β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the golgi complex, shows homology to β-adaptin

Rainer Duden; Gareth Griffiths; Rainer Frank; Patrick Argos; Thomas E. Kreis

doi:10.1016/0092-8674(91)90248-W

β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the golgi complex, shows homology to β-adaptin

Rainer Duden^*, Gareth Griffiths, Rainer Frank, Patrick Argos, Thomas E. Kreis

^*Corresponding author for this work

Institute of Biology

European Molecular Biology Laboratory Heidelberg (EMBL)

449 Citations (Scopus)

Abstract

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 M_r 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.

Original language	English
Journal	Cell
Volume	64
Issue number	3
Pages (from-to)	649-665
Number of pages	17
ISSN	0092-8674
DOIs	https://doi.org/10.1016/0092-8674(91)90248-W
Publication status	Published - 08.02.1991

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

Access to Document

10.1016/0092-8674(91)90248-W

Cite this

@article{48a3b69226aa494bade1257f24a1b039,

title = "β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the golgi complex, shows homology to β-adaptin",

abstract = "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.",

author = "Rainer Duden and Gareth Griffiths and Rainer Frank and Patrick Argos and Kreis, \{Thomas E.\}",

year = "1991",

month = feb,

day = "8",

doi = "10.1016/0092-8674(91)90248-W",

language = "English",

volume = "64",

pages = "649--665",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "3",

}

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.

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 - https://www.scopus.com/pages/publications/0026034357

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 -

β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the golgi complex, shows homology to β-adaptin

Abstract

UN SDGs

Research Areas and Centers

Access to Document

Other files and links

Fingerprint

Cite this