Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: Analysis using yeast three-hybrid system

Clathrin adaptor protein (AP) complexes are heterotetramers composed of two large, one medium, and one small subunits. By exploiting the yeast three-hybrid system, we have found that an interaction between the two large subunits of the AP-1 complex, gamma -adaptin and beta1-adaptin, is markedly enhanced in the presence of the small subunit, sigma1. Similarly, two large subunits of the AP-4 complex, epsilon -adaptin and beta4-adaptin, are found to interact with each other only in the presence of the small subunit, sigma4. Furthermore, we have found that an interaction between two large subunits of the COPI F subcomplex, gamma -COP and beta -COP, is detectable only in the presence of zeta -COP. Because these COPI subunits have common ancestral origins to the corresponding AP subunits, these three-hybrid data, taken together with the previous two hybrid data, suggest that the AP complexes and the COPI F subcomplex assemble by virtue of similar subunit interactions. (C) zool Academic Press.