8p94

Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches

spinqualitylabelsall models 8p94, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8p94 is a 28 chain structure with sequence from Amanita phalloides, Homo sapiens, Mus musculus and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: ADP, DTH, EEP, HYP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ARP5L_HUMAN May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Publication Abstract from PubMed Regulation of the assembly and turnover of branched actin filament networks nucleated by the Arp2/3 complex is essential during many cellular processes, including cell migration and membrane trafficking. Cortactin is important for actin branch stabilization, but the mechanism by which this occurs is unclear. Given this, we determined the structure of vertebrate cortactin-stabilized Arp2/3 actin branches using cryogenic electron microscopy. We find that cortactin interacts with the new daughter filament nucleated by the Arp2/3 complex at the branch site, rather than the initial mother actin filament. Cortactin preferentially binds activated Arp3. It also stabilizes the F-actin-like interface of activated Arp3 with the first actin subunit of the new filament, and its central repeats extend along successive daughter-filament subunits. The preference of cortactin for activated Arp3 explains its retention at the actin branch and accounts for its synergy with other nucleation-promoting factors in regulating branched actin network dynamics. Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament.,Liu T, Cao L, Mladenov M, Jegou A, Way M, Moores CA Nat Struct Mol Biol. 2024 May;31(5):801-809. doi: 10.1038/s41594-023-01205-2. , Epub 2024 Jan 24. PMID:38267598 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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