The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding

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Abstract

Background: Synaptotagmin 1 is the Ca2+ sensor for neuronal exocytosis. Results: The juxtamembrane linker of synaptotagmin 1 is oligomerized through a glycine zipper motif, and this interaction controls the activity of synaptotagmin 1. Conclusion: Structural modifications in the linker alter the activity of synaptotagmin 1. Significance: The oligomerization of synaptotagmin 1 may control the organization at the focal site of fusion. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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Lu, B., Kiessling, V., Tamm, L. K., & Cafiso, D. S. (2014). The juxtamembrane linker of full-length synaptotagmin 1 controls oligomerization and calcium-dependent membrane binding. Journal of Biological Chemistry, 289(32), 22161–22171. https://doi.org/10.1074/jbc.M114.569327

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