A role for protein kinase B beta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes

Hill, M., Clark, S., Tucker, D. F., Birnbaum, M. J., James, D. E. and Macaulay, S. L. (1999) A role for protein kinase B beta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes. Molecular And Cellular Biology, 19 11: 7771-7781.

Author Hill, M.
Clark, S.
Tucker, D. F.
Birnbaum, M. J.
James, D. E.
Macaulay, S. L.
Title A role for protein kinase B beta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes
Journal name Molecular And Cellular Biology   Check publisher's open access policy
ISSN 0270-7306
Publication date 1999
Sub-type Article (original research)
Volume 19
Issue 11
Start page 7771
End page 7781
Total pages 11
Place of publication USA
Publisher American Society for Microbiology
Collection year 1999
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
730105 Endocrine organs and diseases (incl. diabetes)
Abstract Insulin stimulates glucose uptake into muscle and fat cells by promoting the translocation of glucose transporter 4 (GLUT4) to the cell surface. Phosphatidylinositide 3-kinase (PI3K) has been implicated in this process. However, the involvement of protein kinase B (PKB)/Akt, a downstream target of PI3K in regulation of GLUT4 translocation, has been controversial. Here we report that microinjection of a PKB substrate peptide or an antibody to PKB inhibited insulin-stimulated GLUT4 translocation to the plasma membrane by 66 or 56%, respectively. We further examined the activation of PKB isoforms following treatment of cells with insulin or platelet-derived growth factor (PDGF) and found that PKB beta is preferentially expressed in both rat and 3T3-L1 adipocytes, whereas PKB alpha expression is down-regulated in 3T3-L1 adipocytes. A switch in growth factor response was also observed when 3T3-L1 fibroblasts were differentiated into adipocytes. While PDGF was more efficacious than insulin in stimulating PKB phosphorylation in fibroblasts, PDGF did not stimulate PKB beta phosphorylation to any significant extent in adipocytes, as assessed by several methods. Moreover, insulin, but not PDGF, stimulated the translocation of PKB beta to the plasma membrane and high-density microsome fractions of 3T3-L1 adipocytes. These results support a role for PKB beta in insulin-stimulated glucose transport in adipocytes.
Keyword Biochemistry & Molecular Biology
Cell Biology
Rat Adipose-cells
Activated Phosphatidylinositol 3-kinase
Regulatable Glucose Transporter
Glycogen-synthase Kinase-3
B C-akt
3t3-l1 Adipocytes
Potential Role
Phosphoinositide 3-kinase
Receptor Substrate-1
Growth-factor
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collection: Australian Institute for Bioengineering and Nanotechnology Publications
 
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