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http://hdl.handle.net/2445/159980
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DC Field | Value | Language |
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dc.contributor.author | Coccia, Elena | - |
dc.contributor.author | Planells Ferrer, Laura | - |
dc.contributor.author | Badillos Rodríguez, Raquel | - |
dc.contributor.author | Pascual Sánchez, Marta | - |
dc.contributor.author | Segura, Miguel F. | - |
dc.contributor.author | Fernández Hernández, Rita | - |
dc.contributor.author | López Soriano, Joaquin | - |
dc.contributor.author | Garí, Eloi | - |
dc.contributor.author | Soriano García, Eduardo | - |
dc.contributor.author | Barneda Zahonero, Bruna | - |
dc.contributor.author | Moubarak, Rana S. | - |
dc.contributor.author | Pérez García, M. Jose | - |
dc.contributor.author | Comella i Carnicé, Joan Xavier, 1963- | - |
dc.date.accessioned | 2020-05-13T10:50:16Z | - |
dc.date.available | 2020-05-13T10:50:16Z | - |
dc.date.issued | 2020-02-03 | - |
dc.identifier.issn | 2041-4889 | - |
dc.identifier.uri | http://hdl.handle.net/2445/159980 | - |
dc.description.abstract | The long isoform of Fas apoptosis inhibitory molecule (FAIM-L) is a neuron-specific death receptor antagonist that modulates apoptotic cell death and mechanisms of neuronal plasticity. FAIM-L exerts its antiapoptotic action by binding to X-linked inhibitor of apoptosis protein (XIAP), an inhibitor of caspases, which are the main effectors of apoptosis. XIAP levels are regulated by the ubiquitin-proteasome pathway. FAIM-L interaction with XIAP prevents the ubiquitination and degradation of the latter, thereby allowing it to inhibit caspase activation. This interaction also modulates non-apoptotic functions of caspases, such as the endocytosis of AMPA receptor (AMPAR) in hippocampal long-term depression (LTD). The molecular mechanism of action exerted by FAIM-L is unclear since the consensus binding motifs are still unknown. Here, we performed a two-hybrid screening to discover novel FAIM-L-interacting proteins. We found a functional interaction of SIVA-1 with FAIM-L. SIVA-1 is a proapoptotic protein that has the capacity to interact with XIAP. We describe how SIVA-1 regulates FAIM-L function by disrupting the interaction of FAIM-L with XIAP, thereby promoting XIAP ubiquitination, caspase-3 activation and neuronal death. Furthermore, we report that SIVA-1 plays a role in receptor internalization in synapses. SIVA-1 is upregulated upon chemical LTD induction, and it modulates AMPAR internalization via non-apoptotic activation of caspases. In summary, our findings uncover SIVA-1 as new functional partner of FAIM-L and demonstrate its role as a regulator of caspase activity in synaptic function. | - |
dc.format.extent | 19 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Nature Publishing Group | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1038/s41419-020-2282-x | - |
dc.relation.ispartof | Cell Death and Disease, 2020, vol. 11, num. 2, p. 82 | - |
dc.relation.uri | https://doi.org/10.1038/s41419-020-2282-x | - |
dc.rights | cc-by-nc-sa (c) Coccia, Elena et al., 2020 | - |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/3.0/es | - |
dc.source | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) | - |
dc.subject.classification | Apoptosi | - |
dc.subject.classification | Neurociències | - |
dc.subject.other | Apoptosis | - |
dc.subject.other | Neurosciences | - |
dc.title | SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 699819 | - |
dc.date.updated | 2020-05-13T10:50:16Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 32015347 | - |
Appears in Collections: | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL)) |
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699819.pdf | 5.12 MB | Adobe PDF | View/Open |
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