Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation affects G-protein-coupled receptor desensitization.
J Biol Chem
; 286(17): 14830-41, 2011 Apr 29.
Article
em En
| MEDLINE
| ID: mdl-21362625
ABSTRACT
Caveolin (Cav) proteins in the plasma membrane have numerous binding partners, but the determinants of these interactions are poorly understood. We show here that Cav-3 has a small ubiquitin-like modifier (SUMO) consensus motif (ΨKX(D/E, where Ψ is a hydrophobic residue)) near the scaffolding domain and that Cav-3 is SUMOylated in a manner that is enhanced by the SUMO E3 ligase PIASy (protein inhibitor of activated STAT-y). Site-directed mutagenesis revealed that the consensus site lysine is the preferred SUMOylation site but that mutation of all lysines is required to abolish SUMOylation. Co-expression of a SUMOylation-deficient mutant of Cav-3 with ß-adrenergic receptors (ßARs) alters the expression level of ß(2)ARs but not ß(1)ARs following agonist stimulation, thus implicating Cav-3 SUMOylation in the mechanisms for ß(2)AR but not ß(1)AR desensitization. Expression of endothelial nitric-oxide synthase (NOS3) was not altered by the SUMOylation-deficient mutant. Thus, SUMOylation is a covalent modification of caveolins that influence the regulation of certain signaling partners.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Proteínas Inibidoras de STAT Ativados
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Caveolina 3
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Sumoilação
Limite:
Humans
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Estados Unidos