Abstract:
:Coatomer, the major component of the coat of COPI transport vesicles, binds both to the dilysine motif of resident membrane proteins of the endoplasmic reticulum and to the cytoplasmic domain of p23, a major type I membrane protein of COPI vesicles. Using a photocrosslinking approach, we find that under native conditions a peptide analogous to the cytoplasmic domain of p23 interacts with coatomer exclusively through its gamma subunit and shares its binding site with a KKXX retrieval motif. However, upon dissociation of coatomer, interaction with various subunits, including an alpha-, beta'-, epsilon-COP subcomplex, of the photoreactive peptide is observed. We suggest that, under physiological conditions, interaction of coatomer with both endoplasmic reticulum retrieval motifs and the cytoplasmic domain of p23 is mediated by gamma-COP.
journal_name
Proc Natl Acad Sci U S Aauthors
Harter C,Wieland FTdoi
10.1073/pnas.95.20.11649subject
Has Abstractpub_date
1998-09-29 00:00:00pages
11649-54issue
20eissn
0027-8424issn
1091-6490journal_volume
95pub_type
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