TY - JOUR
T1 - β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the golgi complex, shows homology to β-adaptin
AU - Duden, Rainer
AU - Griffiths, Gareth
AU - Frank, Rainer
AU - Argos, Patrick
AU - Kreis, Thomas E.
N1 - Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.
PY - 1991/2/8
Y1 - 1991/2/8
N2 - We have cloned and sequenced β-COP, a peripheral 110 kd Golgi membrane protein. β-COP shows significant homology to β-adaptin. It is present in a membrane-bound form and in a cytosolic complex of 13-14S, with a Stokes radius of ∼10 nm and an estimated Mr of ∼550,000. By immunofluorescence labeling, β-COP is associated with the structures of the Golgi complex. Immunoelectron microscopy has localized β-COP to non-clathrin-coated vesicles and cisternae of the Golgi complex. These coated vesicles accumulate in rat liver Golgi fractions treated with GTPγS and strongly label for-COP Our data suggest that β-COP is a component of a coat associated with vesicles and cisternae of the Golgi complex.
AB - We have cloned and sequenced β-COP, a peripheral 110 kd Golgi membrane protein. β-COP shows significant homology to β-adaptin. It is present in a membrane-bound form and in a cytosolic complex of 13-14S, with a Stokes radius of ∼10 nm and an estimated Mr of ∼550,000. By immunofluorescence labeling, β-COP is associated with the structures of the Golgi complex. Immunoelectron microscopy has localized β-COP to non-clathrin-coated vesicles and cisternae of the Golgi complex. These coated vesicles accumulate in rat liver Golgi fractions treated with GTPγS and strongly label for-COP Our data suggest that β-COP is a component of a coat associated with vesicles and cisternae of the Golgi complex.
UR - http://www.scopus.com/inward/record.url?scp=0026034357&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(91)90248-W
DO - 10.1016/0092-8674(91)90248-W
M3 - Journal articles
C2 - 1840503
AN - SCOPUS:0026034357
SN - 0092-8674
VL - 64
SP - 649
EP - 665
JO - Cell
JF - Cell
IS - 3
ER -
