Characterization of Protein–Membrane Interactions in Yeast Autophagy
Cells rely on autophagy to degrade cytosolic material and maintain homeostasis. During autophagy, content to be degraded is encapsulated in double membrane vesicles, termed autophagosomes, which fuse with the yeast vacuole for degradation. This conserved cellular process requires the dynamic rearran...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-06-01
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| Series: | Cells |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4409/11/12/1876 |
| _version_ | 1797489013848801280 |
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| author | Kelsie A. Leary Michael J. Ragusa |
| author_facet | Kelsie A. Leary Michael J. Ragusa |
| author_sort | Kelsie A. Leary |
| collection | DOAJ |
| description | Cells rely on autophagy to degrade cytosolic material and maintain homeostasis. During autophagy, content to be degraded is encapsulated in double membrane vesicles, termed autophagosomes, which fuse with the yeast vacuole for degradation. This conserved cellular process requires the dynamic rearrangement of membranes. As such, the process of autophagy requires many soluble proteins that bind to membranes to restructure, tether, or facilitate lipid transfer between membranes. Here, we review the methods that have been used to investigate membrane binding by the core autophagy machinery and additional accessory proteins involved in autophagy in yeast. We also review the key experiments demonstrating how each autophagy protein was shown to interact with membranes. |
| first_indexed | 2024-03-10T00:10:28Z |
| format | Article |
| id | doaj.art-c5272d4e16b24db2bfc45dbab2b15f39 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T00:10:28Z |
| publishDate | 2022-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-c5272d4e16b24db2bfc45dbab2b15f392023-11-23T16:00:45ZengMDPI AGCells2073-44092022-06-011112187610.3390/cells11121876Characterization of Protein–Membrane Interactions in Yeast AutophagyKelsie A. Leary0Michael J. Ragusa1Department of Chemistry, Dartmouth College, Hanover, NH 03755, USADepartment of Chemistry, Dartmouth College, Hanover, NH 03755, USACells rely on autophagy to degrade cytosolic material and maintain homeostasis. During autophagy, content to be degraded is encapsulated in double membrane vesicles, termed autophagosomes, which fuse with the yeast vacuole for degradation. This conserved cellular process requires the dynamic rearrangement of membranes. As such, the process of autophagy requires many soluble proteins that bind to membranes to restructure, tether, or facilitate lipid transfer between membranes. Here, we review the methods that have been used to investigate membrane binding by the core autophagy machinery and additional accessory proteins involved in autophagy in yeast. We also review the key experiments demonstrating how each autophagy protein was shown to interact with membranes.https://www.mdpi.com/2073-4409/11/12/1876autophagymembrane binding proteinsyeast |
| spellingShingle | Kelsie A. Leary Michael J. Ragusa Characterization of Protein–Membrane Interactions in Yeast Autophagy Cells autophagy membrane binding proteins yeast |
| title | Characterization of Protein–Membrane Interactions in Yeast Autophagy |
| title_full | Characterization of Protein–Membrane Interactions in Yeast Autophagy |
| title_fullStr | Characterization of Protein–Membrane Interactions in Yeast Autophagy |
| title_full_unstemmed | Characterization of Protein–Membrane Interactions in Yeast Autophagy |
| title_short | Characterization of Protein–Membrane Interactions in Yeast Autophagy |
| title_sort | characterization of protein membrane interactions in yeast autophagy |
| topic | autophagy membrane binding proteins yeast |
| url | https://www.mdpi.com/2073-4409/11/12/1876 |
| work_keys_str_mv | AT kelsiealeary characterizationofproteinmembraneinteractionsinyeastautophagy AT michaeljragusa characterizationofproteinmembraneinteractionsinyeastautophagy |