Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites.
Fiche publication
Date publication
juin 2018
Journal
EMBO reports
Auteurs
Membres identifiés du Cancéropôle Est :
Dr ALPY Fabien, Pr MATHELIN Carole, Dr TOMASETTO Catherine
Tous les auteurs :
Di Mattia T, Wilhelm LP, Ikhlef S, Wendling C, Spehner D, Nominé Y, Giordano F, Mathelin C, Drin G, Tomasetto C, Alpy F
Lien Pubmed
Résumé
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 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.
Mots clés
ER–organelle contact, FFAT motif, VAP proteins, endoplasmic reticulum, membrane contact site
Référence
EMBO Rep.. 2018 Jun 1;: