Identification of Plin5 binding partners involved in lipid droplet-mitochondrial contacts

Perilipin 5 (Plin5) has been shown the induce contact between mitochondria and lipid droplets, though the mechanism by which this occurs is unknown. It has been shown that the unique C-terminal domain of Plin5 is responsible for inducing these contact sites. In this proteomics study, we identify binding partners which mediate this function by performing affinity purification-mass spectrometry using GFP-tagged Plin5 constructs where Plin5 is full length, lacking half of the c-terminal domain, or lacking the entire c-terminal domain. Of the several potential interactors, we validate Fatp4 as a direct interactor with the tether domain of Plin5.