Journal
CURRENT OPINION IN NEUROBIOLOGY
Volume 50, Issue -, Pages 17-23Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.conb.2017.10.015
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Funding
- NIH [R01-CA186568]
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Understanding signaling pathways in neuroscience requires high-resolution maps of the underlying protein networks. Proximity-dependent biotinylation with engineered enzymes, in combination with mass spectrometry-based quantitative proteomics, has emerged as a powerful method to dissect molecular interactions and the localizations of endogenous proteins. Recent applications to neuroscience have provided insights into the composition of sub-synaptic structures, including the synaptic cleft and inhibitory post-synaptic density. Here we compare the different enzymes and small-molecule probes for proximity labeling in the context of cultured neurons and tissue, review existing studies, and provide technical suggestions for the in vivo application of proximity labeling.
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