Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes

Narula, N., McMorrow, I., Plopper, G., Doherty, J., Matlin, K. S., Burke, B. and Stow, J. L. (1992) Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes. Journal of Cell Biology, 117 1: 27-38. doi:10.1083/jcb.117.1.27

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Author Narula, N.
McMorrow, I.
Plopper, G.
Doherty, J.
Matlin, K. S.
Burke, B.
Stow, J. L.
Title Identification of a 200-kD, brefeldin-sensitive protein on Golgi membranes
Journal name Journal of Cell Biology   Check publisher's open access policy
ISSN 0021-9525
1540-8140
Publication date 1992-04-01
Year available 1992
Sub-type Article (original research)
DOI 10.1083/jcb.117.1.27
Open Access Status File (Publisher version)
Volume 117
Issue 1
Start page 27
End page 38
Total pages 12
Place of publication New York, NY, United States
Publisher Rockefeller University Press
Language eng
Abstract A mAb AD7, raised against canine liver Golgi membranes, recognizes a novel, 200-kD protein (p200) which is found in a wide variety of cultured cell lines. Immunofluorescence staining of cultured cells with the AD7 antibody produced intense staining of p200 in the juxtanuclear Golgi complex and more diffuse staining of p200 in the cytoplasm. The p200 protein in the Golgi complex was colocalized with other Golgi proteins, including mannosidase II and beta-COP, a coatomer protein. Localization of p200 by immunoperoxidase staining at the electron microscopic level revealed concentrations of p200 at the dilated rims of Golgi cisternae. Biochemical studies showed that p200 is a peripheral membrane protein which partitions to the aqueous phase of Triton X-114 solutions and is phosphorylated. The p200 protein is located on the cytoplasmic face of membranes, since it was accessible to trypsin digestion in microsomal preparations. and is recovered in approximately equal amounts in membrane pellets and in the cytosol of homogenized cells. Immunofluorescence staining of normal rat kidney cells exposed to the toxin brefeldin A (BFA), showed that there was very rapid redistribution of p200, which was dissociated from Golgi membranes in the presence of this drug. The effect of BFA was reversible, since upon removal of the toxin, AD7 rapidly reassociated with the Golgi complex. In the BFA-resistant cell line PtK1, BFA failed to cause redistribution of p200 from Golgi membranes. Taken together, these results indicate that the p200 Golgi membrane-associated protein has many properties in common with the coatomer protein, beta-COP.
Keyword Fusion Protein
Endoplasmic-Reticulum
Monoclonal-Antibody
Vesicular Transport
Secretory Proteins
Coated Vesicles
Stack
Clathrin
Binding
Yeast
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID DK 42881
GM 38556
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
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