8P94
Cryo-EM structure of cortactin stabilized Arp2/3-complex nucleated actin branches
This is a non-PDB format compatible entry.
Summary for 8P94
| Entry DOI | 10.2210/pdb8p94/pdb |
| EMDB information | 17553 17554 17555 17556 17557 17558 |
| Related PRD ID | PRD_002366 |
| Descriptor | Actin-related protein 3, F-actin-capping protein subunit alpha-1, Isoform 2 of F-actin-capping protein subunit beta, ... (14 entities in total) |
| Functional Keywords | complex, contractile protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 30 |
| Total formula weight | 781196.33 |
| Authors | Liu, T.,Moores, C.A. (deposition date: 2023-06-05, release date: 2024-01-03, Last modification date: 2024-05-29) |
| Primary citation | Liu, T.,Cao, L.,Mladenov, M.,Jegou, A.,Way, M.,Moores, C.A. Cortactin stabilizes actin branches by bridging activated Arp2/3 to its nucleated actin filament. Nat.Struct.Mol.Biol., 31:801-809, 2024 Cited by PubMed Abstract: 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. PubMed: 38267598DOI: 10.1038/s41594-023-01205-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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