Impaired permeability to IP3 in a mutant connexin underlies recessive hereditary deafness. (Articolo in rivista)

Type

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

Label

• Impaired permeability to IP3 in a mutant connexin underlies recessive hereditary deafness. (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Beltramello M, Piazza V, Bukauskas FF, Pozzan T. and Mammano F, (2005)
  Impaired permeability to IP3 in a mutant connexin underlies recessive hereditary deafness.
  in Nature cell biology
  (literal)

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

• Beltramello M, Piazza V, Bukauskas FF, Pozzan T. and Mammano F, (literal)

Pagina inizio

• 63 (literal)

Pagina fine

• 69 (literal)

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

• 7 (literal)

Rivista

• Nature cell biology (Rivista)

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

• 6 (literal)

Note

• PubMe (literal)

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

• Venetian Institute of Molecular Medicine, via G. Orus 2, 35129 Padua, Italy. (literal)

Titolo

• Impaired permeability to IP3 in a mutant connexin underlies recessive hereditary deafness. (literal)

Abstract

• Connexins are membrane proteins that assemble into gap-junction channels and are responsible for direct, electrical and metabolic coupling between connected cells. Here we describe an investigation of the properties of a recombinantly expressed recessive mutant of connexin 26 (Cx26), the V84L mutant, associated with deafness. Unlike other Cx26 mutations, V84L affects neither intracellular sorting nor electrical coupling, but specifically reduces permeability to the Ca(2+)-mobilizing messenger inositol 1,4,5-trisphosphate (Ins(1,4,5)P(3)). Both the permeability to Lucifer Yellow and the unitary channel conductance of V84L-mutant channels are indistinguishable from those of the wild-type Cx26. Injection of Ins(1,4,5)P(3) into supporting cells of the rat organ of Corti, which abundantly express Cx26, ensues in a regenerative wave of Ca(2+) throughout the tissue. Blocking the gap junction communication abolishes wave propagation. We propose that the V84L mutation reduces metabolic coupling mediated by Ins(1,4,5)P(3) to an extent sufficient to impair the propagation of Ca(2+) waves and the formation of a functional syncytium. Our data provide the first demonstration of a specific defect of metabolic coupling and offer a mechanistic explanation for the pathogenesis of an inherited human disease. (literal)

Prodotto di

• Neurobiologia e Neuropatologia (ME.P02.005.001) (Modulo)
• Institute of neuroscience (IN) (Istituto)

Autore CNR

• TULLIO POZZAN (Unità di personale interno)

Incoming links:

Prodotto

• Institute of neuroscience (IN) (Istituto)
• Neurobiologia e Neuropatologia (ME.P02.005.001) (Modulo)

Autore CNR di

• TULLIO POZZAN (Unità di personale interno)

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

• Nature cell biology (Rivista)