Cap binding-independent recruitment of eIF4E to cytoplasmic foci

Autores
Ferrero, Paola V.; Layana, Carla; Paulucci, Ezequiel; Gutiérrez, Pablo; Hernández, Greco; Rivera Pomar, Rolando
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Eukaryotic translation initiation factor 4E (eIF4E) is required for cap-dependent initiation. In addition, eIF4E occurs in cytoplasmic foci such as processing bodies (PB) and stress granules (SG). We examined the role of key functional amino acid residues of eIF4E in the recruitment of this protein to cytoplasmic foci. We demonstrate that tryptophan residues required for mRNA cap recognition are not required for the recruitment of eIF4E to SG or PB. We show that a tryptophan residue required for protein-protein interactions is essential for the accumulation of eIF4E in granules. Moreover, we show, by the analysis of two Drosophila eIF4E isoforms, that the tryptophan residue is the common feature for eIF4E for the transfer of active mRNA from polysomes to other ribonucleoprotein particles in the cytoplasm. This residue resides in a putative interaction domain different than the eIF4E-BP domain. We conclude that protein-protein interactions rather than interactions with the mRNA are essential for the recruitment of eIF4E and for a putative nucleation function.
Fil: Ferrero, Paola V.. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina
Fil: Layana, Carla. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Paulucci, Ezequiel. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Gutiérrez, Pablo. Universidad Nacional de La Plata; Argentina
Fil: Hernández, Greco. No especifíca;
Fil: Rivera Pomar, Rolando. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
CAP-BINDING
EIF4E
P-BODY
STRESS GRANULE
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:11336/196239
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cap binding-independent recruitment of eIF4E to cytoplasmic fociFerrero, Paola V.Layana, CarlaPaulucci, EzequielGutiérrez, PabloHernández, GrecoRivera Pomar, RolandoCAP-BINDINGEIF4EP-BODYSTRESS GRANULEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Eukaryotic translation initiation factor 4E (eIF4E) is required for cap-dependent initiation. In addition, eIF4E occurs in cytoplasmic foci such as processing bodies (PB) and stress granules (SG). We examined the role of key functional amino acid residues of eIF4E in the recruitment of this protein to cytoplasmic foci. We demonstrate that tryptophan residues required for mRNA cap recognition are not required for the recruitment of eIF4E to SG or PB. We show that a tryptophan residue required for protein-protein interactions is essential for the accumulation of eIF4E in granules. Moreover, we show, by the analysis of two Drosophila eIF4E isoforms, that the tryptophan residue is the common feature for eIF4E for the transfer of active mRNA from polysomes to other ribonucleoprotein particles in the cytoplasm. This residue resides in a putative interaction domain different than the eIF4E-BP domain. We conclude that protein-protein interactions rather than interactions with the mRNA are essential for the recruitment of eIF4E and for a putative nucleation function.Fil: Ferrero, Paola V.. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; ArgentinaFil: Layana, Carla. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Paulucci, Ezequiel. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Gutiérrez, Pablo. Universidad Nacional de La Plata; ArgentinaFil: Hernández, Greco. No especifíca;Fil: Rivera Pomar, Rolando. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Science2012-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/196239Ferrero, Paola V.; Layana, Carla; Paulucci, Ezequiel; Gutiérrez, Pablo; Hernández, Greco; et al.; Cap binding-independent recruitment of eIF4E to cytoplasmic foci; Elsevier Science; Biochimica et Biophysica Acta-Molecular Cell Research; 1823; 7; 4-2012; 1217-12240167-4889CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0167488912000791info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamcr.2012.03.013info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:43:50Zoai:ri.conicet.gov.ar:11336/196239instacron: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 09:43:50.806CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cap binding-independent recruitment of eIF4E to cytoplasmic foci
title Cap binding-independent recruitment of eIF4E to cytoplasmic foci
spellingShingle Cap binding-independent recruitment of eIF4E to cytoplasmic foci
Ferrero, Paola V.
CAP-BINDING
EIF4E
P-BODY
STRESS GRANULE
title_short Cap binding-independent recruitment of eIF4E to cytoplasmic foci
title_full Cap binding-independent recruitment of eIF4E to cytoplasmic foci
title_fullStr Cap binding-independent recruitment of eIF4E to cytoplasmic foci
title_full_unstemmed Cap binding-independent recruitment of eIF4E to cytoplasmic foci
title_sort Cap binding-independent recruitment of eIF4E to cytoplasmic foci
dc.creator.none.fl_str_mv Ferrero, Paola V.
Layana, Carla
Paulucci, Ezequiel
Gutiérrez, Pablo
Hernández, Greco
Rivera Pomar, Rolando
author Ferrero, Paola V.
author_facet Ferrero, Paola V.
Layana, Carla
Paulucci, Ezequiel
Gutiérrez, Pablo
Hernández, Greco
Rivera Pomar, Rolando
author_role author
author2 Layana, Carla
Paulucci, Ezequiel
Gutiérrez, Pablo
Hernández, Greco
Rivera Pomar, Rolando
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv CAP-BINDING
EIF4E
P-BODY
STRESS GRANULE
topic CAP-BINDING
EIF4E
P-BODY
STRESS GRANULE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Eukaryotic translation initiation factor 4E (eIF4E) is required for cap-dependent initiation. In addition, eIF4E occurs in cytoplasmic foci such as processing bodies (PB) and stress granules (SG). We examined the role of key functional amino acid residues of eIF4E in the recruitment of this protein to cytoplasmic foci. We demonstrate that tryptophan residues required for mRNA cap recognition are not required for the recruitment of eIF4E to SG or PB. We show that a tryptophan residue required for protein-protein interactions is essential for the accumulation of eIF4E in granules. Moreover, we show, by the analysis of two Drosophila eIF4E isoforms, that the tryptophan residue is the common feature for eIF4E for the transfer of active mRNA from polysomes to other ribonucleoprotein particles in the cytoplasm. This residue resides in a putative interaction domain different than the eIF4E-BP domain. We conclude that protein-protein interactions rather than interactions with the mRNA are essential for the recruitment of eIF4E and for a putative nucleation function.
Fil: Ferrero, Paola V.. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina
Fil: Layana, Carla. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Paulucci, Ezequiel. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Gutiérrez, Pablo. Universidad Nacional de La Plata; Argentina
Fil: Hernández, Greco. No especifíca;
Fil: Rivera Pomar, Rolando. Universidad Nacional del Noroeste de la Provincia de Buenos Aires; Argentina. Universidad Nacional de La Plata. Centro Regional de Estudios Genómicos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Eukaryotic translation initiation factor 4E (eIF4E) is required for cap-dependent initiation. In addition, eIF4E occurs in cytoplasmic foci such as processing bodies (PB) and stress granules (SG). We examined the role of key functional amino acid residues of eIF4E in the recruitment of this protein to cytoplasmic foci. We demonstrate that tryptophan residues required for mRNA cap recognition are not required for the recruitment of eIF4E to SG or PB. We show that a tryptophan residue required for protein-protein interactions is essential for the accumulation of eIF4E in granules. Moreover, we show, by the analysis of two Drosophila eIF4E isoforms, that the tryptophan residue is the common feature for eIF4E for the transfer of active mRNA from polysomes to other ribonucleoprotein particles in the cytoplasm. This residue resides in a putative interaction domain different than the eIF4E-BP domain. We conclude that protein-protein interactions rather than interactions with the mRNA are essential for the recruitment of eIF4E and for a putative nucleation function.
publishDate 2012
dc.date.none.fl_str_mv 2012-04
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/11336/196239
Ferrero, Paola V.; Layana, Carla; Paulucci, Ezequiel; Gutiérrez, Pablo; Hernández, Greco; et al.; Cap binding-independent recruitment of eIF4E to cytoplasmic foci; Elsevier Science; Biochimica et Biophysica Acta-Molecular Cell Research; 1823; 7; 4-2012; 1217-1224
0167-4889
CONICET Digital
CONICET
url http://hdl.handle.net/11336/196239
identifier_str_mv Ferrero, Paola V.; Layana, Carla; Paulucci, Ezequiel; Gutiérrez, Pablo; Hernández, Greco; et al.; Cap binding-independent recruitment of eIF4E to cytoplasmic foci; Elsevier Science; Biochimica et Biophysica Acta-Molecular Cell Research; 1823; 7; 4-2012; 1217-1224
0167-4889
CONICET Digital
CONICET
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/S0167488912000791
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamcr.2012.03.013
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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_ 1842268627617710080
score 13.13397

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