Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.

The Golgi apparatus in mammalian cells is composed of flattened cisternae that are densely packed to form stacks. We have used the Golgi stacking protein GRASP65 as a tool to modify the stacking state of Golgi cisternae. We established an assay to measure protein transport to the cell surface in pos...

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Autores principales: Yanzhuang Wang, Jen-Hsuan Wei, Blaine Bisel, Danming Tang, Joachim Seemann
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Publicado: Public Library of Science (PLoS) 2008
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Acceso en línea:https://doaj.org/article/ff3c1a310827410e8a8804e22c7bd2be
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spelling oai:doaj.org-article:ff3c1a310827410e8a8804e22c7bd2be2021-11-25T06:13:19ZGolgi cisternal unstacking stimulates COPI vesicle budding and protein transport.1932-620310.1371/journal.pone.0001647https://doaj.org/article/ff3c1a310827410e8a8804e22c7bd2be2008-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18297130/?tool=EBIhttps://doaj.org/toc/1932-6203The Golgi apparatus in mammalian cells is composed of flattened cisternae that are densely packed to form stacks. We have used the Golgi stacking protein GRASP65 as a tool to modify the stacking state of Golgi cisternae. We established an assay to measure protein transport to the cell surface in post-mitotic cells in which the Golgi was unstacked. Cells with an unstacked Golgi showed a higher transport rate compared to cells with stacked Golgi membranes. Vesicle budding from unstacked cisternae in vitro was significantly increased compared to stacked membranes. These results suggest that Golgi cisternal stacking can directly regulate vesicle formation and thus the rate of protein transport through the Golgi. The results further suggest that at the onset of mitosis, unstacking of cisternae allows extensive and rapid vesiculation of the Golgi in preparation for its subsequent partitioning.Yanzhuang WangJen-Hsuan WeiBlaine BiselDanming TangJoachim SeemannPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 3, Iss 2, p e1647 (2008)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Yanzhuang Wang
Jen-Hsuan Wei
Blaine Bisel
Danming Tang
Joachim Seemann
Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.
description The Golgi apparatus in mammalian cells is composed of flattened cisternae that are densely packed to form stacks. We have used the Golgi stacking protein GRASP65 as a tool to modify the stacking state of Golgi cisternae. We established an assay to measure protein transport to the cell surface in post-mitotic cells in which the Golgi was unstacked. Cells with an unstacked Golgi showed a higher transport rate compared to cells with stacked Golgi membranes. Vesicle budding from unstacked cisternae in vitro was significantly increased compared to stacked membranes. These results suggest that Golgi cisternal stacking can directly regulate vesicle formation and thus the rate of protein transport through the Golgi. The results further suggest that at the onset of mitosis, unstacking of cisternae allows extensive and rapid vesiculation of the Golgi in preparation for its subsequent partitioning.
format article
author Yanzhuang Wang
Jen-Hsuan Wei
Blaine Bisel
Danming Tang
Joachim Seemann
author_facet Yanzhuang Wang
Jen-Hsuan Wei
Blaine Bisel
Danming Tang
Joachim Seemann
author_sort Yanzhuang Wang
title Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.
title_short Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.
title_full Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.
title_fullStr Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.
title_full_unstemmed Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport.
title_sort golgi cisternal unstacking stimulates copi vesicle budding and protein transport.
publisher Public Library of Science (PLoS)
publishDate 2008
url https://doaj.org/article/ff3c1a310827410e8a8804e22c7bd2be
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AT jenhsuanwei golgicisternalunstackingstimulatescopivesiclebuddingandproteintransport
AT blainebisel golgicisternalunstackingstimulatescopivesiclebuddingandproteintransport
AT danmingtang golgicisternalunstackingstimulatescopivesiclebuddingandproteintransport
AT joachimseemann golgicisternalunstackingstimulatescopivesiclebuddingandproteintransport
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