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Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites.

EMBO Rep. 2018 Jul;19(7). Epub 2018 Jun 01
Thomas Di Mattia 1 , Léa P Wilhelm 1 , Souade Ikhlef 2 , Corinne Wendling 1 , Danièle Spehner 1 , Yves Nominé 1 , Francesca Giordano 3 , Carole Mathelin 4 , Guillaume Drin 2 , Catherine Tomasetto 1 , Fabien Alpy 1
Thomas Di Mattia 1 , Léa P Wilhelm 1 , Souade Ikhlef 2 , Corinne Wendling 1 , Danièle Spehner 1 , Yves Nominé 1 , Francesca Giordano 3 , Carole Mathelin 4 , Guillaume Drin 2 , Catherine Tomasetto 1 , Fabien Alpy 1
+ et al

[No authors listed]

Author information
  • 1 Université de Strasbourg, Illkirch, France.
  • 2 CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Université Côte d'Azur, Valbonne, France.
  • 3 Institut de Biologie Intégrative de la Cellule, CEA, CNRS, Paris-Sud University Paris-Saclay University, Gif-sur-Yvette Cedex 91198, France.
  • 4 Senology Unit, Strasbourg University Hospital (CHRU), Hôpital de Hautepierre, Strasbourg, France.

摘要


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.

KEYWORDS: ER–organelle contact, FFAT motif, VAP proteins, endoplasmic reticulum, membrane contact site