"In vivo" toxicity of a truncated version of the Drosophila Rst-IrreC protein is dependent on the presence of a glutamine-rich region in its intracellular domain
An. acad. bras. ciênc
; 74(2): 285-295, June 2002. graf
Article
em En
| LILACS
| ID: lil-314021
Biblioteca responsável:
BR1.1
RESUMO
The roughest-irregular chiasm C ( rst-irreC) gene of Drosophila melanogaster encodes a transmembrane glycoprotein containing five immunoglobulin-like domains in its extracellular portion and an intracytoplasmic tail rich in serine and threonine as well some conserved motifs suggesting signal transduction activity. In the compound eye, loss-of-function rst-irreC mutants lack the characteristic wave of programmed cell death happening in early pupa and which is essential for the elimination of the surplus interommatidial cells. Here we report an investigation on the role played by the Rst-irreC molecule in triggering programmed cell death. "In vivo" transient expression assays showed that deletion of the last 80 amino acids of the carboxyl terminus produces a form of the protein that is highly toxic to larvae. This toxicity is suppressed if an additional 47 amino acid long, glutamine-rich region ("opa-like domain"), is also removed from the protein. The results suggest the possibility that the opa-like domain and the carboxyl terminus act in concert to modulate rst-irreC function in apoptosis, and we discuss this implication in the context of the general mechanisms causing glutamine-rich neurodegenerative diseases in humans
Texto completo:
1
Coleções:
01-internacional
Base de dados:
LILACS
Assunto principal:
Proteínas de Drosophila
/
Drosophila
/
Glutamina
Limite:
Animals
Idioma:
En
Revista:
An. acad. bras. ciênc
Assunto da revista:
CIENCIA
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Brasil