Tyrosine phosphorylation of Munc18c on residue 521 abrogates binding to Syntaxin 4 |
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| Authors: | Veronica Aran Nia J Bryant Gwyn W Gould |
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| Institution: | (1) Henry Wellcome Laboratory of Cell Biology, Davidson Building, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, G12 9QQ, UK;(2) The Physiological Laboratory, School of Biomedical Sciences, University of Liverpool, Crown Street, Liverpool, L69 3BX, UK |
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| Abstract: | Background Insulin stimulates exocytosis of GLUT4 from an intracellular store to the cell surface of fat and muscle cells. Fusion of
GLUT4-containing vesicles with the plasma membrane requires the SNARE proteins Syntaxin 4, VAMP2 and the regulatory Sec1/Munc18
protein, Munc18c. Syntaxin 4 and Munc18c form a complex that is disrupted upon insulin treatment of adipocytes. Munc18c is
tyrosine phosphorylated in response to insulin in these cells. Here, we directly test the hypothesis that tyrosine phosphorylation
of Munc18c is responsible for the observed insulin-dependent abrogation of binding between Munc18c and Syntaxin 4. |
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