Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase

9 páginas, 2 figuras, 5 tablas

Detalles Bibliográficos
Autores: Moreno, Daniel, Viana, Rosa, Sanz, Pascual
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2009
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/112294
Acceso en línea:http://hdl.handle.net/10261/112294
Access Level:acceso abierto
Palabra clave:AMPK
Two-hybrid screening
Proteasome
PSMD11
Phosphorylation
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spelling Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinaseMoreno, DanielViana, RosaSanz, PascualAMPKTwo-hybrid screeningProteasomePSMD11Phosphorylation9 páginas, 2 figuras, 5 tablasMammalian AMP-activated protein kinase (AMPK) is a heterotrimeric serine/threonine protein kinase that acts as a sensor of cellular energy status. It interacts with a great variety of different substrates leading to short term (i.e. regulation of the activity of different enzymes by direct phosphorylation) and long-term effects (i.e. regulation of transcriptional activity of different transcription factors). In this work, we describe the use of the yeast two-hybrid technology to identify additional proteins that interact with the different subunits of AMPK. We have performed three yeast two-hybrid screenings of a human skeletal muscle cDNA library using three different baits: a constitutively active form of AMPK2 (LexA-AMPK2-T172D) co-expressed with AMPK1, LexA-AMPK2 and LexA-AMPK3. Our results identify novel interaction partners of AMPK in human skeletal muscle. We also further characterize the interaction of AMPK with one of these novel interacting proteins, the non-ATPase subunit of the proteasome PSMD11. Our results indicate that AMPK is able to interact physically with this subunit and modify its phosphorylation status, supporting a possible role for AMPK in regulating proteasome function.This work was supported by grants from the Spanish Ministry of Education and Science (SAF2008-01907) and the European Commission (LSHM-CT-2004-005272).Peer reviewedBlake and Helsey EditoresConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201520152009info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/112294reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.biocel.2009.07.002Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1122942026-05-22T06:33:51Z
dc.title.none.fl_str_mv Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
title Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
spellingShingle Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
Moreno, Daniel
AMPK
Two-hybrid screening
Proteasome
PSMD11
Phosphorylation
title_short Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
title_full Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
title_fullStr Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
title_full_unstemmed Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
title_sort Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase
dc.creator.none.fl_str_mv Moreno, Daniel
Viana, Rosa
Sanz, Pascual
author Moreno, Daniel
author_facet Moreno, Daniel
Viana, Rosa
Sanz, Pascual
author_role author
author2 Viana, Rosa
Sanz, Pascual
author2_role author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv AMPK
Two-hybrid screening
Proteasome
PSMD11
Phosphorylation
topic AMPK
Two-hybrid screening
Proteasome
PSMD11
Phosphorylation
description 9 páginas, 2 figuras, 5 tablas
publishDate 2009
dc.date.none.fl_str_mv 2009
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/112294
url http://hdl.handle.net/10261/112294
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.biocel.2009.07.002
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Blake and Helsey Editores
publisher.none.fl_str_mv Blake and Helsey Editores
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869402737368629248
score 15,811543

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