Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma

Autores
Chiorazzi, Michael; Rui, Lixin; Yang, Yandan; Ceribelli, Michelle; Tishbi, Nima; Maurer. Carine W.; Ranuncolo, Stella Maris; Zhao, Hong; Xu, Weihong; Chan, Wing Chung C.; Jaffe, Elaine S.; Gascoyne, Randy D.; Campo, Elias; Rossenwald, Andreas; Ott, German; Delabie, Jan; Rimsza, Lisa M.; Shaham, Shai; Staudt, Louis M.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.
Fil: Chiorazzi, Michael. The Rockefeller University; Estados Unidos
Fil: Rui, Lixin. No especifíca;
Fil: Yang, Yandan. No especifíca;
Fil: Ceribelli, Michelle. No especifíca;
Fil: Tishbi, Nima. The Rockefeller University; Estados Unidos
Fil: Maurer. Carine W.. The Rockefeller University; Estados Unidos
Fil: Ranuncolo, Stella Maris. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Oncología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina
Fil: Zhao, Hong. No especifíca;
Fil: Xu, Weihong. No especifíca;
Fil: Chan, Wing Chung C.. No especifíca;
Fil: Jaffe, Elaine S.. No especifíca;
Fil: Gascoyne, Randy D.. No especifíca;
Fil: Campo, Elias. Universidad de Barcelona; España
Fil: Rossenwald, Andreas. Universität Würzburg; Alemania
Fil: Ott, German. No especifíca;
Fil: Delabie, Jan. No especifíca;
Fil: Rimsza, Lisa M.. Arizona State University; Estados Unidos
Fil: Shaham, Shai. The Rockefeller University; Estados Unidos
Fil: Staudt, Louis M.. No especifíca;
Materia
CANCER
UBIQUITIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/2181

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphomaChiorazzi, MichaelRui, LixinYang, YandanCeribelli, MichelleTishbi, NimaMaurer. Carine W.Ranuncolo, Stella MarisZhao, HongXu, WeihongChan, Wing Chung C.Jaffe, Elaine S.Gascoyne, Randy D.Campo, EliasRossenwald, AndreasOtt, GermanDelabie, JanRimsza, Lisa M.Shaham, ShaiStaudt, Louis M.CANCERUBIQUITINhttps://purl.org/becyt/ford/3.2https://purl.org/becyt/ford/3Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.Fil: Chiorazzi, Michael. The Rockefeller University; Estados UnidosFil: Rui, Lixin. No especifíca;Fil: Yang, Yandan. No especifíca;Fil: Ceribelli, Michelle. No especifíca;Fil: Tishbi, Nima. The Rockefeller University; Estados UnidosFil: Maurer. Carine W.. The Rockefeller University; Estados UnidosFil: Ranuncolo, Stella Maris. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Oncología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; ArgentinaFil: Zhao, Hong. No especifíca;Fil: Xu, Weihong. No especifíca;Fil: Chan, Wing Chung C.. No especifíca;Fil: Jaffe, Elaine S.. No especifíca;Fil: Gascoyne, Randy D.. No especifíca;Fil: Campo, Elias. Universidad de Barcelona; EspañaFil: Rossenwald, Andreas. Universität Würzburg; AlemaniaFil: Ott, German. No especifíca;Fil: Delabie, Jan. No especifíca;Fil: Rimsza, Lisa M.. Arizona State University; Estados UnidosFil: Shaham, Shai. The Rockefeller University; Estados UnidosFil: Staudt, Louis M.. No especifíca;National Academy of Sciences2013-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/2181Chiorazzi, Michael; Rui, Lixin; Yang, Yandan; Ceribelli, Michelle; Tishbi, Nima; et al.; Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 110; 10; 3-2013; 3943-39480027-8424enginfo:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/110/10/3943.abstractinfo:eu-repo/semantics/altIdentifier/doi/doi:10.1073/pnas.1217271110info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:54:36Zoai:ri.conicet.gov.ar:11336/2181instacron: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:34982025-10-22 11:54:36.858CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
title Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
spellingShingle Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
Chiorazzi, Michael
CANCER
UBIQUITIN
title_short Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
title_full Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
title_fullStr Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
title_full_unstemmed Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
title_sort Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma
dc.creator.none.fl_str_mv Chiorazzi, Michael
Rui, Lixin
Yang, Yandan
Ceribelli, Michelle
Tishbi, Nima
Maurer. Carine W.
Ranuncolo, Stella Maris
Zhao, Hong
Xu, Weihong
Chan, Wing Chung C.
Jaffe, Elaine S.
Gascoyne, Randy D.
Campo, Elias
Rossenwald, Andreas
Ott, German
Delabie, Jan
Rimsza, Lisa M.
Shaham, Shai
Staudt, Louis M.
author Chiorazzi, Michael
author_facet Chiorazzi, Michael
Rui, Lixin
Yang, Yandan
Ceribelli, Michelle
Tishbi, Nima
Maurer. Carine W.
Ranuncolo, Stella Maris
Zhao, Hong
Xu, Weihong
Chan, Wing Chung C.
Jaffe, Elaine S.
Gascoyne, Randy D.
Campo, Elias
Rossenwald, Andreas
Ott, German
Delabie, Jan
Rimsza, Lisa M.
Shaham, Shai
Staudt, Louis M.
author_role author
author2 Rui, Lixin
Yang, Yandan
Ceribelli, Michelle
Tishbi, Nima
Maurer. Carine W.
Ranuncolo, Stella Maris
Zhao, Hong
Xu, Weihong
Chan, Wing Chung C.
Jaffe, Elaine S.
Gascoyne, Randy D.
Campo, Elias
Rossenwald, Andreas
Ott, German
Delabie, Jan
Rimsza, Lisa M.
Shaham, Shai
Staudt, Louis M.
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CANCER
UBIQUITIN
topic CANCER
UBIQUITIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.2
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.
Fil: Chiorazzi, Michael. The Rockefeller University; Estados Unidos
Fil: Rui, Lixin. No especifíca;
Fil: Yang, Yandan. No especifíca;
Fil: Ceribelli, Michelle. No especifíca;
Fil: Tishbi, Nima. The Rockefeller University; Estados Unidos
Fil: Maurer. Carine W.. The Rockefeller University; Estados Unidos
Fil: Ranuncolo, Stella Maris. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Oncología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay; Argentina
Fil: Zhao, Hong. No especifíca;
Fil: Xu, Weihong. No especifíca;
Fil: Chan, Wing Chung C.. No especifíca;
Fil: Jaffe, Elaine S.. No especifíca;
Fil: Gascoyne, Randy D.. No especifíca;
Fil: Campo, Elias. Universidad de Barcelona; España
Fil: Rossenwald, Andreas. Universität Würzburg; Alemania
Fil: Ott, German. No especifíca;
Fil: Delabie, Jan. No especifíca;
Fil: Rimsza, Lisa M.. Arizona State University; Estados Unidos
Fil: Shaham, Shai. The Rockefeller University; Estados Unidos
Fil: Staudt, Louis M.. No especifíca;
description Cell death is a common metazoan cell fate, and its inactivation is central to human malignancy. In Caenorhabditis elegans, apoptotic cell death occurs via the activation of the caspase CED-3 following binding of the EGL-1/BH3-only protein to the antiapoptotic CED-9/ BCL2 protein. Here we report a major alternative mechanism for caspase activation in vivo involving the F-box protein DRE-1. DRE-1 functions in parallel to EGL-1, requires CED-9 for activity, and binds to CED-9, suggesting that DRE-1 promotes apoptosis by inactivating CED-9. FBXO10, a human protein related to DRE-1, binds BCL2 and promotes its degradation, thereby initiating cell death. Moreover, some human diffuse large B-cell lymphomas have inactivating mutations in FBXO10 or express FBXO10 at low levels. Our results suggest that DRE-1/FBXO10 is a conserved regulator of apoptosis.
publishDate 2013
dc.date.none.fl_str_mv 2013-03
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/11336/2181
Chiorazzi, Michael; Rui, Lixin; Yang, Yandan; Ceribelli, Michelle; Tishbi, Nima; et al.; Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 110; 10; 3-2013; 3943-3948
0027-8424
url http://hdl.handle.net/11336/2181
identifier_str_mv Chiorazzi, Michael; Rui, Lixin; Yang, Yandan; Ceribelli, Michelle; Tishbi, Nima; et al.; Related F-­box proteins control cell death in Caenorhabditis elegans and human lymphoma; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 110; 10; 3-2013; 3943-3948
0027-8424
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/110/10/3943.abstract
info:eu-repo/semantics/altIdentifier/doi/doi:10.1073/pnas.1217271110
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 National Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
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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