Calmodulin and Munc13 form a Ca2+ sensor/effector complex that controls short-term synaptic plasticity

Harald J. Junge; Jeong Seop Rhee; Olaf Jahn; Frederique Varoqueaux; Joachim Spiess; M. Neal Waxham; Christian Rosenmund; Nils Brose

doi:10.1016/j.cell.2004.06.029

Calmodulin and Munc13 form a Ca²⁺ sensor/effector complex that controls short-term synaptic plasticity

Harald J. Junge, Jeong Seop Rhee, Olaf Jahn, Frederique Varoqueaux, Joachim Spiess, M. Neal Waxham, Christian Rosenmund, Nils Brose

Research output: Contribution to journal › Article › peer-review

212 Scopus citations

Abstract

The efficacy of synaptic transmission between neurons can be altered transiently during neuronal network activity. This phenomenon of short-term plasticity is a key determinant of network properties; is involved in many physiological processes such as motor control, sound localization, or sensory adaptation; and is critically dependent on cytosolic [Ca²⁺]. However, the underlying molecular mechanisms and the identity of the Ca²⁺ sensor/effector complexes involved are unclear. We now identify a conserved calmodulin binding site in UNC-13/Munc13s, which are essential regulators of synaptic vesicle priming and synaptic efficacy. Ca²⁺ sensor/effector complexes consisting of calmodulin and Munc13s regulate synaptic vesicle priming and synaptic efficacy in response to a residual [Ca²⁺] signal and thus shape short-term plasticity characteristics during periods of sustained synaptic activity.

Original language	English (US)
Pages (from-to)	389-401
Number of pages	13
Journal	Cell
Volume	118
Issue number	3
DOIs	https://doi.org/10.1016/j.cell.2004.06.029
State	Published - Aug 6 2004
Externally published	Yes

Bibliographical note

Funding Information:
We thank S. Handt, I. Herfort, I. Thanhäuser, L. van Werven, and T. Liepold for excellent technical assistance. We are grateful to R. Schneggenburger and J. Putkey for valuable discussions. This work was supported by the German Research Foundation (SFB406/A1 to N.B.) and by the Max-Planck-Society.

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title = "Calmodulin and Munc13 form a Ca2+ sensor/effector complex that controls short-term synaptic plasticity",

abstract = "The efficacy of synaptic transmission between neurons can be altered transiently during neuronal network activity. This phenomenon of short-term plasticity is a key determinant of network properties; is involved in many physiological processes such as motor control, sound localization, or sensory adaptation; and is critically dependent on cytosolic [Ca2+]. However, the underlying molecular mechanisms and the identity of the Ca2+ sensor/effector complexes involved are unclear. We now identify a conserved calmodulin binding site in UNC-13/Munc13s, which are essential regulators of synaptic vesicle priming and synaptic efficacy. Ca2+ sensor/effector complexes consisting of calmodulin and Munc13s regulate synaptic vesicle priming and synaptic efficacy in response to a residual [Ca2+] signal and thus shape short-term plasticity characteristics during periods of sustained synaptic activity.",

author = "Junge, {Harald J.} and Rhee, {Jeong Seop} and Olaf Jahn and Frederique Varoqueaux and Joachim Spiess and Waxham, {M. Neal} and Christian Rosenmund and Nils Brose",

note = "Funding Information: We thank S. Handt, I. Herfort, I. Thanh{\"a}user, L. van Werven, and T. Liepold for excellent technical assistance. We are grateful to R. Schneggenburger and J. Putkey for valuable discussions. This work was supported by the German Research Foundation (SFB406/A1 to N.B.) and by the Max-Planck-Society.",

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AU - Junge, Harald J.

AU - Rhee, Jeong Seop

AU - Jahn, Olaf

AU - Varoqueaux, Frederique

AU - Spiess, Joachim

AU - Waxham, M. Neal

AU - Rosenmund, Christian

AU - Brose, Nils

N1 - Funding Information: We thank S. Handt, I. Herfort, I. Thanhäuser, L. van Werven, and T. Liepold for excellent technical assistance. We are grateful to R. Schneggenburger and J. Putkey for valuable discussions. This work was supported by the German Research Foundation (SFB406/A1 to N.B.) and by the Max-Planck-Society.

PY - 2004/8/6

Y1 - 2004/8/6

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