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Bimolecular Fluorescence Complementation (BiFC) Analysis: Advances and Recent
Applications for Genome-Wide Interaction Studies
#MMPMID25772494
Miller KE
; Kim Y
; Huh WK
; Park HO
J Mol Biol
2015[Jun]; 427
(11
): 2039-2055
PMID25772494
show ga
Complex protein networks are involved in nearly all cellular processes. To
uncover these vast networks of protein interactions, various high-throughput
screening technologies have been developed. Over the last decade, bimolecular
fluorescence complementation (BiFC) assay has been widely used to detect
protein-protein interactions (PPIs) in living cells. This technique is based on
the reconstitution of a fluorescent protein in vivo. Easy quantification of the
BiFC signals allows effective cell-based high-throughput screenings for protein
binding partners and drugs that modulate PPIs. Recently, with the development of
large screening libraries, BiFC has been effectively applied for genome-wide PPI
studies and has uncovered novel protein interactions, providing new insight into
protein functions. In this review, we describe the development of reagents and
methods used for BiFC-based screens in yeast, plants, and mammalian cells. We
also discuss the advantages and drawbacks of these methods and highlight the
application of BiFC in large-scale studies.