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Curr Opin Neurobiol. 2018 Jun;50:17-23. doi: 10.1016/j.conb.2017.10.015. Epub 2017 Nov 8.

Proximity labeling: spatially resolved proteomic mapping for neurobiology.

Author information

1
Department of Chemistry, Stanford University, Stanford, CA 94305, USA.
2
Department of Biology, Stanford University, Stanford, CA 94305, USA.
3
Department of Chemistry, Stanford University, Stanford, CA 94305, USA; Department of Biology, Stanford University, Stanford, CA 94305, USA; Department of Genetics, Stanford University, Stanford, CA 94305, USA. Electronic address: ayting@stanford.edu.

Abstract

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.

PMID:
29125959
DOI:
10.1016/j.conb.2017.10.015

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