Sequence requirements of the FFAT‐like motif for specific binding to VAP‐A are revealed by NMR
Kyoko Furuita, Marina Hiraoka, Kentaro Hanada, Toshimichi Fujiwara, Chojiro Kojima
Abstract
The endoplasmic reticulum transmembrane protein vesicle‐associated membrane protein‐associated protein (VAP) plays a central role in the formation and function of membrane contact sites (MCS) through its interactions with proteins. The major sperm protein (MSP) domain of VAP binds to a variety of sequences which are referred to as FFAT‐like motifs. In this study, we investigated the interactions of eight peptides containing FFAT‐like motifs with the VAP‐A MSP domain (VAP‐A MSP ) by solution NMR. Six of eight peptides are specifically bound to VAP‐A. Furthermore, we found that the RNA‐dependent RNA polymerase of severe acute respiratory syndrome coronavirus 2 has an FFAT‐like motif which specifically binds to VAP‐A MSP as well as other FFAT‐like motifs. Our results will contribute to the discovery of new VAP interactors.