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

FEBS Letters

article

Kyoko Furuita¹  Marina Hiraoka²  Kentaro Hanada³  Toshimichi Fujiwara¹  Chojiro Kojima¹ 

[1] Institute for Protein Research, Osaka University;Graduate School of Engineering Science, Yokohama National University;Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases

关键词: FFAT motif;    FFAT-like motif;    protein–protein interaction;    SARS-CoV-2;    solution NMR;    VAMP-associated protein;   

DOI  :  10.1002/1873-3468.14166

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown