Abstract
The chemical synapse displays specialized intercellular adhesion between pre- and potsynaptic plasma membranes mediated by synaptic cell adhesion proteins. In this asymmetric cell adhesion, pre- and postsynapses have their own unique functions; the presynaptic terminal releases neurotransmitter, which diffuses through the synaptic cleft and is received by receptors accumulated at the postsynapse. Such distinct modes of actions of pre- and postsynapses in synaptic neurotransmission are the rate-limiting factors in signal processing in the brain, and thus protein-protein interactions within the pre- and postsynaptic scaffold are of particular importance for brain function by regulating the pre- and postsynaptic function. In the present paper, we outline a method to screen for binding partners of synaptic scaffold proteins biochemically.
Correspondence may be addressed to either author.
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Acknowledgments
We thank J. Day for discussion and advice on the manuscript. Expression vectors for GST-PSD-95 and GST-SAP97 are kind gifts from O. Schlüter. We thank M. Uecker, D. Hesse, B. Hesse-Niessen, K.-P. Hellmann, I. Thanhäuser, D. Schwerdtfeger, C. Harenberg, and F. Benseler for excellent technical assistance. This work was supported by the Max Planck Society and by grants from the German Research Foundation (SPP1365/KA3423/1-1 and KA3423/3-1; to H.K.), and the Fritz Thyssen Foundation (to H.K.).
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Altas, B., Jahn, O., Kawabe, H. (2017). Biochemical Purification of Binding Partners of Synaptic Scaffold Proteins. In: Poulopoulos, A. (eds) Synapse Development. Methods in Molecular Biology, vol 1538. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6688-2_6
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DOI: https://doi.org/10.1007/978-1-4939-6688-2_6
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