Primary sequence requirements for S‐acylation of β2‐adrenergic receptor peptides

FEBS Letters

Bouvier, Michel¹  Qanbar, Riad¹  Bélanger, Charlène¹  Ansanay, Hervé¹ 

[1] Département de Biochimie and Groupe de Recherche sur le Système Nerveux Autonome, Université de Montréal, C.P. 6128, succursale Centre-Ville, Montréal, QC, Canada H3C 3J7

关键词: Palmitoylation;    Acylation;    Post-translational modification;    Palmitoyl-CoA;    G protein-coupled receptor;    β2-Adrenergic receptor;    MOPS;    3-(N-morpholino)propanesulfonic acid;    DTT;    dithiothreitol;    CoA;    coenzyme A;    TLC;    thin layer chromatography;    β2-AR;    β2-adrenergic receptor;    GPCR;    G protein-coupled receptor;   

DOI  :  10.1016/S0014-5793(01)02513-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 β₂-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.

【 授权许可】

Unknown