Identification and characterization of p49/STRAP as a novel GLUT4-binding protein
| Autor: | Hadi Al-Hasani, Hideko Matsumoto, Annette Schürmann, Ivonne Lisinski, Samuel W. Cushman, Dena R. Yver |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Transcriptional Activation
GLUT8 FGF21 endocrine system diseases Amino Acid Motifs Molecular Sequence Data Biophysics Adipose tissue Biology Biochemistry Cell Line Mice Calnexin Two-Hybrid System Techniques Protein Interaction Mapping Protein biosynthesis Animals Humans Insulin Amino Acid Sequence Molecular Biology Cell Nucleus Glucose Transporter Type 4 Binding protein Cell Membrane Glucose transporter nutritional and metabolic diseases Cell Biology musculoskeletal system Rats Adipose Tissue Mutation biology.protein hormones hormone substitutes and hormone antagonists GLUT4 Transcription Factors |
| Zdroj: | Biochemical and biophysical research communications. 344(4) |
| ISSN: | 0006-291X |
| Popis: | To identify novel regulatory components involved in the recycling of the insulin-responsive glucose transporter GLUT4, we have used the yeast two-hybrid system to isolate GLUT4-binding proteins from a rat adipose cell cDNA library. We found a 49-kDa protein (p49/STRAP) that specifically interacts with an acidic amino acid motif (Q7IGSEDG) in the N-terminus of GLUT4. Confocal immunofluorescence microscopy of primary rat adipose cells shows co-localization of myc-p49 with GLUT4 and also with the ER-resident protein calnexin. Insulin stimulation had no effect on GLUT4-binding and subcellular distribution of p49 in adipose cells. However, overexpression of the GLUT4-binding domain of p49 in adipose cells reduces protein synthesis and cell-surface expression of GLUT4, but not of GLUT8. Moreover, cell-surface expression of a p49-binding-deficient GLUT4 mutant (ED/QN) is also reduced. Kinetic analysis of HA-epitope-tagged GLUT4 protein synthesis indicates a possible role of p49 in biosynthesis and/or processing of GLUT4 in adipose cells. |
| Databáze: | OpenAIRE |
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