Acylation – A New Means to Control Traffic Through the Golgi
The Golgi is well known to act as center for modification and sorting of proteins for secretion and delivery to other organelles. A key sorting step occurs at the trans-Golgi network and is mediated by protein adapters. However, recent data indicate that sorting also occurs much earlier, at the cis-...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-06-01
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| Series: | Frontiers in Cell and Developmental Biology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fcell.2019.00109/full |
| _version_ | 1818380995730079744 |
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| author | Andreas M. Ernst Derek Toomre Jonathan S. Bogan Jonathan S. Bogan |
| author_facet | Andreas M. Ernst Derek Toomre Jonathan S. Bogan Jonathan S. Bogan |
| author_sort | Andreas M. Ernst |
| collection | DOAJ |
| description | The Golgi is well known to act as center for modification and sorting of proteins for secretion and delivery to other organelles. A key sorting step occurs at the trans-Golgi network and is mediated by protein adapters. However, recent data indicate that sorting also occurs much earlier, at the cis-Golgi, and uses lipid acylation as a novel means to regulate anterograde flux. Here, we examine an emerging role of S-palmitoylation/acylation as a mechanism to regulate anterograde routing. We discuss the critical Golgi-localized DHHC S-palmitoyltransferase enzymes that orchestrate this lipid modification, as well as their diverse protein clients (e.g., MAP6, SNAP25, CSP, LAT, β-adrenergic receptors, GABA receptors, and GLUT4 glucose transporters). Critically, for integral membrane proteins, S-acylation can act as new a “self-sorting” signal to concentrate these cargoes in rims of Golgi cisternae, and to promote their rapid traffic through the Golgi or, potentially, to bypass the Golgi. We discuss this mechanism and examine its potential relevance to human physiology and disease, including diabetes and neurodegenerative diseases. |
| first_indexed | 2024-12-14T02:27:33Z |
| format | Article |
| id | doaj.art-ef727070745c42caaf7997f5f0652e48 |
| institution | Directory Open Access Journal |
| issn | 2296-634X |
| language | English |
| last_indexed | 2024-12-14T02:27:33Z |
| publishDate | 2019-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj.art-ef727070745c42caaf7997f5f0652e482022-12-21T23:20:21ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2019-06-01710.3389/fcell.2019.00109465300Acylation – A New Means to Control Traffic Through the GolgiAndreas M. Ernst0Derek Toomre1Jonathan S. Bogan2Jonathan S. Bogan3Department of Cell Biology, Yale School of Medicine, Yale University, New Haven, CT, United StatesDepartment of Cell Biology, Yale School of Medicine, Yale University, New Haven, CT, United StatesDepartment of Cell Biology, Yale School of Medicine, Yale University, New Haven, CT, United StatesSection of Endocrinology and Metabolism, Department of Internal Medicine, Yale School of Medicine, Yale University, New Haven, CT, United StatesThe Golgi is well known to act as center for modification and sorting of proteins for secretion and delivery to other organelles. A key sorting step occurs at the trans-Golgi network and is mediated by protein adapters. However, recent data indicate that sorting also occurs much earlier, at the cis-Golgi, and uses lipid acylation as a novel means to regulate anterograde flux. Here, we examine an emerging role of S-palmitoylation/acylation as a mechanism to regulate anterograde routing. We discuss the critical Golgi-localized DHHC S-palmitoyltransferase enzymes that orchestrate this lipid modification, as well as their diverse protein clients (e.g., MAP6, SNAP25, CSP, LAT, β-adrenergic receptors, GABA receptors, and GLUT4 glucose transporters). Critically, for integral membrane proteins, S-acylation can act as new a “self-sorting” signal to concentrate these cargoes in rims of Golgi cisternae, and to promote their rapid traffic through the Golgi or, potentially, to bypass the Golgi. We discuss this mechanism and examine its potential relevance to human physiology and disease, including diabetes and neurodegenerative diseases.https://www.frontiersin.org/article/10.3389/fcell.2019.00109/fullGolgipalmitoylationacylationanterograde transportGolgi bypassmembrane traffic |
| spellingShingle | Andreas M. Ernst Derek Toomre Jonathan S. Bogan Jonathan S. Bogan Acylation – A New Means to Control Traffic Through the Golgi Frontiers in Cell and Developmental Biology Golgi palmitoylation acylation anterograde transport Golgi bypass membrane traffic |
| title | Acylation – A New Means to Control Traffic Through the Golgi |
| title_full | Acylation – A New Means to Control Traffic Through the Golgi |
| title_fullStr | Acylation – A New Means to Control Traffic Through the Golgi |
| title_full_unstemmed | Acylation – A New Means to Control Traffic Through the Golgi |
| title_short | Acylation – A New Means to Control Traffic Through the Golgi |
| title_sort | acylation a new means to control traffic through the golgi |
| topic | Golgi palmitoylation acylation anterograde transport Golgi bypass membrane traffic |
| url | https://www.frontiersin.org/article/10.3389/fcell.2019.00109/full |
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