Reversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplex.

COPI-coated vesicles mediate protein transport within the early secretory pathway. Their coat consists of ADP ribosylation factor (ARF1, a small guanosine nucleotide binding protein), and coatomer, a cytosolic complex composed of seven subunits, alpha- to zeta-coat proteins (COPs). For coat formation that initiates budding of a vesicle, ARF1 is recruited ...
to the Golgi membrane from the cytosol in its GTP-bound form, and subsequently, coatomer can bind to the membrane. To identify a minimal structure of coatomer capable to bind to Golgi membranes in an ARF1-dependent manner, we have established a procedure to dissociate coatomer under conditions that allow reassociation of the subunits to a complete and functional complex. After dissociation, subunits or subcomplexes can be isolated and may be expected to be functional. Herein we describe isolation of a subcomplex of coatomer consisting of beta- and delta-COPs that is able to bind to Golgi membranes in an ARF1- and GTP-dependent manner.
Mesh Terms:
ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, Animals, Coatomer Protein, Cytosol, Dimerization, GTP-Binding Proteins, Golgi Apparatus, Guanosine 5'-O-(3-Thiotriphosphate), Guanosine Diphosphate, Guanosine Triphosphate, Liver, Macromolecular Substances, Maleic Anhydrides, Membrane Proteins, Microtubule-Associated Proteins, Rabbits, Thionucleotides
Proc. Natl. Acad. Sci. U.S.A.
Date: Mar. 03, 1998
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