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A Role for Giantin in Docking COPI Vesicles to Golgi Membranes

We have previously shown that p115, a vesicle docking protein, binds to two proteins (p130 and p400) in detergent extracts of Golgi membranes. p130 was identified as GM130, a Golgi matrix protein, and was shown to act as a membrane receptor for p115. p400 has now been identified as giantin, a Golgi...

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Detalles Bibliográficos
Autores principales: Sönnichsen, Birte, Lowe, Martin, Levine, Tim, Jämsä, Eija, Dirac-Svejstrup, Barbara, Warren, Graham
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1998
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132694/
https://www.ncbi.nlm.nih.gov/pubmed/9490716
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author Sönnichsen, Birte
Lowe, Martin
Levine, Tim
Jämsä, Eija
Dirac-Svejstrup, Barbara
Warren, Graham
author_facet Sönnichsen, Birte
Lowe, Martin
Levine, Tim
Jämsä, Eija
Dirac-Svejstrup, Barbara
Warren, Graham
author_sort Sönnichsen, Birte
collection PubMed
description We have previously shown that p115, a vesicle docking protein, binds to two proteins (p130 and p400) in detergent extracts of Golgi membranes. p130 was identified as GM130, a Golgi matrix protein, and was shown to act as a membrane receptor for p115. p400 has now been identified as giantin, a Golgi membrane protein with most of its mass projecting into the cytoplasm. Giantin is found on COPI vesicles and pretreatment with antibodies inhibits both the binding of p115 and the docking of these vesicles with Golgi membranes. In contrast, GM130 is depleted from COPI vesicles and inhibition of the GM130 on Golgi membranes, using either antibodies or an NH(2)-terminal GM130 peptide, inhibits p115 binding and vesicle docking. Together these results suggest that COPI vesicles are docked by giantin on the COPI vesicles and GM130 on Golgi membranes with p115 providing a bridge.
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spelling pubmed-21326942008-05-01 A Role for Giantin in Docking COPI Vesicles to Golgi Membranes Sönnichsen, Birte Lowe, Martin Levine, Tim Jämsä, Eija Dirac-Svejstrup, Barbara Warren, Graham J Cell Biol Article We have previously shown that p115, a vesicle docking protein, binds to two proteins (p130 and p400) in detergent extracts of Golgi membranes. p130 was identified as GM130, a Golgi matrix protein, and was shown to act as a membrane receptor for p115. p400 has now been identified as giantin, a Golgi membrane protein with most of its mass projecting into the cytoplasm. Giantin is found on COPI vesicles and pretreatment with antibodies inhibits both the binding of p115 and the docking of these vesicles with Golgi membranes. In contrast, GM130 is depleted from COPI vesicles and inhibition of the GM130 on Golgi membranes, using either antibodies or an NH(2)-terminal GM130 peptide, inhibits p115 binding and vesicle docking. Together these results suggest that COPI vesicles are docked by giantin on the COPI vesicles and GM130 on Golgi membranes with p115 providing a bridge. The Rockefeller University Press 1998-03-09 /pmc/articles/PMC2132694/ /pubmed/9490716 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Sönnichsen, Birte
Lowe, Martin
Levine, Tim
Jämsä, Eija
Dirac-Svejstrup, Barbara
Warren, Graham
A Role for Giantin in Docking COPI Vesicles to Golgi Membranes
title A Role for Giantin in Docking COPI Vesicles to Golgi Membranes
title_full A Role for Giantin in Docking COPI Vesicles to Golgi Membranes
title_fullStr A Role for Giantin in Docking COPI Vesicles to Golgi Membranes
title_full_unstemmed A Role for Giantin in Docking COPI Vesicles to Golgi Membranes
title_short A Role for Giantin in Docking COPI Vesicles to Golgi Membranes
title_sort role for giantin in docking copi vesicles to golgi membranes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132694/
https://www.ncbi.nlm.nih.gov/pubmed/9490716
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