Last update 19 Sep 2024

MOSPD2

Last update 19 Sep 2024

Basic Info

Synonyms

MGC26706, MOSPD2, motile sperm domain containing 2

+ [1]

Introduction

Endoplasmic reticulum-anchored receptor which modulates interorganelle contacts by interacting with other organelle-bound proteins via their FFAT motif (PubMed:29858488). Might have a more important role in endoplasmic reticulum and endosomes contacts (PubMed:29858488). Promotes migration of primary monocytes and neutrophils, in response to various chemokines (PubMed:28137892).

Drugs associated with MOSPD2

CD3xMOSPD2 BiTE

Target

CD3 x MOSPD2

Mechanism

CD3 modulators [+1]

Active Org.

Vascular Biogenics Ltd.

Originator Org.

Vascular Biogenics Ltd.

Active Indication

Uterine Cervical Cancer [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

VB-611

Target

CD3 x MOSPD2

Mechanism

CD3 stimulants [+1]

Active Org.

Vascular Biogenics Ltd.

Originator Org.

Vascular Biogenics Ltd.

Active Indication

Solid tumor

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with MOSPD2

100 Translational Medicine associated with MOSPD2

0 Patents (Medical) associated with MOSPD2

Literatures (Medical) associated with MOSPD2

24 Aug 2023·mSphere

Host MOSPD2 enrichment at the parasitophorous vacuole membrane varies between Toxoplasma strains and involves complex interactions.

Article

Author: Coppens, Isabelle ; Romano, Julia ; Boothroyd, John C ; Ferrel, Abel ; Panas, Michael W

Toxoplasma gondii is an obligate, intracellular parasite. Infection of a cell produces a unique niche for the parasite named the parasitophorous vacuole (PV) initially composed of host plasma membrane invaginated during invasion. The PV and its membrane (parasitophorous vacuole membrane [PVM]) are subsequently decorated with a variety of parasite proteins allowing the parasite to optimally grow in addition to manipulate host processes. Recently, we reported a proximity-labeling screen at the PVM-host interface and identified host endoplasmic reticulum (ER)-resident motile sperm domain-containing protein 2 (MOSPD2) as being enriched at this location. Here we extend these findings in several important respects. First, we show that the extent and pattern of host MOSPD2 association with the PVM differ dramatically in cells infected with different strains of Toxoplasma. Second, in cells infected with Type I RH strain, the MOSPD2 staining is mutually exclusive with regions of the PVM that associate with mitochondria. Third, immunoprecipitation and liquid chromatography tandem mass spectrometry (LC-MS/MS) with epitope-tagged MOSPD2-expressing host cells reveal strong enrichment of several PVM-localized parasite proteins, although none appear to play an essential role in MOSPD2 association. Fourth, most MOSPD2 associating with the PVM is newly translated after infection of the cell and requires the major functional domains of MOSPD2, identified as the CRAL/TRIO domain and tail anchor, although these domains were not sufficient for PVM association. Lastly, ablation of MOSPD2 results in, at most, a modest impact on Toxoplasma growth in vitro. Collectively, these studies provide new insight into the molecular interactions involving MOSPD2 at the dynamic interface between the PVM and the host cytosol. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that lives within a membranous vacuole inside of its host cell. This vacuole is decorated by a variety of parasite proteins that allow it to defend against host attack, acquire nutrients, and interact with the host cell. Recent work identified and validated host proteins enriched at this host-pathogen interface. Here, we follow up on one candidate named MOSPD2 shown to be enriched at the vacuolar membrane and describe it as having a dynamic interaction at this location depending on a variety of factors. Some of these include the presence of host mitochondria, intrinsic domains of the host protein, and whether translation is active. Importantly, we show that MOSPD2 enrichment at the vacuole membrane differs between strains indicating active involvement of the parasite with this phenotype. Altogether, these results shed light on the mechanism and role of protein associations in the host-pathogen interaction.

06 Jun 2022·Journal of Cell BiologyQ1 · BIOLOGY

MOSPD2 is an endoplasmic reticulum–lipid droplet tether functioning in LD homeostasis

Q1 · BIOLOGY

Article

Author: Mathelin, Carole ; Schwab, Yannick ; Tomishige, Nario ; Wendling, Corinne ; Di Mattia, Thomas ; Tomasetto, Catherine ; Mizzon, Giulia ; Drin, Guillaume ; Fuggetta, Nicolas ; Grandgirard, Erwan ; Thiam, Abdou Rachid ; Reina-San-Martin, Bernardo ; Carpentier, Maxime ; Alpy, Fabien ; Dumesnil, Calvin ; Zouiouich, Mehdi ; Fromental-Ramain, Catherine ; Eichler, Julie ; Kobayashi, Toshihide ; Martinet, Arthur

Membrane contact sites between organelles are organized by protein bridges. Among the components of these contacts, the VAP family comprises ER–anchored proteins, such as MOSPD2, that function as major ER–organelle tethers. MOSPD2 distinguishes itself from the other members of the VAP family by the presence of a CRAL-TRIO domain. In this study, we show that MOSPD2 forms ER–lipid droplet (LD) contacts, thanks to its CRAL-TRIO domain. MOSPD2 ensures the attachment of the ER to LDs through a direct protein–membrane interaction. The attachment mechanism involves an amphipathic helix that has an affinity for lipid packing defects present at the surface of LDs. Remarkably, the absence of MOSPD2 markedly disturbs the assembly of lipid droplets. These data show that MOSPD2, in addition to being a general ER receptor for inter-organelle contacts, possesses an additional tethering activity and is specifically implicated in the biology of LDs via its CRAL-TRIO domain.

21 Dec 2021·mBioQ1 · BIOLOGY

Proximity-Labeling Reveals Novel Host and Parasite Proteins at the Toxoplasma Parasitophorous Vacuole Membrane

Q1 · BIOLOGY

ArticleOA

Author: Mendoza, Alma G. ; Carr, Steven A. ; Ting, Alice Y. ; Boothroyd, John C. ; Branon, Tess C. ; Jean Beltran, Pierre M. ; Cygan, Alicja M.

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MOSPD2

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