Author: Takatsu H. Futatsumori M. Yoshino K. Yoshida Y. Shin H-W. Nakayama K.
Publisher: Elsevier
ISSN: 0006-291X
Source: Biochemical and Biophysical Research Communications, Vol.284, Iss.4, 2001-06, pp. : 1083-1089
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Abstract
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, γ-adaptin and β1-adaptin, is markedly enhanced in the presence of the small subunit, ς1. Similarly, two large subunits of the AP-4 complex, ε-adaptin and β4-adaptin, are found to interact with each other only in the presence of the small subunit, ς4. Furthermore, we have found that an interaction between two large subunits of the COPI F subcomplex, γ-COP and β-COP, is detectable only in the presence of ζ-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.
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