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4BNE

Pacsin2 Interacts with Membranes and Actin-Filaments

Summary for 4BNE
Entry DOI10.2210/pdb4bne/pdb
DescriptorPROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 2, SULFATE ION, TRIETHYLENE GLYCOL, ... (4 entities in total)
Functional Keywordsendocytosis, membrane sculpting, f- actin binding
Biological sourceGALLUS GALLUS (CHICKEN)
Cellular locationCell junction, focal adhesion : O13154
Total number of polymer chains2
Total formula weight106784.23
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 citationKostan, 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: 25216944
DOI: 10.15252/EMBR.201439267
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.57 Å)
Structure validation

226707

건을2024-10-30부터공개중

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