Comparative effects of PKB- alpha and PKC- zeta on the phosphorylation of GLUT4-containing vesicles in rat adipocytes
The Korean Journal of Physiology and Pharmacology
;
: 487-496, 2000.
Artículo
en Inglés
| WPRIM
| ID: wpr-728126
ABSTRACT
Insulin stimulates glucose transport in muscle and fat cells by promoting the translocation of glucose transporter (GLUT4) to the cell surface. Phosphatidylinositide 3-kinase (PI3-kinase) has been implicated in this process. However, the involvement of protein kinase B (PKB)/Akt and PKC- zeta, those are known as the downstream target of PI3-kinase in regulation of GLUT4 translocation, is not known yet. An interesting possibility is that these protein kinases phosphorylate GLUT4 directly in this process. In the present study, PKB- alpha and PKC- zeta were added exogenously to GLUT4-containing vesicles purified from low density microsome (LDM) of the rat adipocytes by immunoadsorption and immunoprecipitation for direct phosphorylation of GLUT4. Interestingly GLUT4 was phosphorylated by PKC- zeta and its phosphorylation was increased in insulin stimulated state but GLUT4 was not phosphorylated by PKB- alpha. However, the GST-fusion proteins, GLUT4 C-terminal cytoplasmic domain (GLUT4C) and the entire major GLUT4 cytoplasmic domain corresponding to N-terminus, central loop and C-terminus in tandem (GLUT4NLC) were phosphorylated by both PKB- alpha and PKC- zeta. The immunoblots of PKC- zeta and PKB- alpha antibodies with GLUT4-containing vesicles preparation showed that PKC- zeta was co-localized with the vesicles but not PKB- alpha. From the above results, it is clear that PKC- zeta interacts with GLUT4-containing vesicles and it phosphorylates GLUT4 protein directly but PKB- alpha does not interact with GLUT4, suggesting that insulin-elicited signals that pass through PI3-kinase subsequently diverge into two independent pathways, an Akt pathway and a PKC- zeta pathway, and that later pathway contributes, at least in part, insulin stimulation of GLUT4 translocation in adipocytes via a direct GLUT4 phosphorylation.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Fosforilación
/
Proteínas Quinasas
/
Adipocitos
/
Fosfatidilinositol 3-Quinasas
/
Citoplasma
/
Inmunoprecipitación
/
Proteínas Proto-Oncogénicas c-akt
/
Proteínas Facilitadoras del Transporte de la Glucosa
/
Transportador de Glucosa de Tipo 4
/
Glucosa
Límite:
Animales
Idioma:
Inglés
Revista:
The Korean Journal of Physiology and Pharmacology
Año:
2000
Tipo del documento:
Artículo
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