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Munc18c phosphorylation by the insulin receptor links cell signaling directly to SNARE exocytosis

By Jenna L. Jewell, Eunjin Oh, Latha Ramalingam, Michael A. Kalwat, Vincent S. Tagliabracci, Lixuan Tackett, Jeffrey S. Elmendorf and Debbie C. Thurmond


SNARE complex assembly and mobilization of GLUT4 vesicles is coordinated through direct targeting of Munc18c by the insulin receptor tyrosine kinase

Topics: Research Articles
Publisher: The Rockefeller University Press
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Provided by: PubMed Central

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  5. (1995). Molecular identification of two novel Munc-18 isoforms expressed in non-neuronal tissues.
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  10. (1998). SNAREpins: minimal machinery for membrane fusion.
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