Ask about this productRelated genes to: ELMOD2 Blocking Peptide
- Gene:
- ELMOD2 NIH gene
- Name:
- ELMO domain containing 2
- Previous symbol:
- -
- Synonyms:
- MGC10084
- Chromosome:
- 4q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-08-20
- Date modifiied:
- 2016-02-29
Related products to: ELMOD2 Blocking Peptide
Related articles to: ELMOD2 Blocking Peptide
- Glioma is a highly heterogeneous and malignant intracranial tumor that presents challenges for clinical treatment. ELMO domain containing 2 (ELMOD2) is a GTPase-activating protein that regulates a range of cellular biological processes. However, its specific role and prognostic value in tumorigenesis are still unknown. This study aimed to assess the prognostic relevance and signaling function of ELMOD2 in gliomas. - Source: PubMed
Publication date: 2025/05/21
Li Rui-ChaoLiu ChangWang Guo-JianWang ZiLi Rong-LinLu Hao-TianXie Xiao-XunZhang Qing-MeiFeng Da-QinYun XiangLuo Bin - Chronic alcohol consumption leads to lipid accumulation, oxidative stress, cellular damage, and inflammation in the liver, collectively referred to as alcohol-associated liver disease (ALD). FAF2/UBXD8/ETEA (Fas-associated factor 2) is a ubiquitin ligase adaptor protein that plays a crucial role in the ubiquitin-mediated degradation of misfolded proteins in the endoplasmic reticulum. A recent genome-wide association study indicated an association between FAF2 and ALD; however, the exact contribution of FAF2 to ALD pathogenesis remains unclear. - Source: PubMed
Publication date: 2025/02/19
Huda NazmulKusumanchi PraveenJiang YanchaoGao HuiThoudam ThemisZeng GeSkill Nicholas JSun ZhaoliLiangpunsakul SuthatMa JingYang Zhihong - The present study investigates the potential interaction between nano‑titanium dioxide (nano-TiO) and the water accommodated fraction (WAF) of crude oil and associated chemicals on bioavailability and biotransformation responses in the European sea bass (Dicentrarchus labrax). An in vivo (48-h) waterborne exposure with nano-TiO (10 mgL), crude oil WAF (0.068 gL), alone and in combination was performed. Combined exposure significantly reduced levels of polycyclic aromatic hydrocarbons (PAH) in either seawater and fish fillets compared to WAF alone. A significant reduction in the expression of several biotransformation genes (cyp1a, gsta, erβ2, elmod2, abcb1 and abcc1) when nano-TiO was combined with WAF was observed in fish liver, compared to WAF alone. EROD and GST enzyme activities were also significantly reduced. Nano-TiO can reduce PAHs bioavailability in seawater and biological responses in European sea bass, suggesting a potential safe application of nano-TiO for the remediation of crude oil WAF in the marine environment. - Source: PubMed
Publication date: 2024/11/12
Vannuccini M LDella Torre CGrassi GZambonin CCotugno PLeaver M JCorsi I - ELMODs are a family of three mammalian paralogues that display GTPase-activating protein (GAP) activity toward a uniquely broad array of ADP-ribosylation factor (ARF) family GTPases that includes ARF-like (ARL) proteins. ELMODs are ubiquitously expressed in mammalian tissues, highly conserved across eukaryotes, and ancient in origin, being present in the last eukaryotic common ancestor. We described functions of ELMOD2 in immortalized mouse embryonic fibroblasts (MEFs) in the regulation of cell division, microtubules, ciliogenesis, and mitochondrial fusion. Here, using similar strategies with the paralogues ELMOD1 and ELMOD3, we identify novel functions and locations of these cell regulators and compare them to those of ELMOD2, allowing the determination of functional redundancy among the family members. We found strong similarities in phenotypes resulting from deletion of either or and marked differences from those arising in deletion lines. Deletion of either or results in the decreased ability of cells to form primary cilia, loss of a subset of proteins from cilia, and accumulation of some ciliary proteins at the Golgi, predicted to result from compromised traffic from the Golgi to cilia. These phenotypes are reversed upon activating mutant expression of either ARL3 or ARL16, linking their roles to ELMOD1/3 actions. - Source: PubMed
Publication date: 2021/11/24
Turn Rachel EHu YihanDewees Skylar IDevi NarraEast Michael PHardin Katherine RKhatib TalaLinnert JoshuaWolfrum UweLim Michael JCasanova James ECaspary TamaraKahn Richard A - ELMOD2 is a GTPase-activating protein with uniquely broad specificity for ARF family GTPases. We previously showed that it acts with ARL2 in mitochondrial fusion and microtubule stability and with ARF6 during cytokinesis. Mouse embryonic fibroblasts deleted for ELMOD2 also displayed changes in cilia-related processes including increased ciliation, multiciliation, ciliary morphology, ciliary signaling, centrin accumulation inside cilia, and loss of rootlets at centrosomes with loss of centrosome cohesion. Increasing ARL2 activity or overexpressing Rootletin reversed these defects, revealing close functional links between the three proteins. This was further supported by the findings that deletion of Rootletin yielded similar phenotypes, which were rescued upon increasing ARL2 activity but not ELMOD2 overexpression. Thus, we propose that ARL2, ELMOD2, and Rootletin all act in a common pathway that suppresses spurious ciliation and maintains centrosome cohesion. Screening a number of markers of steps in the ciliation pathway supports a model in which ELMOD2, Rootletin, and ARL2 act downstream of TTBK2 and upstream of CP110 to prevent spurious release of CP110 and to regulate ciliary vesicle docking. These data thus provide evidence supporting roles for ELMOD2, Rootletin, and ARL2 in the regulation of ciliary licensing. - Source: PubMed
Publication date: 2021/02/17
Turn Rachel ELinnert JoshuaGigante Eduardo DWolfrum UweCaspary TamaraKahn Richard A