Rea, Antonio (2025) TEX2 controls mitochondrial dynamics at ER-mitochondria MCSs. [Tesi di dottorato]
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| Tipologia del documento: | Tesi di dottorato |
|---|---|
| Lingua: | English |
| Titolo: | TEX2 controls mitochondrial dynamics at ER-mitochondria MCSs |
| Autori: | Autore Email Rea, Antonio antoniorea.posta@gmail.com |
| Data: | 9 Dicembre 2025 |
| Numero di pagine: | 175 |
| Istituzione: | Università degli Studi di Napoli Federico II |
| Dipartimento: | Scuola Superiore Meridionale |
| Dottorato: | Genomic and experimental medicine |
| Ciclo di dottorato: | 37 |
| Coordinatore del Corso di dottorato: | nome email Franco, Brunella franco@tigem.it |
| Tutor: | nome email De Matteis, Maria Antonietta [non definito] |
| Data: | 9 Dicembre 2025 |
| Numero di pagine: | 175 |
| Parole chiave: | TEX2; MAM; ER-mitochondria; LTP; membrane contact sites |
| Settori scientifico-disciplinari del MIUR: | Area 05 - Scienze biologiche > BIO/10 - Biochimica Area 05 - Scienze biologiche > BIO/11 - Biologia molecolare Area 05 - Scienze biologiche > BIO/13 - Biologia applicata Area 05 - Scienze biologiche > BIO/18 - Genetica |
| Informazioni aggiuntive: | 37 ciclo |
| Depositato il: | 20 Gen 2026 16:25 |
| Ultima modifica: | 02 Set 2026 08:08 |
| URI: | https://www.fedoa.unina.it/id/eprint/16852 |
Abstract
This work identifies TEX2 as a conserved ER-resident protein that functions as a novel tether at ER–mitochondria contact sites (MAMs). TEX2 localizes to tubular ER subdomains enriched at MAMs, and its depletion reduces ER–mitochondria contacts, impairs DRP1 activation, and causes mitochondrial elongation, indicating a key role in mitochondrial fission. TEX2 interacts with the mitochondrial protein FUNDC1, and both proteins act in the same pathway to sustain MAM structure and organelle remodeling. Through its SMP domain, TEX2 likely mediates ceramide transfer to mitochondria, generating lipid environments that facilitate membrane constriction and DRP1 recruitment. Beyond MAMs, TEX2 also functions at ER–lysosome contacts via TMEM55B, and its loss alters mitochondria–lysosome coupling, supporting a model in which TEX2 coordinates communication across multiple organelles. Overall, TEX2 emerges as a lipid-transfer tether that integrates structural and metabolic signals to regulate mitochondrial dynamics and inter-organelle connectivity.
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