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Time- and polariy-dependent proteomic changes associated with homeostatic scaling at central synapses

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Schanzenbächer,  Christoph T.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Langer,  Julian David
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Schuman,  Erin Margaret
Synaptic Plasticity Department, Max Planck Institute for Brain Research, Max Planck Society;

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Citation

Schanzenbächer, C. T., Langer, J. D., & Schuman, E. M. (2018). Time- and polariy-dependent proteomic changes associated with homeostatic scaling at central synapses. eLife, 15(7). doi:10.7554/eLife.33322.


Cite as: http://hdl.handle.net/21.11116/0000-0002-748D-D
Abstract
In homeostatic scaling at central synapses, the depth and breadth of cellular mechamism hat detect the offset from set-point, detect the duration of the offset and implement a cellular response are not well understood. To understand the time-dependent scaling dynamics we treated cultured rat hippocampal cells with either TTX or biccuculline for 2 hr to induce the process of up- or down-scaling, respectively. During the activity manipulation we metabolically labeled newly synthesized proteins using BONCAT. We identified 168 newly synthesized porteins that exhibited signifcant changes in expression. To obain a temporal trajectory of the response, we compared the proteins synthesized within 2 hr or 24 hr of the activity manipulation. Surprisingly, there was little overlap in the significantly regulated newly synthesized proteins identified n the early- and integrated late response datasets. There was, however, overlap in the functional categories that are modulated early and late. These data indicate that within protein function groups, different proteomic choices can be made to effect early and late homeostatic responses that detect the duration and polarity of the activity manipulation.