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Biochem Biophys Res Commun. 1989 Jan 16;158(1):17-23.

Identification of the clathrin-binding domain of assembly protein AP-2.

Author information

1
Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA 19140.

Abstract

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.

PMID:
2912448
DOI:
10.1016/s0006-291x(89)80170-6
[Indexed for MEDLINE]

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