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GTP-dependent binding of ADP-ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1999 May 14; Vol. 274 (20), pp. 14198-203. - Publication Year :
- 1999
-
Abstract
- A site-directed photocross-linking approach was employed to determine components that act downstream of ADP-ribosylation factor (ARF). To this end, a photolabile phenylalanine analog was incorporated at various positions of the putative effector region of the ARF molecule. Depending on the position of incorporation, we find specific and GTP-dependent interactions of ARF with two subunits of the coatomer complex, beta-COP and gamma-COP, as well as an interaction with a cytosolic protein (approximately 185 kDa). In addition, we observe homodimer formation of ARF molecules at the Golgi membrane. These data suggest that the binding site of ARF to coatomer is at the interface of its beta- and gamma-subunits, and this is in close proximity to the second site of interaction of coatomer with the Golgi membrane, the binding site within gamma-COP for cytosolic dibasic/diphenylalanine motifs.
- Subjects :
- ADP-Ribosylation Factors
Animals
Binding Sites
CHO Cells
Cattle
Coatomer Protein
Cricetinae
Cross-Linking Reagents metabolism
Crystallography, X-Ray
Dimerization
Golgi Apparatus metabolism
Macromolecular Substances
Microtubule-Associated Proteins metabolism
Molecular Weight
Photochemistry
Protein Conformation
Protein Structure, Secondary
Rabbits
Carrier Proteins metabolism
GTP-Binding Proteins metabolism
Guanosine Triphosphate metabolism
Lysine metabolism
Membrane Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 274
- Issue :
- 20
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 10318838
- Full Text :
- https://doi.org/10.1074/jbc.274.20.14198