TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death
- Autores
- Seillier, M.; Peuget, S.; Gayet, O.; Gauthier, C.; N'Guessan, P.; Monte, Martin; Carrier, A.; Iovanna, J. L.; Dusetti, N. J.
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- TP53INP1 (tumor protein 53-induced nuclear protein 1) is a tumor suppressor, whose expression is downregulated in cancers from different organs. It was described as a p53 target gene involved in cell death, cell-cycle arrest and cellular migration. In this work, we show that TP53INP1 is also able to interact with ATG8-family proteins and to induce autophagy-dependent cell death. In agreement with this finding, we observe that TP53INP1, which is mainly nuclear, relocalizes in autophagosomes during autophagy where it is eventually degraded. TP53INP1-LC3 interaction occurs via a functional LC3-interacting region (LIR). Inactivating mutations of this sequence abolish TP53INP1-LC3 interaction, relocalize TP53INP1 in autophagosomes and decrease TP53INP1 ability to trigger cell death. Interestingly, TP53INP1 binds to ATG8-family proteins with higher affinity than p62, suggesting that it could partially displace p62 from autophagosomes, modifying thereby their composition. Moreover, silencing the expression of autophagy related genes (ATG5 or Beclin-1) or inhibiting caspase activity significantly decreases cell death induced by TP53INP1. These data indicate that cell death observed after TP53INP1-LC3 interaction depends on both autophagy and caspase activity. We conclude that TP53INP1 could act as a tumor suppressor by inducing cell death by caspase-dependent autophagy. © 2012 Macmillan Publishers Limited All rights reserved.
Fil: Seillier, M.. Inserm; Francia. Aix-Marseille Université; Francia
Fil: Peuget, S.. Inserm; Francia. Aix-Marseille Université; Francia
Fil: Gayet, O.. Inserm; Francia. Aix-Marseille Université; Francia
Fil: Gauthier, C.. Inserm; Francia. Aix-Marseille Université; Francia
Fil: N'Guessan, P.. Inserm; Francia. Aix-Marseille Université; Francia
Fil: Monte, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Carrier, A.. Aix-Marseille Université; Francia. Inserm; Francia
Fil: Iovanna, J. L.. Aix-Marseille Université; Francia. Inserm; Francia
Fil: Dusetti, N. J.. Aix-Marseille Université; Francia. Inserm; Francia - Materia
-
Autophagy
Lc3
P53
P62
Tumor Suppressor - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/60927
Ver los metadatos del registro completo
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TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell deathSeillier, M.Peuget, S.Gayet, O.Gauthier, C.N'Guessan, P.Monte, MartinCarrier, A.Iovanna, J. L.Dusetti, N. J.AutophagyLc3P53P62Tumor Suppressorhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1TP53INP1 (tumor protein 53-induced nuclear protein 1) is a tumor suppressor, whose expression is downregulated in cancers from different organs. It was described as a p53 target gene involved in cell death, cell-cycle arrest and cellular migration. In this work, we show that TP53INP1 is also able to interact with ATG8-family proteins and to induce autophagy-dependent cell death. In agreement with this finding, we observe that TP53INP1, which is mainly nuclear, relocalizes in autophagosomes during autophagy where it is eventually degraded. TP53INP1-LC3 interaction occurs via a functional LC3-interacting region (LIR). Inactivating mutations of this sequence abolish TP53INP1-LC3 interaction, relocalize TP53INP1 in autophagosomes and decrease TP53INP1 ability to trigger cell death. Interestingly, TP53INP1 binds to ATG8-family proteins with higher affinity than p62, suggesting that it could partially displace p62 from autophagosomes, modifying thereby their composition. Moreover, silencing the expression of autophagy related genes (ATG5 or Beclin-1) or inhibiting caspase activity significantly decreases cell death induced by TP53INP1. These data indicate that cell death observed after TP53INP1-LC3 interaction depends on both autophagy and caspase activity. We conclude that TP53INP1 could act as a tumor suppressor by inducing cell death by caspase-dependent autophagy. © 2012 Macmillan Publishers Limited All rights reserved.Fil: Seillier, M.. Inserm; Francia. Aix-Marseille Université; FranciaFil: Peuget, S.. Inserm; Francia. Aix-Marseille Université; FranciaFil: Gayet, O.. Inserm; Francia. Aix-Marseille Université; FranciaFil: Gauthier, C.. Inserm; Francia. Aix-Marseille Université; FranciaFil: N'Guessan, P.. Inserm; Francia. Aix-Marseille Université; FranciaFil: Monte, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Carrier, A.. Aix-Marseille Université; Francia. Inserm; FranciaFil: Iovanna, J. L.. Aix-Marseille Université; Francia. Inserm; FranciaFil: Dusetti, N. J.. Aix-Marseille Université; Francia. Inserm; FranciaNature Publishing Group2012-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/60927Seillier, M.; Peuget, S.; Gayet, O.; Gauthier, C.; N'Guessan, P.; et al.; TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death; Nature Publishing Group; Cell Death and Differentiation; 19; 9; 9-2012; 1525-15351350-9047CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1038/cdd.2012.30info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/cdd201230info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:46:18Zoai:ri.conicet.gov.ar:11336/60927instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:46:18.436CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death |
title |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death |
spellingShingle |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death Seillier, M. Autophagy Lc3 P53 P62 Tumor Suppressor |
title_short |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death |
title_full |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death |
title_fullStr |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death |
title_full_unstemmed |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death |
title_sort |
TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death |
dc.creator.none.fl_str_mv |
Seillier, M. Peuget, S. Gayet, O. Gauthier, C. N'Guessan, P. Monte, Martin Carrier, A. Iovanna, J. L. Dusetti, N. J. |
author |
Seillier, M. |
author_facet |
Seillier, M. Peuget, S. Gayet, O. Gauthier, C. N'Guessan, P. Monte, Martin Carrier, A. Iovanna, J. L. Dusetti, N. J. |
author_role |
author |
author2 |
Peuget, S. Gayet, O. Gauthier, C. N'Guessan, P. Monte, Martin Carrier, A. Iovanna, J. L. Dusetti, N. J. |
author2_role |
author author author author author author author author |
dc.subject.none.fl_str_mv |
Autophagy Lc3 P53 P62 Tumor Suppressor |
topic |
Autophagy Lc3 P53 P62 Tumor Suppressor |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
TP53INP1 (tumor protein 53-induced nuclear protein 1) is a tumor suppressor, whose expression is downregulated in cancers from different organs. It was described as a p53 target gene involved in cell death, cell-cycle arrest and cellular migration. In this work, we show that TP53INP1 is also able to interact with ATG8-family proteins and to induce autophagy-dependent cell death. In agreement with this finding, we observe that TP53INP1, which is mainly nuclear, relocalizes in autophagosomes during autophagy where it is eventually degraded. TP53INP1-LC3 interaction occurs via a functional LC3-interacting region (LIR). Inactivating mutations of this sequence abolish TP53INP1-LC3 interaction, relocalize TP53INP1 in autophagosomes and decrease TP53INP1 ability to trigger cell death. Interestingly, TP53INP1 binds to ATG8-family proteins with higher affinity than p62, suggesting that it could partially displace p62 from autophagosomes, modifying thereby their composition. Moreover, silencing the expression of autophagy related genes (ATG5 or Beclin-1) or inhibiting caspase activity significantly decreases cell death induced by TP53INP1. These data indicate that cell death observed after TP53INP1-LC3 interaction depends on both autophagy and caspase activity. We conclude that TP53INP1 could act as a tumor suppressor by inducing cell death by caspase-dependent autophagy. © 2012 Macmillan Publishers Limited All rights reserved. Fil: Seillier, M.. Inserm; Francia. Aix-Marseille Université; Francia Fil: Peuget, S.. Inserm; Francia. Aix-Marseille Université; Francia Fil: Gayet, O.. Inserm; Francia. Aix-Marseille Université; Francia Fil: Gauthier, C.. Inserm; Francia. Aix-Marseille Université; Francia Fil: N'Guessan, P.. Inserm; Francia. Aix-Marseille Université; Francia Fil: Monte, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Carrier, A.. Aix-Marseille Université; Francia. Inserm; Francia Fil: Iovanna, J. L.. Aix-Marseille Université; Francia. Inserm; Francia Fil: Dusetti, N. J.. Aix-Marseille Université; Francia. Inserm; Francia |
description |
TP53INP1 (tumor protein 53-induced nuclear protein 1) is a tumor suppressor, whose expression is downregulated in cancers from different organs. It was described as a p53 target gene involved in cell death, cell-cycle arrest and cellular migration. In this work, we show that TP53INP1 is also able to interact with ATG8-family proteins and to induce autophagy-dependent cell death. In agreement with this finding, we observe that TP53INP1, which is mainly nuclear, relocalizes in autophagosomes during autophagy where it is eventually degraded. TP53INP1-LC3 interaction occurs via a functional LC3-interacting region (LIR). Inactivating mutations of this sequence abolish TP53INP1-LC3 interaction, relocalize TP53INP1 in autophagosomes and decrease TP53INP1 ability to trigger cell death. Interestingly, TP53INP1 binds to ATG8-family proteins with higher affinity than p62, suggesting that it could partially displace p62 from autophagosomes, modifying thereby their composition. Moreover, silencing the expression of autophagy related genes (ATG5 or Beclin-1) or inhibiting caspase activity significantly decreases cell death induced by TP53INP1. These data indicate that cell death observed after TP53INP1-LC3 interaction depends on both autophagy and caspase activity. We conclude that TP53INP1 could act as a tumor suppressor by inducing cell death by caspase-dependent autophagy. © 2012 Macmillan Publishers Limited All rights reserved. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-09 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/60927 Seillier, M.; Peuget, S.; Gayet, O.; Gauthier, C.; N'Guessan, P.; et al.; TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death; Nature Publishing Group; Cell Death and Differentiation; 19; 9; 9-2012; 1525-1535 1350-9047 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/60927 |
identifier_str_mv |
Seillier, M.; Peuget, S.; Gayet, O.; Gauthier, C.; N'Guessan, P.; et al.; TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins through the LC3-interacting region (LIR) and promotes autophagy-dependent cell death; Nature Publishing Group; Cell Death and Differentiation; 19; 9; 9-2012; 1525-1535 1350-9047 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1038/cdd.2012.30 info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/cdd201230 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf 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 |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |