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Trends Cell Biol. 2016 Nov;26(11):804-817. doi: 10.1016/j.tcb.2016.09.004. Epub 2016 Sep 22.

Filling the Void: Proximity-Based Labeling of Proteins in Living Cells.

Author information

1
Sanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104, USA.
2
Sanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104, USA; Department of Pediatrics, Sanford School of Medicine, University of South Dakota, Sioux Falls, SD 57105, USA. Electronic address: Kyle.Roux@sanfordhealth.org.

Abstract

There are inherent limitations with traditional methods to study protein behavior or to determine the constituency of proteins in discrete subcellular compartments. In response to these limitations, several methods have recently been developed that use proximity-dependent labeling. By fusing proteins to enzymes that generate reactive molecules, most commonly biotin, proximate proteins are covalently labeled to enable their isolation and identification. In this review we describe current methods for proximity-dependent labeling in living cells and discuss their applications and future use in the study of protein behavior.

KEYWORDS:

APEX; BioID; protein–protein interactions; proteomics; proximity-dependent labeling; subcellular proteome

PMID:
27667171
PMCID:
PMC5077660
DOI:
10.1016/j.tcb.2016.09.004
[Indexed for MEDLINE]
Free PMC Article

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