SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L

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 o...

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Autores: Coccia, Elena, Planells Ferrer, Laura, Badillos Rodríguez, Raquel, Pascual Sánchez, Marta, Segura, Miguel F., Fernández Hernández, Rita, López Soriano, Joaquin, Garí, Eloi, Soriano García, Eduardo, Barneda Zahonero, Bruna, Moubarak, Rana S., Pérez García, M. Jose, Comella i Carnicé, Joan Xavier, 1963-
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/159980
Acceso en línea:https://hdl.handle.net/2445/159980
Access Level:acceso abierto
Palabra clave:Apoptosi
Neurociències
Apoptosis
Neurosciences
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spelling SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-LCoccia, ElenaPlanells Ferrer, LauraBadillos Rodríguez, RaquelPascual Sánchez, MartaSegura, Miguel F.Fernández Hernández, RitaLópez Soriano, JoaquinGarí, EloiSoriano García, EduardoBarneda Zahonero, BrunaMoubarak, Rana S.Pérez García, M. JoseComella i Carnicé, Joan Xavier, 1963-ApoptosiNeurociènciesApoptosisNeurosciencesThe 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.Nature Publishing Group2020202020202020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion19 p.application/pdfhttps://hdl.handle.net/2445/159980Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: https://doi.org/10.1038/s41419-020-2282-xCell Death and Disease, 2020, vol. 11, num. 2, p. 82https://doi.org/10.1038/s41419-020-2282-xcc-by-nc-sa (c) Coccia, Elena et al., 2020http://creativecommons.org/licenses/by-nc-sa/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/1599802026-05-29T05:05:01Z
dc.title.none.fl_str_mv SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
title SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
spellingShingle SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
Coccia, Elena
Apoptosi
Neurociències
Apoptosis
Neurosciences
title_short SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
title_full SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
title_fullStr SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
title_full_unstemmed SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
title_sort SIVA-1 regulates apoptosis and synaptic function by modulating XIAP interaction with the death receptor antagonist FAIM-L
dc.creator.none.fl_str_mv Coccia, Elena
Planells Ferrer, Laura
Badillos Rodríguez, Raquel
Pascual Sánchez, Marta
Segura, Miguel F.
Fernández Hernández, Rita
López Soriano, Joaquin
Garí, Eloi
Soriano García, Eduardo
Barneda Zahonero, Bruna
Moubarak, Rana S.
Pérez García, M. Jose
Comella i Carnicé, Joan Xavier, 1963-
author Coccia, Elena
author_facet Coccia, Elena
Planells Ferrer, Laura
Badillos Rodríguez, Raquel
Pascual Sánchez, Marta
Segura, Miguel F.
Fernández Hernández, Rita
López Soriano, Joaquin
Garí, Eloi
Soriano García, Eduardo
Barneda Zahonero, Bruna
Moubarak, Rana S.
Pérez García, M. Jose
Comella i Carnicé, Joan Xavier, 1963-
author_role author
author2 Planells Ferrer, Laura
Badillos Rodríguez, Raquel
Pascual Sánchez, Marta
Segura, Miguel F.
Fernández Hernández, Rita
López Soriano, Joaquin
Garí, Eloi
Soriano García, Eduardo
Barneda Zahonero, Bruna
Moubarak, Rana S.
Pérez García, M. Jose
Comella i Carnicé, Joan Xavier, 1963-
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Apoptosi
Neurociències
Apoptosis
Neurosciences
topic Apoptosi
Neurociències
Apoptosis
Neurosciences
description 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.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/159980
url https://hdl.handle.net/2445/159980
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.1038/s41419-020-2282-x
Cell Death and Disease, 2020, vol. 11, num. 2, p. 82
https://doi.org/10.1038/s41419-020-2282-x
dc.rights.none.fl_str_mv cc-by-nc-sa (c) Coccia, Elena et al., 2020
http://creativecommons.org/licenses/by-nc-sa/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-sa (c) Coccia, Elena et al., 2020
http://creativecommons.org/licenses/by-nc-sa/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 19 p.
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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