Canavanine inhibits vimentin assembly but not its synthesis in chicken embryo erythroid cells.
J Cell Biol
; 97(4): 1309-14, 1983 Oct.
Article
em En
| MEDLINE
| ID: mdl-6684664
ABSTRACT
In chicken embryo erythroid cells, newly synthesized vimentin first enters a Triton X-100 (TX-100)-soluble pool and subsequently assembles posttranslationally into TX-100-insoluble vimentin filaments (Blikstad I., and E. Lazarides, J. Cell Biol., 961803-1808). Here we show that incubation of chicken embryo erythroid cells in a medium in which arginine has been substituted by its amino acid analogue, canavanine, results in the inhibition of the posttranslational assembly of vimentin into the TX-100-insoluble filaments. Immunoprecipitation and subsequent SDS gel electrophoresis showed that the synthesis of canavanine-vimentin is not inhibited and that it accumulates in the TX-100-soluble compartment. Pulse-chase experiments with [35S]methionine demonstrated that while arginine-vimentin can be rapidly chased from the soluble to the cytoskeletal fraction, canavanine-vimentin remains in the soluble fraction, where it turns over. The effect of canavanine on the assembly of vimentin did not prevent the assembly of arginine-vimentin, as cells labeled with [35S]methionine first in the presence of canavanine and then in the presence of arginine contained labeled canavanine-vimentin only in the soluble fraction, and arginine-vimentin in both the soluble and cytoskeletal fractions. These results suggest that arginine residues play an essential role in the assembly of vimentin in vivo.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Citoesqueleto
/
Canavanina
/
Processamento de Proteína Pós-Traducional
/
Eritrócitos
/
Proteínas de Filamentos Intermediários
Limite:
Animals
Idioma:
En
Ano de publicação:
1983
Tipo de documento:
Article