Abstract
The clathrin-associated protein complex 2 (AP-2 complex) is a group of proteins associated with clathrin-coated vesicles and believed to interact with cytoplasmic domains of receptors found in the plasma membrane. AP-2 was purified as an assembly of several polypeptide chains (α, β, AP50, and AP17), of which only the α and β chains (110-115 kDa) show significant heterogeneity. We have obtained cDNA clones for two distinct rat brain β chains. We have also studied the domain organization of bovine brain AP-2 complexes by selective proteolysis. Results of these studies show that the α and β chains have a similar two-domain organization. Their amino-terminal domains are relatively invariant whereas their carboxyl-terminal domains are variable in both sequence and length. We propose that the variable domains select receptors for inclusion in coated vesicles.
Original language | English (US) |
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Pages (from-to) | 2612-2616 |
Number of pages | 5 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 86 |
Issue number | 8 |
State | Published - 1989 |
Externally published | Yes |
ASJC Scopus subject areas
- General
- Genetics