Cap binding-independent recruitment of eIF4E to cytoplasmic foci

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...

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Autores principales: Ferrero, Paola Viviana, Layana, Carla, Paulucci, Ezequiel, Gutiérrez, Pablo S., Hernández, Greco, Rivera Pomar, Rolando Víctor
Formato: Articulo
Lenguaje:Inglés
Publicado: 2012
Materias:
Ciencias Exactas
Cap-binding
EIF4E
P-body
Stress granule
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/84709
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-84709
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Cap-binding
EIF4E
P-body
Stress granule
spellingShingle Ciencias Exactas
Cap-binding
EIF4E
P-body
Stress granule
Ferrero, Paola Viviana
Layana, Carla
Paulucci, Ezequiel
Gutiérrez, Pablo S.
Hernández, Greco
Rivera Pomar, Rolando Víctor
Cap binding-independent recruitment of eIF4E to cytoplasmic foci
topic_facet Ciencias Exactas
Cap-binding
EIF4E
P-body
Stress granule
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.
format Articulo
Articulo
author Ferrero, Paola Viviana
Layana, Carla
Paulucci, Ezequiel
Gutiérrez, Pablo S.
Hernández, Greco
Rivera Pomar, Rolando Víctor
author_facet Ferrero, Paola Viviana
Layana, Carla
Paulucci, Ezequiel
Gutiérrez, Pablo S.
Hernández, Greco
Rivera Pomar, Rolando Víctor
author_sort Ferrero, Paola Viviana
title Cap binding-independent recruitment of eIF4E to cytoplasmic foci
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
publishDate 2012
url http://sedici.unlp.edu.ar/handle/10915/84709
work_keys_str_mv AT ferreropaolaviviana capbindingindependentrecruitmentofeif4etocytoplasmicfoci
AT layanacarla capbindingindependentrecruitmentofeif4etocytoplasmicfoci
AT paulucciezequiel capbindingindependentrecruitmentofeif4etocytoplasmicfoci
AT gutierrezpablos capbindingindependentrecruitmentofeif4etocytoplasmicfoci
AT hernandezgreco capbindingindependentrecruitmentofeif4etocytoplasmicfoci
AT riverapomarrolandovictor capbindingindependentrecruitmentofeif4etocytoplasmicfoci
bdutipo_str Repositorios
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