Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase

Autores
Rossi, Mario; Duan, Shanshan; Jeong, Yeon Tae; Horn, Moritz; Saraf, Anita; Florens, Laurence; Washburn, Michael P.; Antebi, Adam; Pagano, Michele
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
F-box proteins and DCAF proteins are the substrate binding subunits of the Skp1-Cul1-F-box protein (SCF) and Cul4-RING protein ligase (CRL4) ubiquitin ligase complexes, respectively. Using affinity purification and mass spectrometry, we determined that the F-box protein FBXO11 interacts with CDT2, a DCAF protein that controls cell-cycle progression, and recruits CDT2 to the SCF(FBXO11)complex to promote its proteasomal degradation. In contrast to most SCF substrates, which exhibit phosphodegron-dependent binding to F-box proteins, CDK-mediated phosphorylation of Thr464 present in the CDT2 degron inhibits recognition by FBXO11. Finally, our results show that the functional interaction between FBXO11 and CDT2 is evolutionary conserved from worms to humans and plays an important role in regulating the timing of cell-cycle exit.
Fil: Rossi, Mario. University Of New York; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigación en Biomedicina de Buenos Aires; Argentina
Fil: Duan, Shanshan. University Of New York; Estados Unidos. Howard Hughes Medical Institute; Estados Unidos
Fil: Jeong, Yeon Tae. University Of New York; Estados Unidos
Fil: Horn, Moritz. Max Planck Institute for Biology of Ageing; Alemania. University of Cologne; Alemania
Fil: Saraf, Anita. The Stowers Institute for Medical Research; Estados Unidos
Fil: Florens, Laurence. The Stowers Institute for Medical Research; Estados Unidos
Fil: Washburn, Michael P.. The Stowers Institute for Medical Research; Estados Unidos. University of Kansas; Estados Unidos
Fil: Antebi, Adam. Max Planck Institute for Biology of Ageing; Alemania. University of Cologne; Alemania
Fil: Pagano, Michele. University Of New York; Estados Unidos. Howard Hughes Medical Institute; Estados Unidos
Materia
Ubiquitin
Hetrechronic genes
SCF complexes
C.eegans
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/12299
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/12299
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligaseRossi, MarioDuan, ShanshanJeong, Yeon TaeHorn, MoritzSaraf, AnitaFlorens, LaurenceWashburn, Michael P.Antebi, AdamPagano, MicheleUbiquitinHetrechronic genesSCF complexesC.eeganshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1F-box proteins and DCAF proteins are the substrate binding subunits of the Skp1-Cul1-F-box protein (SCF) and Cul4-RING protein ligase (CRL4) ubiquitin ligase complexes, respectively. Using affinity purification and mass spectrometry, we determined that the F-box protein FBXO11 interacts with CDT2, a DCAF protein that controls cell-cycle progression, and recruits CDT2 to the SCF(FBXO11)complex to promote its proteasomal degradation. In contrast to most SCF substrates, which exhibit phosphodegron-dependent binding to F-box proteins, CDK-mediated phosphorylation of Thr464 present in the CDT2 degron inhibits recognition by FBXO11. Finally, our results show that the functional interaction between FBXO11 and CDT2 is evolutionary conserved from worms to humans and plays an important role in regulating the timing of cell-cycle exit.Fil: Rossi, Mario. University Of New York; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigación en Biomedicina de Buenos Aires; ArgentinaFil: Duan, Shanshan. University Of New York; Estados Unidos. Howard Hughes Medical Institute; Estados UnidosFil: Jeong, Yeon Tae. University Of New York; Estados UnidosFil: Horn, Moritz. Max Planck Institute for Biology of Ageing; Alemania. University of Cologne; AlemaniaFil: Saraf, Anita. The Stowers Institute for Medical Research; Estados UnidosFil: Florens, Laurence. The Stowers Institute for Medical Research; Estados UnidosFil: Washburn, Michael P.. The Stowers Institute for Medical Research; Estados Unidos. University of Kansas; Estados UnidosFil: Antebi, Adam. Max Planck Institute for Biology of Ageing; Alemania. University of Cologne; AlemaniaFil: Pagano, Michele. University Of New York; Estados Unidos. Howard Hughes Medical Institute; Estados UnidosCell Press2013-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/12299Rossi, Mario; Duan, Shanshan; Jeong, Yeon Tae; Horn, Moritz; Saraf, Anita; et al.; Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase; Cell Press; Molecular Cell; 49; 6; 3-2013; 1159-11661097-2765enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1097276513001317info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcel.2013.02.004info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3624904/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:51:07Zoai:ri.conicet.gov.ar:11336/12299instacron: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:34982025-09-03 09:51:08.212CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
title Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
spellingShingle Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
Rossi, Mario
Ubiquitin
Hetrechronic genes
SCF complexes
C.eegans
title_short Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
title_full Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
title_fullStr Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
title_full_unstemmed Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
title_sort Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase
dc.creator.none.fl_str_mv Rossi, Mario
Duan, Shanshan
Jeong, Yeon Tae
Horn, Moritz
Saraf, Anita
Florens, Laurence
Washburn, Michael P.
Antebi, Adam
Pagano, Michele
author Rossi, Mario
author_facet Rossi, Mario
Duan, Shanshan
Jeong, Yeon Tae
Horn, Moritz
Saraf, Anita
Florens, Laurence
Washburn, Michael P.
Antebi, Adam
Pagano, Michele
author_role author
author2 Duan, Shanshan
Jeong, Yeon Tae
Horn, Moritz
Saraf, Anita
Florens, Laurence
Washburn, Michael P.
Antebi, Adam
Pagano, Michele
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ubiquitin
Hetrechronic genes
SCF complexes
C.eegans
topic Ubiquitin
Hetrechronic genes
SCF complexes
C.eegans
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv F-box proteins and DCAF proteins are the substrate binding subunits of the Skp1-Cul1-F-box protein (SCF) and Cul4-RING protein ligase (CRL4) ubiquitin ligase complexes, respectively. Using affinity purification and mass spectrometry, we determined that the F-box protein FBXO11 interacts with CDT2, a DCAF protein that controls cell-cycle progression, and recruits CDT2 to the SCF(FBXO11)complex to promote its proteasomal degradation. In contrast to most SCF substrates, which exhibit phosphodegron-dependent binding to F-box proteins, CDK-mediated phosphorylation of Thr464 present in the CDT2 degron inhibits recognition by FBXO11. Finally, our results show that the functional interaction between FBXO11 and CDT2 is evolutionary conserved from worms to humans and plays an important role in regulating the timing of cell-cycle exit.
Fil: Rossi, Mario. University Of New York; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigación en Biomedicina de Buenos Aires; Argentina
Fil: Duan, Shanshan. University Of New York; Estados Unidos. Howard Hughes Medical Institute; Estados Unidos
Fil: Jeong, Yeon Tae. University Of New York; Estados Unidos
Fil: Horn, Moritz. Max Planck Institute for Biology of Ageing; Alemania. University of Cologne; Alemania
Fil: Saraf, Anita. The Stowers Institute for Medical Research; Estados Unidos
Fil: Florens, Laurence. The Stowers Institute for Medical Research; Estados Unidos
Fil: Washburn, Michael P.. The Stowers Institute for Medical Research; Estados Unidos. University of Kansas; Estados Unidos
Fil: Antebi, Adam. Max Planck Institute for Biology of Ageing; Alemania. University of Cologne; Alemania
Fil: Pagano, Michele. University Of New York; Estados Unidos. Howard Hughes Medical Institute; Estados Unidos
description F-box proteins and DCAF proteins are the substrate binding subunits of the Skp1-Cul1-F-box protein (SCF) and Cul4-RING protein ligase (CRL4) ubiquitin ligase complexes, respectively. Using affinity purification and mass spectrometry, we determined that the F-box protein FBXO11 interacts with CDT2, a DCAF protein that controls cell-cycle progression, and recruits CDT2 to the SCF(FBXO11)complex to promote its proteasomal degradation. In contrast to most SCF substrates, which exhibit phosphodegron-dependent binding to F-box proteins, CDK-mediated phosphorylation of Thr464 present in the CDT2 degron inhibits recognition by FBXO11. Finally, our results show that the functional interaction between FBXO11 and CDT2 is evolutionary conserved from worms to humans and plays an important role in regulating the timing of cell-cycle exit.
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/11336/12299
Rossi, Mario; Duan, Shanshan; Jeong, Yeon Tae; Horn, Moritz; Saraf, Anita; et al.; Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase; Cell Press; Molecular Cell; 49; 6; 3-2013; 1159-1166
1097-2765
url http://hdl.handle.net/11336/12299
identifier_str_mv Rossi, Mario; Duan, Shanshan; Jeong, Yeon Tae; Horn, Moritz; Saraf, Anita; et al.; Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase; Cell Press; Molecular Cell; 49; 6; 3-2013; 1159-1166
1097-2765
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1097276513001317
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcel.2013.02.004
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3624904/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
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
_version_ 1842269075167772672
score 13.13397

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