更新于：2024-09-19

MOSPD2

更新于：2024-09-19

基本信息

别名

MGC26706、MOSPD2、motile sperm domain containing 2

+ [1]

简介

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).

关联

项与 MOSPD2 相关的药物

CD3xMOSPD2 BiTE

靶点

CD3 x MOSPD2

作用机制

CD3调节剂 [+1]

在研机构

Vascular Biogenics Ltd.

原研机构

Vascular Biogenics Ltd.

在研适应症

宫颈癌 [+1]

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

VB-611

靶点

CD3 x MOSPD2

作用机制

CD3刺激剂 [+1]

在研机构

Vascular Biogenics Ltd.

原研机构

Vascular Biogenics Ltd.

在研适应症

实体瘤

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

100 项与 MOSPD2 相关的临床结果

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100 项与 MOSPD2 相关的转化医学

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0 项与 MOSPD2 相关的专利（医药）

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项与 MOSPD2 相关的文献（医药）

2023-08-24·mSphere

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

Article

作者: 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.

2022-06-06·Journal of Cell Biology1区 · 生物学

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

1区 · 生物学

Article

作者: 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.

2021-12-21·mBio1区 · 生物学

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

1区 · 生物学

ArticleOA

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