Interaction of Tau with Fe65 links tau to APP. (Articolo in rivista)

Type
Label
  • Interaction of Tau with Fe65 links tau to APP. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.nbd.2004.10.011 (literal)
Alternative label
  • Christian Barbato a, b; Nadia Canu a, b, 1; Nicola Zambrano c; Annalucia Serafino b; Giuseppina Minopoli c; Maria Teresa Ciotti b; Giuseppina Amadoro a, b; Tommaso Russo c; Pietro Calissanoa, b. (2005)
    Interaction of Tau with Fe65 links tau to APP.
    in Neurobiology of disease
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Christian Barbato a, b; Nadia Canu a, b, 1; Nicola Zambrano c; Annalucia Serafino b; Giuseppina Minopoli c; Maria Teresa Ciotti b; Giuseppina Amadoro a, b; Tommaso Russo c; Pietro Calissanoa, b. (literal)
Pagina inizio
  • 399 (literal)
Pagina fine
  • 408 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Impact Factor (2005) = 4.048 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 18 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • a Dipartimento di Neuroscienze, Università di Roma Tor Vergata, Via Montpellier 1, 00133 Roma, Italy b Istituto di Neurobiologia e Medicina Molecolare, CNR, Viale Marx 43, 00137 Rome, Italy c Dipartimento di Biochimica e Biotecnologie Biomediche, Università degli Studi di Napoli Federico II, Via S. Pansini 5, and CEINGE Biotecnologie Avanzate SCaRL, Via Comunale Margherita, 424, 80131 Napoli, Italy (literal)
Titolo
  • Interaction of Tau with Fe65 links tau to APP. (literal)
Abstract
  • The beta-amyloid precursor protein APP and the microtubule-associated protein Tau play a crucial role in the pathogenesis of Alzheimer's disease (AD). However, the possible molecular events linking these two proteins are still unknown. Here, we show that Fe65, one of the ligands of the APP cytodomain, is associated with Tau in vivo and in vitro, as demonstrated by co-immunoprecipitation, co-localization, and FRET experiments. Deletion studies indicated that the N-terminal domain of Tau and the PTB1 domain of Fe65 are required for this association. This interaction is regulated by the phosphorylation of Tau at selected sites, by glycogen synthase kinase-3beta (GSK3beta) and cyclin-dependent kinase 5 (Cdk5), and requires an intact microtubule network. Furthermore, laser scanner microscopy and co-immunoprecipitation experiments provide preliminary evidence of possible complex(es) involving Tau, Fe65, APP. These findings open new perspectives for the study of the possible crosstalk between these proteins in the pathogenesis of AD. (literal)
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