Structural and functional division into two domains of the large (100- to 115-kDa) chains of the clathrin-associated protein complex AP-2

T. Kirchhausen, K. L. Nathanson, W. Matsui, A. Vaisberg, E. P. Chow, C. Burne, J. H. Keen, A. E. Davis

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)2612-2616
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number8
Publication statusPublished - 1989
Externally publishedYes

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ASJC Scopus subject areas

  • General
  • Genetics

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