A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptin
T Serafini, G Stenbeck, A Brecht, F Lottspeich, L Orel… - Nature, 1991 - nature.com
Nature, 1991•nature.com
Four high-molecular-weight proteins form the main subunits of the coat of Golgi-derived (non-
clathrin) coated vesicles. One of these coat proteins, β-COP, is identical to a Golgi-
associated protein of relative mass 110,000 (110K) that shares homology with the adaptin
proteins of clathrin-coated vesicles. This connection, and the comparable molecular weights
of the coat proteins of Golgi-derived and clathrin-coated vesicles, indicates that they may be
structurally related. The identification of β-COP as the 110K protein explains the blocking of …
clathrin) coated vesicles. One of these coat proteins, β-COP, is identical to a Golgi-
associated protein of relative mass 110,000 (110K) that shares homology with the adaptin
proteins of clathrin-coated vesicles. This connection, and the comparable molecular weights
of the coat proteins of Golgi-derived and clathrin-coated vesicles, indicates that they may be
structurally related. The identification of β-COP as the 110K protein explains the blocking of …
Abstract
Four high-molecular-weight proteins form the main subunits of the coat of Golgi-derived (non-clathrin) coated vesicles. One of these coat proteins, β-COP, is identical to a Golgi-associated protein of relative mass 110,000 (110K) that shares homology with the adaptin proteins of clathrin-coated vesicles. This connection, and the comparable molecular weights of the coat proteins of Golgi-derived and clathrin-coated vesicles, indicates that they may be structurally related. The identification of β-COP as the 110K protein explains the blocking of secretion by the drug brefeldin A.
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