Primary sequence requirements for S-acylation of beta(2)-adrenergic receptor peptides.
FEBS Lett
; 499(1-2): 59-64, 2001 Jun 15.
Article
em En
| MEDLINE
| ID: mdl-11418112
ABSTRACT
Palmitoylation is a post-translational modification that occurs on selected cysteines of many proteins. Since a high proportion of basic and hydrophobic residues is often found near the palmitoylated cysteine, the role of these residues in the selection of specific palmitoylation sites was assessed. Short peptides derived from the beta(2)-adrenergic receptor sequence, modified to present different proportions of basic, acidic and hydrophobic residues, were tested in an in vitro S-acylation assay. Basic residues proved to be essential, whereas hydrophobic residues greatly enhanced S-acylation and acidic residues inhibited it. Taken together, these results show that short peptides contain the required molecular determinants leading to selective S-acylation. Whether or not these sequence characteristics also contribute to the selectivity of palmitoylation in vivo will need to be further investigated.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Processamento de Proteína Pós-Traducional
/
Receptores Adrenérgicos beta 2
/
Ácido Palmítico
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Canadá