A Novel Pleckstrin Homology Domain-containing Protein Enhances Insulin-stimulated Akt Phosphorylation and GLUT4 Translocation in Adipocytes

Protein kinase B/Akt protein kinases control an array of diverse functions, including cell growth, survival, proliferation, and metabolism. We report here the identification of pleckstrin homology-like domain family B member 1 (PHLDB1) as an insulin-responsive protein that enhances Akt activation. P...

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Veröffentlicht in:	The Journal of biological chemistry 2010-09, Vol.285 (36), p.27581-27589
Hauptverfasser:	Zhou, Qiong L., Jiang, Zhen Y., Mabardy, Allan S., Del Campo, Claudia M., Lambright, David G., Holik, John, Fogarty, Kevin E., Straubhaar, Juerg, Nicoloro, Sarah, Chawla, Anil, Czech, Michael P.
Format:	Artikel
Sprache:	eng
Schlagworte:	3T3-L1 Cells Adipocytes - drug effects Adipocytes - metabolism Akt PKB Animals Blood Proteins - chemistry Cancer Therapy Diabetes Enzyme Activation - drug effects Gene Expression Regulation - drug effects Gene Silencing Glucose - metabolism Glucose Transport Glucose Transporter Type 4 - metabolism Humans Insulin Insulin - pharmacology Intracellular Signaling Peptides and Proteins - chemistry Intracellular Signaling Peptides and Proteins - deficiency Intracellular Signaling Peptides and Proteins - genetics Intracellular Signaling Peptides and Proteins - metabolism Metabolism Mice PH Domain PHLDB1 Phosphatidylinositol Phosphates - metabolism Phosphoproteins - chemistry Phosphorylation - drug effects Protein Structure, Tertiary Protein Transport - drug effects Proto-Oncogene Proteins c-akt - metabolism Ribosomal Protein S6 Kinases, 70-kDa - metabolism Sequence Homology, Amino Acid Signal Transduction
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