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Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites
Author(s) -
Di Mattia Thomas,
Wilhelm Léa P,
Ikhlef Souade,
Wendling Corinne,
Spehner Danièle,
Nominé Yves,
Giordano Francesca,
Mathelin Carole,
Drin Guillaume,
Tomasetto Catherine,
Alpy Fabien
Publication year - 2018
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201745453
Subject(s) - endoplasmic reticulum , membrane contact site , golgi apparatus , microbiology and biotechnology , organelle , endosome , biology , scaffold protein , membrane protein , stim1 , tethering , chemistry , biochemistry , signal transduction , membrane , integral membrane protein , intracellular
Membrane contact sites are cellular structures that mediate interorganelle exchange and communication. The two major tether proteins of the endoplasmic reticulum (ER), VAP‐A and VAP‐B, interact with proteins from other organelles that possess a small VAP‐interacting motif, named FFAT [two phenylalanines (FF) in an acidic track (AT)]. In this study, using an unbiased proteomic approach, we identify a novel ER tether named motile sperm domain‐containing protein 2 (MOSPD2). We show that MOSPD2 possesses a Major Sperm Protein (MSP) domain which binds FFAT motifs and consequently allows membrane tethering in vitro . MOSPD2 is an ER‐anchored protein, and it interacts with several FFAT‐containing tether proteins from endosomes, mitochondria, or Golgi. Consequently, MOSPD2 and these organelle‐bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi. Thus, we characterized here MOSPD2, a novel tethering component related to VAP proteins, bridging the ER with a variety of distinct organelles.