The molecular chaperone Hsp90 is a component of the cap-binding complex and interacts with the translational repressor Cup during Drosophila oogenesis (Articolo in rivista)

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  • The molecular chaperone Hsp90 is a component of the cap-binding complex and interacts with the translational repressor Cup during Drosophila oogenesis (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.gene.2008.11.025 (literal)
Alternative label
  • Pisa V.; Cozzolino M.; Gargiulo S.; Ottone C.; Piccioni F.; Monti M.; Gigliotti S.; Talamo F.; Graziani F.; Pucci P.; Verrotti A.C. (2009)
    The molecular chaperone Hsp90 is a component of the cap-binding complex and interacts with the translational repressor Cup during Drosophila oogenesis
    in Gene (Amst.)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Pisa V.; Cozzolino M.; Gargiulo S.; Ottone C.; Piccioni F.; Monti M.; Gigliotti S.; Talamo F.; Graziani F.; Pucci P.; Verrotti A.C. (literal)
Pagina inizio
  • 67 (literal)
Pagina fine
  • 74 (literal)
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  • 432 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • PMID: 19101615 (literal)
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  • 1-2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CEINGE-Biotecnologie Avanzate, Italy SEMM-European School of Molecular Medicine, Via Comunale Margherita 482, 80145 Naples, Italy Dipartimento di Biochimica e Biotecnologie Mediche, Italy School of Biotechnological Sciences, Università di Napoli \"FedericoII\", Via S. Pansini 5, 80131 Naples, Italy Dipartimento di Chimica Organica e Biochimica, Università di Napoli \"Federico II\", Via Cinthia 4, 80126 Naples, Italy Institute of Genetics and Biophysics \"A. Buzzati Traverso\", CNR, Via P. Castellino 111, 80131 Naples, Italy Istituto di Ricerche di Biologia Molecolare (IRBM) \"P. Angeletti\", Via Pontina Km 30,600, 00040 Pomezia, Rome, Italy (literal)
Titolo
  • The molecular chaperone Hsp90 is a component of the cap-binding complex and interacts with the translational repressor Cup during Drosophila oogenesis (literal)
Abstract
  • In metazoa, the spatio-temporal translation of diverse mRNAs is essential to guarantee proper oocyte maturation and early embryogenesis. The eukaryotic translation initiation factor 4E (eIF4E), which binds the 5' cap structure of eukaryotic mRNAs, associates with either stimulatory or inhibitory factors to modulate protein synthesis. In order to identify novel factors that might act at the translational level during Drosophila oogenesis, we have undertaken a functional proteomic approach and isolated the product of the Hsp83 gene, the evolutionarily conserved chaperone Hsp90, as a specific component of the cap-binding complex. Here we report that Hsp90 interacts in vitro with the translational repressor Cup. In addition, we show that Hsp83 and cup interact genetically, since lowering Hsp90 activity enhances the oogenesis alterations linked to diverse cup mutant alleles. Hsp90 and Cup co-localize in the cytoplasm of the developing germ-line cells within the germarium, thus suggesting a common function from the earliest stages of oogenesis. Taken together, our data start elucidating the role of Hsp90 during Drosophila female germ-line development and strengthen the idea that Cup has multiple essential functions during egg chamber development. (literal)
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