Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three-hybrid system.
Biochem Biophys Res Commun
; 284(4): 1083-9, 2001 Jun 22.
Article
in En
| MEDLINE
| ID: mdl-11409905
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, 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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Phosphoproteins
/
Coat Protein Complex I
/
Adaptor Protein Complex 1
/
Adaptor Protein Complex 2
/
Adaptor Protein Complex sigma Subunits
/
Nerve Tissue Proteins
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2001
Document type:
Article
Affiliation country:
Japan
Publication country:
EEUU
/
ESTADOS UNIDOS
/
ESTADOS UNIDOS DA AMERICA
/
EUA
/
UNITED STATES
/
UNITED STATES OF AMERICA
/
US
/
USA