Abstract
Protein-protein interactions (PPIs) are central to the proper functioning of the most basic molecular mechanisms underlying cellular life and are often perturbed in disease states. Traditional techniques contributed to the improvement of knowledge in this field but they demonstrated significant limitations. Recently, a new method called BioID (proximity dependent biotin identification) based on proximity-dependent labeling of proteins has been developed (Ruox et al., 2012 doi.org/10.1083/jcb.201112098). The technique exploits a promiscuous biotinylating enzyme, BirA, that can be fused to the protein of interest. In this work, we applied the BioID protocol to study the PPIs of the voltage gated potassium channel Kv1.3, that displays subcellular localization to various organelles in addition to being present in the plasmamembrane. Proteins identified by BioID are candidate interactors for the channel and represent the starting point to improve our knowledge about the role this protein plays in human diseases and to possibly to identify new pathways in which Kv1.3 is involved at the cellular level.
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