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Sequence requirements of the FFAT‐like motif for specific binding to VAP‐A are revealed by NMR
Author(s) -
Furuita Kyoko,
Hiraoka Marina,
Hanada Kentaro,
Fujiwara Toshimichi,
Kojima Chojiro
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14166
Subject(s) - endoplasmic reticulum , biology , sequence motif , rna , transmembrane protein , transmembrane domain , peptide sequence , biochemistry , microbiology and biotechnology , chemistry , gene , receptor
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.