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Calcium Dependent Interaction of Calmodulin with the GlyT1 C-terminus

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Abstract

The cytoplasmic regions of neurotransmitter transporters play an important role in their trafficking. This process is, to a high extent, tuned by calcium and calcium binding proteins, but the exact molecular connection are still not fully understood. In this work we found that the C-terminal region of the mouse glycine transporter GlyT1b is able to specifically interact with calmodulin in the presence of calcium. We found that several GlyT1 C-terminal mutations, including those in the ER retention signal, either eliminate or increase calmodulin interaction in vitro. In tissue-culture-expressed GlyT1 at least two of these mutations altered the sensitivity of GlyT1 surface expression and glycine uptake to calmodulin antagonists. These results suggest the possible involvement of calmodulin or calmodulin-like interactions in the regulation of GlyT1C-mediated transporter trafficking.

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Acknowledgments

This work was supported by the Slovak Grant agency VEGA, Grants 2/0084/13 and 2/0086/13. We thank Dr. G. Bukovska for the access to fluorescent microscope and Dr. J. Bauer for careful reading of the manuscript.

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  1. Laboratory of Neurobiology, Institute of Molecular Biology, Slovak Academy of Sciences, Dubravska cesta 21, 845 51, Bratislava, Slovakia

    Andrea Mihalikova, Martina Baliova & Frantisek Jursky

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  1. Andrea Mihalikova
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  2. Martina Baliova
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  3. Frantisek Jursky
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Correspondence to Frantisek Jursky.

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Mihalikova, A., Baliova, M. & Jursky, F. Calcium Dependent Interaction of Calmodulin with the GlyT1 C-terminus. Neurochem Res 39, 2225–2233 (2014). https://doi.org/10.1007/s11064-014-1424-x

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  • DOI: https://doi.org/10.1007/s11064-014-1424-x

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