
pmid: 8607835
We have identified VAMP isoforms, VAMP-2 and cellubrevin, on GLUT4-containing vesicle membranes isolated from 3T3-Ll adipocytes. These proteins translocate from a low density microsomal fraction to the plasma membrane upon insulin stimulation in a fashion similar to GLUT4. VAMP-1 was not detected in this low density microsomal fraction nor on purified GLUT4-containing vesicles. In streptolysin-O permeabilized 3T3-L1 adipocytes, both VAMP-2 and cellubrevin were cleaved with botulinum neurotoxin isoform B, BoNTx/B. In addition, BoNTx/B partially inhibited insulin-stimulated GLUT4 translocation and glucose transport activity. We conclude that the synaptobrevin isoforms are important components of the insulin-dependent translocation of GLUT4 to the cell surface in adipocytes.
1303 Biochemistry, Monosaccharide Transport Proteins, Molecular Sequence Data, Biophysics, Muscle Proteins, Nerve Tissue Proteins, Deoxyglucose, Biochemistry, Antibodies, 1307 Cell Biology, R-SNARE Proteins, Mice, Microsomes, 1312 Molecular Biology, Adipocytes, Animals, Insulin, Amino Acid Sequence, Molecular Biology, Glucose Transporter Type 4, Cell Membrane, Membrane Proteins, Biological Transport, Cell Biology, 3T3 Cells, Peptide Fragments, Glucose, 1304 Biophysics
1303 Biochemistry, Monosaccharide Transport Proteins, Molecular Sequence Data, Biophysics, Muscle Proteins, Nerve Tissue Proteins, Deoxyglucose, Biochemistry, Antibodies, 1307 Cell Biology, R-SNARE Proteins, Mice, Microsomes, 1312 Molecular Biology, Adipocytes, Animals, Insulin, Amino Acid Sequence, Molecular Biology, Glucose Transporter Type 4, Cell Membrane, Membrane Proteins, Biological Transport, Cell Biology, 3T3 Cells, Peptide Fragments, Glucose, 1304 Biophysics
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