Filling the Void: Proximity-Based Labeling of Proteins in Living Cells.
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.
Sanford Children's Health Research Center, Sanford Research, Sioux Falls, SD 57104, USA.
Dae In
DI
Kim
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.
Kyle J
KJ
Roux
D000818:Animals; D002470:Cell Survival; D006801:Humans; D011485:Protein Binding; D015202:Protein Engineering; D025941:Protein Interaction Mapping; D011506:Proteins / Q000378:metabolism*; D013194:Staining and Labeling / Q000379:methods*
D011506:Proteins
APEX; BioID; protein–protein interactions; proteomics; proximity-dependent labeling; subcellular proteome
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