BioID Identification of Lamin-Associated Proteins

Methods in Enzymology
Aaron A MehusKyle J Roux

Abstract

A- and B-type lamins support the nuclear envelope, contribute to heterochromatin organization, and regulate a myriad of nuclear processes. The mechanisms by which lamins function in different cell types and the mechanisms by which lamin mutations cause over a dozen human diseases (laminopathies) remain unclear. The identification of proteins associated with lamins is likely to provide fundamental insight into these mechanisms. BioID (proximity-dependent biotin identification) is a unique and powerful method for identifying protein-protein and proximity-based interactions in living cells. BioID utilizes a mutant biotin ligase from bacteria that is fused to a protein of interest (bait). When expressed in living cells and stimulated with excess biotin, this BioID-fusion protein promiscuously biotinylates directly interacting and vicinal endogenous proteins. Following biotin-affinity capture, the biotinylated proteins can be identified using mass spectrometry. BioID thus enables screening for physiologically relevant protein associations that occur over time in living cells. BioID is applicable to insoluble proteins such as lamins that are often refractory to study by other methods and can identify weak and/or transient interaction...Continue Reading

Citations

Jan 6, 2017·Differentiation; Research in Biological Diversity·Katharina ThanischIrina Solovei
Oct 11, 2017·Cells·Ilaria PecorariOrfeo Sbaizero
Feb 26, 2016·Molecular Biology of the Cell·Dae In KimKyle J Roux
Nov 22, 2019·Experimental & Molecular Medicine·Hongming SongLin Fang
Nov 15, 2020·Cancers·Benoît BégantonJérôme Solassol
Mar 25, 2021·Life Science Alliance·Xianrong WongKaren L Reddy
Jun 5, 2021·Journal of Proteome Research·Yenni A GarciaJorge Z Torres
Dec 27, 2018·Journal of Proteome Research·Sanna Abbasi, Caroline Schild-Poulter

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