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Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking
In mammalian cells, the Golgi reassembly stacking protein 65 (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers through the N-terminal GRASP domain. Because the GRASP domain is globular and relatively small, but the gaps between stacks are large and he...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694753/ https://www.ncbi.nlm.nih.gov/pubmed/26538023 http://dx.doi.org/10.1091/mbc.E15-09-0650 |
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author | Tang, Danming Zhang, Xiaoyan Huang, Shijiao Yuan, Hebao Li, Jie Wang, Yanzhuang |
author_facet | Tang, Danming Zhang, Xiaoyan Huang, Shijiao Yuan, Hebao Li, Jie Wang, Yanzhuang |
author_sort | Tang, Danming |
collection | PubMed |
description | In mammalian cells, the Golgi reassembly stacking protein 65 (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers through the N-terminal GRASP domain. Because the GRASP domain is globular and relatively small, but the gaps between stacks are large and heterogeneous, it remains puzzling how GRASP65 physically links Golgi stacks into a ribbon. To explore the possibility that other proteins may help GRASP65 in ribbon linking, we used biochemical methods and identified the actin elongation factor Mena as a novel GRASP65-binding protein. Mena is recruited onto the Golgi membranes through interaction with GRASP65. Depleting Mena or disrupting actin polymerization resulted in Golgi fragmentation. In cells, Mena and actin were required for Golgi ribbon formation after nocodazole washout; in vitro, Mena and microfilaments enhanced GRASP65 oligomerization and Golgi membrane fusion. Thus Mena interacts with GRASP65 to promote local actin polymerization, which facilitates Golgi ribbon linking. |
format | Online Article Text |
id | pubmed-4694753 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-46947532016-03-16 Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking Tang, Danming Zhang, Xiaoyan Huang, Shijiao Yuan, Hebao Li, Jie Wang, Yanzhuang Mol Biol Cell Articles In mammalian cells, the Golgi reassembly stacking protein 65 (GRASP65) has been implicated in both Golgi stacking and ribbon linking by forming trans-oligomers through the N-terminal GRASP domain. Because the GRASP domain is globular and relatively small, but the gaps between stacks are large and heterogeneous, it remains puzzling how GRASP65 physically links Golgi stacks into a ribbon. To explore the possibility that other proteins may help GRASP65 in ribbon linking, we used biochemical methods and identified the actin elongation factor Mena as a novel GRASP65-binding protein. Mena is recruited onto the Golgi membranes through interaction with GRASP65. Depleting Mena or disrupting actin polymerization resulted in Golgi fragmentation. In cells, Mena and actin were required for Golgi ribbon formation after nocodazole washout; in vitro, Mena and microfilaments enhanced GRASP65 oligomerization and Golgi membrane fusion. Thus Mena interacts with GRASP65 to promote local actin polymerization, which facilitates Golgi ribbon linking. The American Society for Cell Biology 2016-01-01 /pmc/articles/PMC4694753/ /pubmed/26538023 http://dx.doi.org/10.1091/mbc.E15-09-0650 Text en © 2016 Tang et al. 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 for Cell Biology. |
spellingShingle | Articles Tang, Danming Zhang, Xiaoyan Huang, Shijiao Yuan, Hebao Li, Jie Wang, Yanzhuang Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking |
title | Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking |
title_full | Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking |
title_fullStr | Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking |
title_full_unstemmed | Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking |
title_short | Mena–GRASP65 interaction couples actin polymerization to Golgi ribbon linking |
title_sort | mena–grasp65 interaction couples actin polymerization to golgi ribbon linking |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4694753/ https://www.ncbi.nlm.nih.gov/pubmed/26538023 http://dx.doi.org/10.1091/mbc.E15-09-0650 |
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