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Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization
Homotypic membrane tethering by the Golgi reassembly and stacking proteins (GRASPs) is required for the lateral linkage of mammalian Golgi ministacks into a ribbon-like membrane network. Although GRASP65 and GRASP55 are specifically localized to cis and medial/trans cisternae, respectively, it is un...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873884/ https://www.ncbi.nlm.nih.gov/pubmed/24227884 http://dx.doi.org/10.1091/mbc.E13-07-0395 |
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author | Jarvela, Timothy Linstedt, Adam D. |
author_facet | Jarvela, Timothy Linstedt, Adam D. |
author_sort | Jarvela, Timothy |
collection | PubMed |
description | Homotypic membrane tethering by the Golgi reassembly and stacking proteins (GRASPs) is required for the lateral linkage of mammalian Golgi ministacks into a ribbon-like membrane network. Although GRASP65 and GRASP55 are specifically localized to cis and medial/trans cisternae, respectively, it is unknown whether each GRASP mediates cisternae-specific tethering and whether such specificity is necessary for Golgi compartmentalization. Here each GRASP was tagged with KillerRed (KR), expressed in HeLa cells, and inhibited by 1-min exposure to light. Significantly, inactivation of either GRASP unlinked the Golgi ribbon, and the immediate effect of GRASP65-KR inactivation was a loss of cis- rather than trans-Golgi integrity, whereas inactivation of GRASP55-KR first affected the trans- and not the cis-Golgi. Thus each GRASP appears to play a direct and cisternae-specific role in linking ministacks into a continuous membrane network. To test the consequence of loss of cisternae-specific tethering, we generated Golgi membranes with a single GRASP on all cisternae. Remarkably, the membranes exhibited the full connectivity of wild-type Golgi ribbons but were decompartmentalized and defective in glycan processing. Thus the GRASP isoforms specifically link analogous cisternae to ensure Golgi compartmentalization and proper processing. |
format | Online Article Text |
id | pubmed-3873884 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-38738842014-03-16 Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization Jarvela, Timothy Linstedt, Adam D. Mol Biol Cell Articles Homotypic membrane tethering by the Golgi reassembly and stacking proteins (GRASPs) is required for the lateral linkage of mammalian Golgi ministacks into a ribbon-like membrane network. Although GRASP65 and GRASP55 are specifically localized to cis and medial/trans cisternae, respectively, it is unknown whether each GRASP mediates cisternae-specific tethering and whether such specificity is necessary for Golgi compartmentalization. Here each GRASP was tagged with KillerRed (KR), expressed in HeLa cells, and inhibited by 1-min exposure to light. Significantly, inactivation of either GRASP unlinked the Golgi ribbon, and the immediate effect of GRASP65-KR inactivation was a loss of cis- rather than trans-Golgi integrity, whereas inactivation of GRASP55-KR first affected the trans- and not the cis-Golgi. Thus each GRASP appears to play a direct and cisternae-specific role in linking ministacks into a continuous membrane network. To test the consequence of loss of cisternae-specific tethering, we generated Golgi membranes with a single GRASP on all cisternae. Remarkably, the membranes exhibited the full connectivity of wild-type Golgi ribbons but were decompartmentalized and defective in glycan processing. Thus the GRASP isoforms specifically link analogous cisternae to ensure Golgi compartmentalization and proper processing. The American Society for Cell Biology 2014-01-01 /pmc/articles/PMC3873884/ /pubmed/24227884 http://dx.doi.org/10.1091/mbc.E13-07-0395 Text en © 2014 Jarvela and Linstedt. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Jarvela, Timothy Linstedt, Adam D. Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization |
title | Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization |
title_full | Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization |
title_fullStr | Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization |
title_full_unstemmed | Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization |
title_short | Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization |
title_sort | isoform-specific tethering links the golgi ribbon to maintain compartmentalization |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873884/ https://www.ncbi.nlm.nih.gov/pubmed/24227884 http://dx.doi.org/10.1091/mbc.E13-07-0395 |
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