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Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes.

Insulin-stimulated glucose transport and GLUT4 translocation require regulated interactions between the v-SNARE, VAMP2, and the t-SNARE, syntaxin 4. We have isolated a novel syntaxin 4-binding protein, Synip, which specifically interacts with syntaxin 4. Insulin induces a dissociation of the Synip:syntaxin 4 complex due to an apparent decrease in the binding affinity of Synip for syntaxin 4. In contrast, the carboxyterminal domain of Synip does not dissociate from syntaxin 4 in response to insulin stimulation but inhibits glucose transport and GLUT4 translocation. These data implicate Synip as an insulin-regulated syntaxin 4-binding protein directly involved in the control of glucose transport and GLUT4 vesicle translocation.

Pubmed ID: 10394363

Authors

  • Min J
  • Okada S
  • Kanzaki M
  • Elmendorf JS
  • Coker KJ
  • Ceresa BP
  • Syu LJ
  • Noda Y
  • Saltiel AR
  • Pessin JE

Journal

Molecular cell

Publication Data

June 16, 1999

Associated Grants

None

Mesh Terms

  • Adipocytes
  • Amino Acid Sequence
  • Animals
  • Binding, Competitive
  • Biological Transport
  • Carrier Proteins
  • Cell Line
  • Cloning, Molecular
  • Cricetinae
  • Genes, Dominant
  • Glucose
  • Glucose Transporter Type 4
  • Humans
  • Insulin
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • Monosaccharide Transport Proteins
  • Muscle Proteins
  • Mutation
  • Organelles
  • Protein Binding
  • Qa-SNARE Proteins
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • R-SNARE Proteins
  • RNA, Messenger
  • Vesicular Transport Proteins
  • Yeasts