7RWC
AP2 bound to the APA domain of SGIP and heparin; partial signal subtraction and symmetry expansion
Summary for 7RWC
| Entry DOI | 10.2210/pdb7rwc/pdb |
| EMDB information | 24714 |
| Descriptor | AP-2 complex subunit alpha-2, AP-2 complex subunit beta, AP-2 complex subunit mu, ... (5 entities in total) |
| Functional Keywords | ap2, clathrin vesicle, endocytosis, lipid-binding, adaptor, membrane, transport, muniscin, regulator |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 5 |
| Total formula weight | 204990.70 |
| Authors | Baker, R.W.,Hollopeter, G.,Partlow, E.A. (deposition date: 2021-08-19, release date: 2022-03-30, Last modification date: 2024-06-05) |
| Primary citation | Partlow, E.A.,Cannon, K.S.,Hollopeter, G.,Baker, R.W. Structural basis of an endocytic checkpoint that primes the AP2 clathrin adaptor for cargo internalization. Nat.Struct.Mol.Biol., 29:339-347, 2022 Cited by PubMed Abstract: Clathrin-mediated endocytosis (CME) is the main route of internalization from the plasma membrane. It is known that the heterotetrameric AP2 clathrin adaptor must open to simultaneously engage membrane and endocytic cargo, yet it is unclear how transmembrane cargos are captured to catalyze CME. Using cryogenic-electron microscopy, we discover a new way in which mouse AP2 can reorganize to expose membrane- and cargo-binding pockets, which is not observed in clathrin-coated structures. Instead, it is stimulated by endocytic pioneer proteins called muniscins, which do not enter vesicles. Muniscin-engaged AP2 is primed to rearrange into the vesicle-competent conformation on binding the tyrosine cargo internalization motif (YxxΦ). We propose adaptor priming as a checkpoint to ensure cargo internalization. PubMed: 35347313DOI: 10.1038/s41594-022-00749-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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