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.
Mesh Terms:
Adaptor Protein Complex 1, Adaptor Protein Complex 2, Adaptor Protein Complex sigma Subunits, Adaptor Proteins, Vesicular Transport, Clathrin, Cloning, Molecular, Coat Protein Complex I, Humans, Liver, Nerve Tissue Proteins, Phosphoproteins, Protein Subunits, Recombinant Fusion Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, beta-Galactosidase
Biochem. Biophys. Res. Commun.
Date: Jun. 22, 2001
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