期刊
EMBO JOURNAL
卷 19, 期 15, 页码 3905-3917出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/19.15.3905
关键词
ARF-GAP; clathrin; coatomer; COPI; Glo3; Golgi
We performed a systematic mapping of interaction domains on COP I subunits to gain novel insights into the architecture of coatomer, Using the two-hybrid system, we characterize the domain structure of the alpha-, beta'-, epsilon-COP and beta-, gamma-, delta-, zeta-COP coatomer subcomplexes and identify links between them that contribute to coatomer integrity. Our results demonstrate that the domain organization of the beta-, gamma-, delta-, zeta-COP subcomplex and AP adaptor complexes is related. Through in vivo analysis of alpha-COP truncation mutants, we characterize distinct functional domains on alpha-COP, Its N-terminal WD40 domain is dispensable for yeast cell viability and overall coatomer function, but is required for KKXX-dependent trafficking. The last similar to 170 amino acids of alpha-COP are also nonessential for cell viability, but required for epsilon-COP incorporation into coatomer and maintainance of normal epsilon-COP levels. Further, we demonstrate navel direct interactions of coatomer subunits with regulatory proteins: beta'- and gamma-COP interact with the ARF-GTP-activating protein (GAP) Glo3p, but not Gcs1p, and beta- and epsilon-COP interact with ARF-GTP. Glo3p also interacts with intact coatomer in vitro.
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