The clathrin binding domain of the assembly protein AP-2 has been identified by proteolytically cleaving AP-2 into 2 discrete moieties, termed light and heavy mero-AP (LM-AP and HM-AP), and testing their ability to bind to clathrin assembled into cage structures or to clathrin trimers immobilized on Sepharose. The smaller product (LM-AP), which contains 20-40-kD fragments of the parent 100-kD polypeptides and which comprises two small appendages in the native AP-2 molecule, did not significantly interact with clathrin under either condition. In contrast, the HM-AP complex, which forms the larger central mass of the native AP-2 structure and contains uncleaved 50-kD and 16-kD polypeptides as well as 60-66-kD fragments of the parent 100-kD polypeptides, retained binding activity for both dissociated and assembled clathrin.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jan 16 1989|
ASJC Scopus subject areas
- Molecular Biology