2 Interacts with Membranes and Actin-Filaments
Summary for 4BNE
Entry DOI | 10.2210/pdb4bne/pdb |
Descriptor | PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 2, SULFATE ION, TRIETHYLENE GLYCOL, ... (4 entities in total) |
Functional Keywords | endocytosis, membrane sculpting, f- actin binding |
Biological source | GALLUS GALLUS (CHICKEN) |
Cellular location | Cell junction, focal adhesion : O13154 |
Total number of polymer chains | 2 |
Total formula weight | 106784.23 |
Authors | Kostan, J.,Salzer, U.,Orlova, A.,Toeroe, I.,Hodnik, V.,Schreiner, C.,Merilainen, J.,Nikki, M.,Virtanen, I.,Lehto, V.-P.,Anderluh, G.,Egelman, E.H.,Djinovic-Carugo, K. (deposition date: 2013-05-15, release date: 2014-05-14, Last modification date: 2024-05-08) |
Primary citation | 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, V.,Anderluh, G.,Egelman, E.H.,Djinovic-Carugo, K. Direct Interaction of Actin Filaments with F-Bar Protein Pacsin2. Embo Rep., 15:1154-, 2014 Cited by PubMed Abstract: 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. PubMed: 25216944DOI: 10.15252/EMBR.201439267 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.57 Å) |
Structure validation
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