AP-2 is the class of clathrin-associated protein complex found in coated vesicles derived from the plasma membrane of eukaryotic cells. We demonstrate here, using a chemical method, that an AP-2 complex is an asymmetric structure consisting of one large α chain, one large β chain, one medium AP50 chain, and one small AP17 chain. The complex has been shown to contain a core and two appendages. The AP core includes the small AP17 and the medium AP50 chains together with the amino-terminal domains of the large α and β chains. One appendage corresponds to the carboxy-terminal domain of the β chain. We find that as in the case of the β chains, the carboxy-terminal portion of the β chains is an independently folded domain corresponding to the second appendage. We use limited tryptic proteolysis of clathrin/AP-2 coats to show the release of the appendages from the interior of the coats and the retention of the AP core by the remaining clathrin lattice. In addition, we find that the AP core stabilizes the coat and prevents its depolymerization. These results are consistent with the proposal that the AP core contains the binding site(s) for clathrin, while the α- and β-chain appendages interact with membrane components of coated pits and coated vesicles.
|Original language||English (US)|
|Number of pages||8|
|State||Published - 1990|
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