New Insights Into the Golgi Stacking Proteins
The Golgi stacking proteins, GRASP55 and GRASP65, are best known for their roles in Golgi structure formation. These peripheral Golgi proteins form trans-oligomers that hold the flat cisternal membranes into stacks. Depletion of both GRASP proteins in cells disrupts the Golgi stack structure, increa...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-07-01
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| Series: | Frontiers in Cell and Developmental Biology |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/article/10.3389/fcell.2019.00131/full |
| _version_ | 1818910440250408960 |
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| author | Erpan Ahat Jie Li Yanzhuang Wang Yanzhuang Wang |
| author_facet | Erpan Ahat Jie Li Yanzhuang Wang Yanzhuang Wang |
| author_sort | Erpan Ahat |
| collection | DOAJ |
| description | The Golgi stacking proteins, GRASP55 and GRASP65, are best known for their roles in Golgi structure formation. These peripheral Golgi proteins form trans-oligomers that hold the flat cisternal membranes into stacks. Depletion of both GRASP proteins in cells disrupts the Golgi stack structure, increases protein trafficking, but impairs accurate glycosylation, and sorting. Golgi unstacking by GRASPs depletion also reduces cell adhesion and migration in an integrin-dependent manner. In addition to Golgi structure formation and regulation of cellular activities, GRASPs, in particular GRASP55, have recently drawn attention in their roles in autophagy, and unconventional secretion. In autophagy, GRASP55 senses the energy level by O-GlcNAcylation, which regulates GRASP55 translocation from the Golgi to the autophagosome-lysosome interface, where it interacts with LC3 and LAMP2 to facilitate autophagosome-lysosome fusion. This newly discovered function of GRASP55 in autophagy may help explain its role in the stress-induced, autophagosome-dependent unconventional secretion. In this review, we summarize the emerging functions of the GRASP proteins, focusing on their roles in cell adhesion and migration, autophagy, unconventional secretion, as well as on novel GRASP-interacting proteins. |
| first_indexed | 2024-12-19T22:42:50Z |
| format | Article |
| id | doaj.art-929626b0a2e34042bc05043cdff210e8 |
| institution | Directory Open Access Journal |
| issn | 2296-634X |
| language | English |
| last_indexed | 2024-12-19T22:42:50Z |
| publishDate | 2019-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cell and Developmental Biology |
| spelling | doaj.art-929626b0a2e34042bc05043cdff210e82022-12-21T20:03:01ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2019-07-01710.3389/fcell.2019.00131466853New Insights Into the Golgi Stacking ProteinsErpan Ahat0Jie Li1Yanzhuang Wang2Yanzhuang Wang3Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, United StatesDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, United StatesDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, United StatesDepartment of Neurology, University of Michigan School of Medicine, Ann Arbor, MI, United StatesThe Golgi stacking proteins, GRASP55 and GRASP65, are best known for their roles in Golgi structure formation. These peripheral Golgi proteins form trans-oligomers that hold the flat cisternal membranes into stacks. Depletion of both GRASP proteins in cells disrupts the Golgi stack structure, increases protein trafficking, but impairs accurate glycosylation, and sorting. Golgi unstacking by GRASPs depletion also reduces cell adhesion and migration in an integrin-dependent manner. In addition to Golgi structure formation and regulation of cellular activities, GRASPs, in particular GRASP55, have recently drawn attention in their roles in autophagy, and unconventional secretion. In autophagy, GRASP55 senses the energy level by O-GlcNAcylation, which regulates GRASP55 translocation from the Golgi to the autophagosome-lysosome interface, where it interacts with LC3 and LAMP2 to facilitate autophagosome-lysosome fusion. This newly discovered function of GRASP55 in autophagy may help explain its role in the stress-induced, autophagosome-dependent unconventional secretion. In this review, we summarize the emerging functions of the GRASP proteins, focusing on their roles in cell adhesion and migration, autophagy, unconventional secretion, as well as on novel GRASP-interacting proteins.https://www.frontiersin.org/article/10.3389/fcell.2019.00131/fullGolgistackingGRASP65GRASP55O-GlcNAcylationautophagy |
| spellingShingle | Erpan Ahat Jie Li Yanzhuang Wang Yanzhuang Wang New Insights Into the Golgi Stacking Proteins Frontiers in Cell and Developmental Biology Golgi stacking GRASP65 GRASP55 O-GlcNAcylation autophagy |
| title | New Insights Into the Golgi Stacking Proteins |
| title_full | New Insights Into the Golgi Stacking Proteins |
| title_fullStr | New Insights Into the Golgi Stacking Proteins |
| title_full_unstemmed | New Insights Into the Golgi Stacking Proteins |
| title_short | New Insights Into the Golgi Stacking Proteins |
| title_sort | new insights into the golgi stacking proteins |
| topic | Golgi stacking GRASP65 GRASP55 O-GlcNAcylation autophagy |
| url | https://www.frontiersin.org/article/10.3389/fcell.2019.00131/full |
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