ORAI1 _ CRACM1
- Known as:
- ORAI1 _ CRACM1
- Catalog number:
- Y214049
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ORAI1 _ CRACM1
Related genes to: ORAI1 _ CRACM1
- Gene:
- ORAI1 NIH gene
- Name:
- ORAI calcium release-activated calcium modulator 1
- Previous symbol:
- TMEM142A
- Synonyms:
- FLJ14466, CRACM1
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 2006-04-10
- Date modifiied:
- 2019-04-23
Related products to: ORAI1 _ CRACM1
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- The pore-forming Orai1 protein is an essential component of store-operated calcium entry (SOCE), a process vital to diverse cellular and physiological functions. Mutations in human Orai1 cause severe immunodeficiencies and myopathies, yet structural insights have remained largely elusive. To address this, we studied the structure of detergent-solubilized human Orai1 (hOrai1) by cryo-electron microscopy. While the overall resolution is moderate, the reconstructed map confirms a conserved hexameric architecture and enables assignment of transmembrane helices. We observed profound structural heterogeneity, with particles adopting both C6- and C2-symmetric conformations, indicative of dynamic rearrangements. This study establishes a framework for future structural and mechanistic studies of hOrai1. - Source: PubMed
Publication date: 2026/05/11
Zhang YimingWang YuanLiu JindouBei WeiweiWang HongkunWang JunliChen LeiWang Youjun - Diabetes mellitus is a major metabolic disorder that significantly increases the risk of cardiovascular disease. Altered calcium (Ca) homeostasis, particularly through store-operated calcium entry (SOCE), has emerged as a critical pathway linking diabetes with cardiac dysfunction. Evidence indicates that SOCE is dysregulated in diabetes, but findings remain controversial. Some studies report reduced SOCE due to downregulation or impaired coupling of STIM1 and Orai1, leading to altered Ca homeostasis and cardiac dysfunction. Others demonstrate enhanced SOCE linked to Orai and STIM isoforms upregulation, contributing to mitochondrial dysfunction, maladaptive hypertrophy, and metabolic remodeling in diabetic cardiomyopathy. Recent work also highlighted an unexpected role of STIM1 in fatty acid metabolism, linking Ca signaling with energy substrate preference in the diabetic heart. This chapter synthesizes current evidence on the molecular mechanisms of STIM and Orai proteins in the regulation of SOCE under diabetic conditions, highlighting their roles in heart dysfunction. - Source: PubMed
Publication date: 2026/05/12
Smani TarikDominguez-Liste Beltzanede Jesús Gutiérrez-Barranco MartaAspron-Martin CarlosCordero-Sánchez CeliaCalderón-Sánchez Eva MRosado Juan AntonioHmadcha Abdelkrim - Diabetic retinopathy (DR), a major cause of blindness, is partly driven by methylglyoxal (MGO), a glycolytic byproduct with cytotoxic properties. Retinal Müller cells (MCs), which preserve retinal integrity and function, are highly susceptible to MGO-induced damage. Calcium/calmodulin-dependent serine protein kinase (CASK), a scaffold protein widely expressed in the retina, has an unidentified role in MCs and DR progression. In murine rMC1 cells, CASK was detected in both the nucleus and cytosol, with strong mitochondrial localization. Knockdown of CASK markedly reduced MGO-induced apoptosis, mitochondrial reactive oxygen species (mtROS) accumulation, mitochondrial membrane potential collapse, and impairment of oxidative phosphorylation. The cytotoxic effects were abolished by the ROS scavengers NAC and MitoTEMPO. Notably, silencing CASK also elevated basal antioxidant proteins, including SOD2, GPX4, and catalase. Furthermore, CASK depletion prevented MGO-induced increases in cytosolic and mitochondrial Ca²⁺, as well as Ca²⁺ influx through ER Ca²⁺ store depletion. Pharmacological inhibition of store-operated Ca²⁺ entry (SOCE), the mitochondrial calcium uniporter (MCU), or CASK kinase activity suppressed MGO-induced Ca overload and cell death without altering mtROS production. Mechanistically, CASK is associated with STIM1 to facilitate Orai1 clustering, thereby enhancing SOCE activity. Inhibition of p38 signaling similarly reduced Ca accumulation and apoptosis. Transcriptomic analysis revealed that CASK silencing upregulated genes involved in mitochondrial respiration and oxidative phosphorylation, particularly complexes I and V. Collectively, these findings demonstrate that CASK promotes MGO-induced apoptosis through kinase-independent disruption of mitochondrial and antioxidant defenses, and kinase-dependent activation of SOCE, identifying CASK as a potential therapeutic target in DR. - Source: PubMed
Publication date: 2026/05/08
Yeoh Chuin ShungHuang Duen-YiHuang Wan-ChenWu Liang HuanChen Chieh-YingSekar PonarulselvamChan Chi-MingLin Wan-Wan - Calcium (Ca2+) signaling is a fundamental regulator of virtually all aspects of eukaryotic cell physiology, including gene expression, secretion, metabolism, motility, and cell fate decisions. The spatial and temporal control of cytosolic Ca2+ signals relies on a coordinated interplay between intracellular Ca2+ stores and plasma membrane (PM) Ca2+ channels. A critical advance in this field over the past two decades was the molecular identification of stromal interaction molecule 1 (STIM1) as the long-sought Ca2+ sensor that couples depletion of endoplasmic reticulum Ca2+ stores to Ca2+ influx across the PM. STIM1 has been established as a core component of store-operated Ca2+ entry, acting through direct activation of ORAI Ca2+ channels. However, accumulating evidence now indicates that STIM1 functions extend beyond this canonical role. STIM1 participates in the regulation of multiple classes of ion channels, contributes to the organization of membrane contact sites, and acts as a signaling scaffold influencing cellular processes independently of classical store depletion. This review summarizes the discovery and canonical functions of STIM1 and focuses on its emerging non-canonical roles, highlighting how STIM1 has evolved from an ER Ca2+ sensor into a multifunctional signaling hub. - Source: PubMed
Sanchez-Lopez IreneOrantos-Aguilera YolandaLopez-Guerrero Aida MPozo-Guisado EulaliaMartin-Romero Francisco Javier - Intracellular calcium (Ca) signaling controls myoblast proliferation, fusion, and myofiber formation. In myoblasts, Transient Receptor Potential Canonical (TRPC) channels, with TRPC1 as a predominant isoform, mediate store-operated Ca²⁺ entry (SOCE) and are essential for myogenesis. PDLIM5 (ENH1), a PDZ-LIM scaffold protein, organizes signaling events, including ion channel regulation and transcriptional control in muscles. This study aims to test the hypothesis that PDLIM5 regulates TRPC1-mediated Ca entry in myoblasts. Thapsigargin-induced SOCE was suppressed by the SOCE inhibitors Gd and 2-APB, as well as by TRPC1 siRNA, supporting the involvement of TRPC1 in SOCE in C2C12 myoblasts. Additionally, SOCE inhibition decreased the number of nuclei per myotube and reduced the size of myotubes. ENH1 siRNA knockdown significantly downregulated TRPC1 and STIM1 mRNA expression, increased basal cytosolic Ca level, and impaired SOCE response and myotube maturation. Overexpression of ENH4, a skeletal muscle-specific short splice variant of ENH1, similarly repressed TRPC1-mediated SOCE and myotube formation. Conversely, ENH1 overexpression enhanced SOCE without altering the mRNA levels of TRPC1, Orai1, or STIM1. Immunoprecipitation showed a physical interaction between ENH1/ENH4 and TRPC1. In differentiated myotubes, TRPC1 also contributed to thapsigargin-induced SOCE, as evidenced by the reduced Ca entry following TRPC1 knockdown. ENH1 knockdown and ENH4 overexpression significantly attenuated SOCE in myotubes; notably, ENH1 knockdown also increased basal cytosolic Ca level. In contrast to myoblasts, ENH1 overexpression did not enhance SOCE in myotubes, concomitant with the absence of a detectable interaction between ENH1 and TRPC1, whereas ENH4 retained its association with TRPC1. These findings suggest that ENH1 and ENH4 differentially modulate TRPC1-dependent Ca entry in C2C12 cells, thereby regulating myogenic differentiation and contributing to skeletal muscle formation and development. - Source: PubMed
Dong MingyiNiimi TomoakiMaturana Andrés Daniel