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Different states of synaptotagmin regulate evoked versus spontaneous release

Author

Listed:
  • Hua Bai

    (University of Wisconsin
    Present address: Department of Biochemistry, University of Washington, Seattle, Washington 98195, USA)

  • Renhao Xue

    (University of Wisconsin)

  • Huan Bao

    (University of Wisconsin)

  • Leili Zhang

    (University of Wisconsin)

  • Arun Yethiraj

    (University of Wisconsin)

  • Qiang Cui

    (University of Wisconsin)

  • Edwin R. Chapman

    (University of Wisconsin)

Abstract

The tandem C2-domains of synaptotagmin 1 (syt) function as Ca2+-binding modules that trigger exocytosis; in the absence of Ca2+, syt inhibits spontaneous release. Here, we used proline linkers to constrain and alter the relative orientation of these C2-domains. Short poly-proline helices have a period of three, so large changes in the relative disposition of the C2-domains result from changing the length of the poly-proline linker by a single residue. The length of the linker was varied one residue at a time, revealing a periodicity of three for the ability of the linker mutants to interact with anionic phospholipids and drive evoked synaptic transmission; syt efficiently drove exocytosis when its tandem C2-domains pointed in the same direction. Analysis of spontaneous release revealed a reciprocal relationship between the activation and clamping activities of the linker mutants. Hence, different structural states of syt underlie the control of distinct forms of synaptic transmission.

Suggested Citation

  • Hua Bai & Renhao Xue & Huan Bao & Leili Zhang & Arun Yethiraj & Qiang Cui & Edwin R. Chapman, 2016. "Different states of synaptotagmin regulate evoked versus spontaneous release," Nature Communications, Nature, vol. 7(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10971
    DOI: 10.1038/ncomms10971
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    Cited by:

    1. Nikunj Mehta & Sayantan Mondal & Emma T. Watson & Qiang Cui & Edwin R. Chapman, 2024. "The juxtamembrane linker of synaptotagmin 1 regulates Ca2+ binding via liquid-liquid phase separation," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Kevin C. Courtney & Taraknath Mandal & Nikunj Mehta & Lanxi Wu & Yueqi Li & Debasis Das & Qiang Cui & Edwin R. Chapman, 2023. "Synaptotagmin-7 outperforms synaptotagmin-1 to promote the formation of large, stable fusion pores via robust membrane penetration," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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