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

Abstract:

:In homeostatic scaling at central synapses, the depth and breadth of cellular mechanisms that detect the offset from the 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 bicucculline 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 proteins that exhibited significant changes in expression. To obtain 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 in 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.

journal_name

Elife

journal_title

eLife

authors

Schanzenbächer CT,Langer JD,Schuman EM

doi

10.7554/eLife.33322

subject

Has Abstract

pub_date

2018-02-15 00:00:00

issn

2050-084X

pii

33322

journal_volume

7

pub_type

杂志文章

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