Sequence requirements of the FFAT‐like motif for specific binding to VAP‐A are revealed by NMR

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 se...

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Bibliographic Details
Published in:FEBS letters 2021-09, Vol.595 (17), p.2248-2256
Main Authors: Furuita, Kyoko, Hiraoka, Marina, Hanada, Kentaro, Fujiwara, Toshimichi, Kojima, Chojiro
Format: Article
Language:English
Subjects:
FFAT motif
FFAT‐like motif
protein–protein interaction
SARS‐CoV‐2
solution NMR
VAMP‐associated protein
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Summary: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‐AMSP) 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‐AMSP as well as other FFAT‐like motifs. Our results will contribute to the discovery of new VAP interactors.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.14166