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Journal Articles EMBO Reports Year : 2018

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

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Abstract

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.
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Origin : Publication funded by an institution

Dates and versions

hal-02177612 , version 1 (04-11-2021)

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Thomas Di Mattia, Léa P. Wilhelm, Souade Ikhlef, Corinne Wendling, Danièle Spehner, et al.. Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites. EMBO Reports, 2018, 19 (7), ⟨10.15252/embr.201745453⟩. ⟨hal-02177612⟩
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