Interaction between the cellular prion (PrPC) and the 2P domain K+ channel TREK-1 protein. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Interaction between the cellular prion (PrPC) and the 2P domain K+ channel TREK-1 protein. (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

Alternative label

• Azzalin A, Ferrara V, Arias A, Cerri S, Avella D, Pisu MB, Nano R, Bernocchi G, Ferretti L, Comincini S. (2006)
  Interaction between the cellular prion (PrPC) and the 2P domain K+ channel TREK-1 protein.
  in Biochemical and biophysical research communications (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Azzalin A, Ferrara V, Arias A, Cerri S, Avella D, Pisu MB, Nano R, Bernocchi G, Ferretti L, Comincini S. (literal)

Pagina inizio

• 108 (literal)

Pagina fine

• 115 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 346 (literal)

Rivista

• Biochemical and biophysical research communications (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note

• I.F. 2005: 2.000 (literal)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Interaction between the cellular prion (PrPC) and the 2P domain K+ channel TREK-1 protein. (literal)

Abstract

• The cellular prion protein (PrP(C)) is a highly conserved protein throughout the evolution of mammals and therefore is thought to play important cellular functions. Despite decades of intensive researches, the physiological function of PrP(C) remains enigmatic. Differently, in particular pathological contexts, generally referred as transmissible spongiform encephalopathies, a conformational isoform of PrP(C), i.e., PrP(Sc), is considered the causative agent of these diseases. In this study, we investigated putative PrP(C) cellular functions through the identification of PrP(C) protein interactants. Using a bacterial two-hybrid approach, we identified a novel interaction between PrP(C) and a two-pore potassium channel protein, TREK-1. This interaction was further verified in transfected eukaryotic cells using co-immunoprecipitation and confocal microscopic analysis of the fluorescent transfected proteins. Importantly, in the cerebellar cortex, the endogenous PrP(C) and TREK-1 proteins exhibited co-localization signals in correspondence of the Purkinje cells. Furthermore, a deletion mapping study defined the carboxyl-terminal regions of the two proteins as the possible determinants of the PrP(C)-TREK-1 interaction. Our results indicated a novel PrP(C) interacting protein and suggested that this complex might be relevant in modulating a variety of electrophysiological-dependent cellular responses. (literal)

Prodotto di

• Institute of molecular genetics (IGM) (Istituto)
• Sviluppi metodologici in citometria e applicazioni alla sperimentazione biomedica; in vitro imaging (ME.P06.010.001) (Modulo)

Autore CNR

• GRAZIELLA BERNOCCHI (Unità di personale esterno)

Insieme di parole chiave

• Parole chiave di "Interaction between the cellular prion (PrPC) and the 2P domain K+ channel TREK-1 protein." (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of molecular genetics (IGM) (Istituto)
• Sviluppi metodologici in citometria e applicazioni alla sperimentazione biomedica; in vitro imaging (ME.P06.010.001) (Modulo)

Autore CNR di

• GRAZIELLA BERNOCCHI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biochemical and biophysical research communications (Rivista)

Insieme di parole chiave di

• Parole chiave di "Interaction between the cellular prion (PrPC) and the 2P domain K+ channel TREK-1 protein." (Insieme di parole chiave)