MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i>
SNARE proteins reside between opposing membranes and facilitate vesicle fusion, a physiological process ubiquitously required for secretion, endocytosis and autophagy. With age, neurosecretory SNARE activity drops and is pertinent to age-associated neurological disorders. Despite the importance of S...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/4/4230 |
| _version_ | 1797620307758940160 |
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| author | Ilias Gkikas Ioanna Daskalaki Konstantinos Kounakis Nektarios Tavernarakis Eirini Lionaki |
| author_facet | Ilias Gkikas Ioanna Daskalaki Konstantinos Kounakis Nektarios Tavernarakis Eirini Lionaki |
| author_sort | Ilias Gkikas |
| collection | DOAJ |
| description | SNARE proteins reside between opposing membranes and facilitate vesicle fusion, a physiological process ubiquitously required for secretion, endocytosis and autophagy. With age, neurosecretory SNARE activity drops and is pertinent to age-associated neurological disorders. Despite the importance of SNARE complex assembly and disassembly in membrane fusion, their diverse localization hinders the complete understanding of their function. Here, we revealed a subset of SNARE proteins, the syntaxin SYX-17, the synaptobrevins VAMP-7, SNB-6 and the tethering factor USO-1, to be either localized or in close proximity to mitochondria, in vivo. We term them mitoSNAREs and show that animals deficient in mitoSNAREs exhibit increased mitochondria mass and accumulation of autophagosomes. The SNARE disassembly factor NSF-1 seems to be required for the effects of mitoSNARE depletion. Moreover, we find mitoSNAREs to be indispensable for normal aging in both neuronal and non-neuronal tissues. Overall, we uncover a previously unrecognized subset of SNAREs that localize to mitochondria and propose a role of mitoSNARE assembly and disassembly factors in basal autophagy regulation and aging. |
| first_indexed | 2024-03-11T08:39:18Z |
| format | Article |
| id | doaj.art-07a1d2409e704f969aad6d89d4652301 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T08:39:18Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-07a1d2409e704f969aad6d89d46523012023-11-16T21:11:25ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-02-01244423010.3390/ijms24044230MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i>Ilias Gkikas0Ioanna Daskalaki1Konstantinos Kounakis2Nektarios Tavernarakis3Eirini Lionaki4Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, 70013 Heraklion, Crete, GreeceInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, 70013 Heraklion, Crete, GreeceInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, 70013 Heraklion, Crete, GreeceInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, 70013 Heraklion, Crete, GreeceInstitute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, 70013 Heraklion, Crete, GreeceSNARE proteins reside between opposing membranes and facilitate vesicle fusion, a physiological process ubiquitously required for secretion, endocytosis and autophagy. With age, neurosecretory SNARE activity drops and is pertinent to age-associated neurological disorders. Despite the importance of SNARE complex assembly and disassembly in membrane fusion, their diverse localization hinders the complete understanding of their function. Here, we revealed a subset of SNARE proteins, the syntaxin SYX-17, the synaptobrevins VAMP-7, SNB-6 and the tethering factor USO-1, to be either localized or in close proximity to mitochondria, in vivo. We term them mitoSNAREs and show that animals deficient in mitoSNAREs exhibit increased mitochondria mass and accumulation of autophagosomes. The SNARE disassembly factor NSF-1 seems to be required for the effects of mitoSNARE depletion. Moreover, we find mitoSNAREs to be indispensable for normal aging in both neuronal and non-neuronal tissues. Overall, we uncover a previously unrecognized subset of SNAREs that localize to mitochondria and propose a role of mitoSNARE assembly and disassembly factors in basal autophagy regulation and aging.https://www.mdpi.com/1422-0067/24/4/4230mitochondriaSNAREsautophagyagingSYX-17NSF-1 |
| spellingShingle | Ilias Gkikas Ioanna Daskalaki Konstantinos Kounakis Nektarios Tavernarakis Eirini Lionaki MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i> International Journal of Molecular Sciences mitochondria SNAREs autophagy aging SYX-17 NSF-1 |
| title | MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i> |
| title_full | MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i> |
| title_fullStr | MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i> |
| title_full_unstemmed | MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i> |
| title_short | MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging in <i>C. elegans</i> |
| title_sort | mitosnare assembly and disassembly factors regulate basal autophagy and aging in i c elegans i |
| topic | mitochondria SNAREs autophagy aging SYX-17 NSF-1 |
| url | https://www.mdpi.com/1422-0067/24/4/4230 |
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