Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 1 de 1
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
Biosci Biotechnol Biochem ; 76(6): 1201-9, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-22790947

RESUMO

The subcellular localization of 13 recently identified N-myristoylated proteins and the effects of overexpression of these proteins on cellular morphology were examined with the aim of understanding the physiological roles of the protein N-myristoylation that occurs on these proteins. Immunofluorescence staining of HEK293T cells transfected with cDNAs coding for the proteins revealed that most of them were associated with the plasma membrane or the membranes of intracellular compartments, and did not affect cellular morphology. However, two proteins, formin-like2 (FMNL2) and formin-like3 (FMNL3), both of them are members of the formin family of proteins, were associated mainly with the plasma membrane and induced significant cellular morphological changes. Inhibition of protein N-myristoylation by replacement of Gly2 with Ala or by the use of N-myristoylation inhibitor significantly inhibited membrane localization and the induction of cellular morphological changes, indicating that protein N-myristoylation plays critical roles in the cellular morphological changes induced by FMNL2 and FMNL3.


Assuntos
Membrana Celular/metabolismo , Ácido Mirístico/metabolismo , Processamento de Proteína Pós-Traducional , Proteínas/metabolismo , Alanina/genética , Alanina/metabolismo , Membrana Celular/genética , Imunofluorescência , Forminas , Expressão Gênica , Glicina/genética , Glicina/metabolismo , Células HEK293 , Humanos , Plasmídeos , Proteínas/genética , Transfecção
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...