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Journal articles on the topic 'Orai1'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Eckstein, Miriam, Martin Vaeth, Francisco J. Aulestia, et al. "Differential regulation of Ca2+ influx by ORAI channels mediates enamel mineralization." Science Signaling 12, no. 578 (2019): eaav4663. http://dx.doi.org/10.1126/scisignal.aav4663.

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Store-operated Ca2+ entry (SOCE) channels are highly selective Ca2+ channels activated by the endoplasmic reticulum (ER) sensors STIM1 and STIM2. Their direct interaction with the pore-forming plasma membrane ORAI proteins (ORAI1, ORAI2, and ORAI3) leads to sustained Ca2+ fluxes that are critical for many cellular functions. Mutations in the human ORAI1 gene result in immunodeficiency, anhidrotic ectodermal dysplasia, and enamel defects. In our investigation of the role of ORAI proteins in enamel, we identified enamel defects in a patient with an ORAI1 null mutation. Targeted deletion of the O

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Jardin, Isaac, Alejandro Berna-Erro, Joel Nieto-Felipe та ін. "Similarities and Differences between the Orai1 Variants: Orai1α and Orai1β". International Journal of Molecular Sciences 23, № 23 (2022): 14568. http://dx.doi.org/10.3390/ijms232314568.

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Orai1, the first identified member of the Orai protein family, is ubiquitously expressed in the animal kingdom. Orai1 was initially characterized as the channel responsible for the store-operated calcium entry (SOCE), a major mechanism that allows cytosolic calcium concentration increments upon receptor-mediated IP3 generation, which results in intracellular Ca2+ store depletion. Furthermore, current evidence supports that abnormal Orai1 expression or function underlies several disorders. Orai1 is, together with STIM1, the key element of SOCE, conducting the Ca2+ release-activated Ca2+ (CRAC)

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3

Liang, Ch, and F. Wu. "Reconstitution of calcium channel protein Orai3 into liposomes for functional studies." Биохимия 88, no. 9 (2023): 1570–80. http://dx.doi.org/10.31857/s0320972523090099.

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Store-operated calcium entry (SOCE) is the main mechanism for the Ca2+ influx in non-excitable cells. The two major components of SOCE are stromal interaction molecule 1 (STIM1) in the endoplasmic reticulum and Ca2+ release-activated Ca2+ channel (CRAC) Orai on the plasma membrane. SOCE requires interaction between STIM1 and Orai. Mammals have three Orai homologs: Orai1, Orai2, and Orai3. Although Orai1 has been widely studied and proven to be essential for numerous cellular processes, Orai3 has also attracted a significant attention recently. The gating and activation mechanisms of Orai3 have

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Fresquez, Adriana M., and Carl White. "Extracellular cysteines C226 and C232 mediate hydrogen sulfide-dependent inhibition of Orai3-mediated store-operated calcium entry." American Journal of Physiology-Cell Physiology 322, no. 1 (2022): C38—C48. http://dx.doi.org/10.1152/ajpcell.00490.2019.

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The gaseous signaling molecule hydrogen sulfide (H2S) physiologically regulates store-operated Ca2+ entry (SOCE). The SOCE machinery consists of the plasma membrane-localized Orai channels (Orai1-3) and endoplasmic reticulum-localized stromal interaction molecule (STIM)1 and STIM2 proteins. H2S inhibits Orai3- but not Orai1- or Orai2-mediated SOCE. The current objective was to define the mechanism by which H2S selectively modifies Orai3. We measured SOCE and STIM1/Orai3 dynamics and interactions in HEK293 cells exogenously expressing fluorescently tagged human STIM1 and Orai3 in the presence a

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Grimes, Derayvia, Ryan Johnson, Madeline Pashos, et al. "ORAI1 and ORAI2 modulate murine neutrophil calcium signaling, cellular activation, and host defense." Proceedings of the National Academy of Sciences 117, no. 39 (2020): 24403–14. http://dx.doi.org/10.1073/pnas.2008032117.

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Calcium signals are initiated in immune cells by the process of store-operated calcium entry (SOCE), where receptor activation triggers transient calcium release from the endoplasmic reticulum, followed by opening of plasma-membrane calcium-release activated calcium (CRAC) channels. ORAI1, ORAI2, and ORAI3 are known to comprise the CRAC channel; however, the contributions of individual isoforms to neutrophil function are not well understood. Here, we show that loss of ORAI1 partially decreases calcium influx, while loss of both ORAI1 and ORAI2 completely abolishes SOCE. In other immune-cell ty

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Smyth, Jeremy T., and James W. Putney. "Regulation of store-operated calcium entry during cell division." Biochemical Society Transactions 40, no. 1 (2012): 119–23. http://dx.doi.org/10.1042/bst20110612.

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Store-operate Ca2+ channels gate Ca2+ entry into the cytoplasm in response to the depletion of Ca2+ from endoplasmic reticulum Ca2+ stores. The major molecular components of store-operated Ca2+ entry are STIM (stromal-interacting molecule) 1 (and in some instances STIM2) that serves as the endoplasmic reticulum Ca2+ sensor, and Orai (Orai1, Orai2 and Orai3) which function as pore-forming subunits of the store-operated channel. It has been known for some time that store-operated Ca2+ entry is shut down during cell division. Recent work has revealed complex mechanisms regulating the functions an

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Tiffner, Adéla, and Isabella Derler. "Isoform-Specific Properties of Orai Homologues in Activation, Downstream Signaling, Physiology and Pathophysiology." International Journal of Molecular Sciences 22, no. 15 (2021): 8020. http://dx.doi.org/10.3390/ijms22158020.

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Ca2+ ion channels are critical in a variety of physiological events, including cell growth, differentiation, gene transcription and apoptosis. One such essential entry pathway for calcium into the cell is the Ca2+ release-activated Ca2+ (CRAC) channel. It consists of the Ca2+ sensing protein, stromal interaction molecule 1 (STIM1) located in the endoplasmic reticulum (ER) and a Ca2+ ion channel Orai in the plasma membrane. The Orai channel family includes three homologues Orai1, Orai2 and Orai3. While Orai1 is the “classical” Ca2+ ion channel within the CRAC channel complex and plays a univers

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8

Zhang, Xuexin, Ping Xin, Ryan E. Yoast, et al. "Distinct pharmacological profiles of ORAI1, ORAI2, and ORAI3 channels." Cell Calcium 91 (November 2020): 102281. http://dx.doi.org/10.1016/j.ceca.2020.102281.

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9

Baryshnikov, Sergey G., Maria V. Pulina, Alessandra Zulian, Cristina I. Linde, and Vera A. Golovina. "Orai1, a critical component of store-operated Ca2+ entry, is functionally associated with Na+/Ca2+ exchanger and plasma membrane Ca2+ pump in proliferating human arterial myocytes." American Journal of Physiology-Cell Physiology 297, no. 5 (2009): C1103—C1112. http://dx.doi.org/10.1152/ajpcell.00283.2009.

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Ca2+ entry through store-operated channels (SOCs) in the plasma membrane plays an important role in regulation of vascular smooth muscle contraction, tone, and cell proliferation. The C-type transient receptor potential (TRPC) channels have been proposed as major candidates for SOCs in vascular smooth muscle. Recently, two families of transmembrane proteins, Orai [also known as Ca2+ release-activated Ca2+ channel modulator (CRACM)] and stromal interacting molecule 1 (STIM1), were shown to be essential for the activation of SOCs mainly in nonexcitable cells. Here, using small interfering RNA, w

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Liu, Xiaoling, Tianyuan Zheng, Yan Jiang, et al. "Molecular Mechanism Analysis of STIM1 Thermal Sensation." Cells 12, no. 22 (2023): 2613. http://dx.doi.org/10.3390/cells12222613.

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STIM1 has been identified as a new warm sensor, but the exact molecular mechanism remains unclear. In this study, a variety of mutants of STIM1, Orai1 and Orai3 were generated. The single–cell calcium imaging and confocal analysis were used to evaluate the thermal sensitivity of the resulting STIM mutants and the interaction between STIM1 and Orai mutants in response to temperature. Our results suggested that the CC1–SOAR of STIM1 was a direct activation domain of temperature, leading to subsequent STIM1 activation, and the transmembrane (TM) region and K domain but not EF–SAM were needed for

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11

Bisaillon, Jonathan M., Rajender K. Motiani, José C. Gonzalez-Cobos, et al. "Essential role for STIM1/Orai1-mediated calcium influx in PDGF-induced smooth muscle migration." American Journal of Physiology-Cell Physiology 298, no. 5 (2010): C993—C1005. http://dx.doi.org/10.1152/ajpcell.00325.2009.

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We recently demonstrated that thapsigargin-induced passive store depletion activates Ca2+ entry in vascular smooth muscle cells (VSMC) through stromal interaction molecule 1 (STIM1)/Orai1, independently of transient receptor potential canonical (TRPC) channels. However, under physiological stimulations, despite the ubiquitous depletion of inositol 1,4,5-trisphosphate-sensitive stores, many VSMC PLC-coupled agonists (e.g., vasopressin and endothelin) activate various store-independent Ca2+ entry channels. Platelet-derived growth factor (PDGF) is an important VSMC promigratory agonist with an es

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Sanchez-Collado, Jose, Isaac Jardin, Jose J. López, et al. "Role of Orai3 in the Pathophysiology of Cancer." International Journal of Molecular Sciences 22, no. 21 (2021): 11426. http://dx.doi.org/10.3390/ijms222111426.

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The mammalian exclusive Orai3 channel participates in the generation and/or modulation of two independent Ca2+ currents, the store-operated current, Icrac, involving functional interactions between the stromal interaction molecules (STIM), STIM1/STIM2, and Orai1/Orai2/Orai3, as well as the store-independent arachidonic acid (AA) (or leukotriene C4)-regulated current Iarc, which involves Orai1, Orai3 and STIM1. Overexpression of functional Orai3 has been described in different neoplastic cells and cancer tissue samples as compared to non-tumor cells or normal adjacent tissue. In these cells, Or

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El Assar, Mariam, Esther García-Rojo, Alejandro Sevilleja-Ortiz, et al. "Functional Role of STIM-1 and Orai1 in Human Microvascular Aging." Cells 11, no. 22 (2022): 3675. http://dx.doi.org/10.3390/cells11223675.

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The impact of aging on vascular function is heterogeneous depending on the vascular territories. Calcium regulation plays a key role in vascular function and has been implicated in aging-related hypercontractility of corpus cavernosum. We aimed to evaluate stromal interaction molecule (STIM)/Orai system involvement in aging-related vascular alterations in the human macro and microvasculature. Aortae specimens and mesenteric arteries (MA), obtained from 45 organ donors, were functionally evaluated in organ chambers and wire myographs. Subjects were divided into groups either younger or older th

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Angulo, Javier, Argentina Fernández, Alejandro Sevilleja-Ortiz, Alberto Sánchez-Ferrer, Leocadio Rodríguez-Mañas, and Mariam El Assar. "Upregulation of Orai Channels Contributes to Aging-Related Vascular Alterations in Rat Coronary Arteries." International Journal of Molecular Sciences 24, no. 17 (2023): 13402. http://dx.doi.org/10.3390/ijms241713402.

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Vascular territories display heterogeneous sensitivity to the impacts of aging. The relevance of the STIM/Orai system to vascular function depends on the vascular bed. We aimed to evaluate the contribution of the STIM/Orai system to aging-related vascular dysfunction in rat coronary circulation. Vascular function was evaluated according to myography in coronary arteries from young (three-month-old) and older (twenty-month-old) rats. The effects of aging and STIM/Orai inhibition on the contraction and relaxation of the coronary arteries and on the protein expression of STIM-1, Orai1, and Orai3

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15

Zhang, Xuexin, Wei Zhang, José C. González-Cobos, et al. "Complex role of STIM1 in the activation of store-independent Orai1/3 channels." Journal of General Physiology 143, no. 3 (2014): 345–59. http://dx.doi.org/10.1085/jgp.201311084.

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Orai proteins contribute to Ca2+ entry into cells through both store-dependent, Ca2+ release–activated Ca2+ (CRAC) channels (Orai1) and store-independent, arachidonic acid (AA)-regulated Ca2+ (ARC) and leukotriene C4 (LTC4)-regulated Ca2+ (LRC) channels (Orai1/3 heteromultimers). Although activated by fundamentally different mechanisms, CRAC channels, like ARC and LRC channels, require stromal interacting molecule 1 (STIM1). The role of endoplasmic reticulum–resident STIM1 (ER-STIM1) in CRAC channel activation is widely accepted. Although ER-STIM1 is necessary and sufficient for LRC channel ac

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Spinelli, Amy M., and Mohamed Trebak. "Orai channel-mediated Ca2+ signals in vascular and airway smooth muscle." American Journal of Physiology-Cell Physiology 310, no. 6 (2016): C402—C413. http://dx.doi.org/10.1152/ajpcell.00355.2015.

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Orai (Orai1, Orai2, and Orai3) proteins form a family of highly Ca2+-selective plasma membrane channels that are regulated by stromal-interacting molecules (STIM1 and STIM2); STIM proteins are Ca2+ sensors located in the membrane of the endoplasmic reticulum. STIM and Orai proteins are expressed in vascular and airway smooth muscle and constitute the molecular components of the ubiquitous store-operated Ca2+ entry pathway that mediate the Ca2+ release-activated Ca2+ current. STIM/Orai proteins also encode store-independent Ca2+ entry pathways in smooth muscle. Altered expression and function o

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Sánchez-Collado, José, José J. López, and Juan A. Rosado. "The Orai1-AC8 Interplay: How Breast Cancer Cells Escape from Orai1 Channel Inactivation." Cells 10, no. 6 (2021): 1308. http://dx.doi.org/10.3390/cells10061308.

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The interplay between the Ca2+-sensitive adenylyl cyclase 8 (AC8) and Orai1 channels plays an important role both in the activation of the cAMP/PKA signaling and the modulation of Orai1-dependent Ca2+ signals. AC8 interacts with a N-terminal region that is exclusive to the Orai1 long variant, Orai1α. The interaction between both proteins allows the Ca2+ that enters the cell through Orai1α to activate the generation of cAMP by AC8. Subsequent PKA activation results in Orai1α inactivation by phosphorylation at serine-34, thus shaping Orai1-mediated cellular functions. In breast cancer cells, AC8

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Kar, Pulak, Yu-Ping Lin, Rajesh Bhardwaj, et al. "The N terminus of Orai1 couples to the AKAP79 signaling complex to drive NFAT1 activation by local Ca2+ entry." Proceedings of the National Academy of Sciences 118, no. 19 (2021): e2012908118. http://dx.doi.org/10.1073/pnas.2012908118.

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To avoid conflicting and deleterious outcomes, eukaryotic cells often confine second messengers to spatially restricted subcompartments. The smallest signaling unit is the Ca2+ nanodomain, which forms when Ca2+ channels open. Ca2+ nanodomains arising from store-operated Orai1 Ca2+ channels stimulate the protein phosphatase calcineurin to activate the transcription factor nuclear factor of activated T cells (NFAT). Here, we show that NFAT1 tethered directly to the scaffolding protein AKAP79 (A-kinase anchoring protein 79) is activated by local Ca2+ entry, providing a mechanism to selectively re

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Kilch, Tatiana, Dalia Alansary, Kathrin Dörr, Christine Peinelt, and Barbara Niemeyer. "Modification of glycan chains as a mechanism to regulate SOCE (P1156)." Journal of Immunology 190, no. 1_Supplement (2013): 190.3. http://dx.doi.org/10.4049/jimmunol.190.supp.190.3.

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Abstract T cell receptor mediated activation requires the influx of calcium from the extracellular medium. Here, the endoplasmic reticulum (ER) Ca2+ sensor STIM1 reports the decrease in luminal [Ca2+] caused by IP3 receptor activity, clusters and directly binds and activates Orai1 channels, providing Ca2+ influx (store-operated, SOCE) essential for immune cell activation. We are interested in the regulation and modulation of this pathway. Because alterations of glycosylation of several T cell epitopes are implicated in immunsenescence and cancer, we investigated N-glycosylation site mutants of

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Zhou, Yandong, Robert M. Nwokonko, Xiangyu Cai, et al. "Cross-linking of Orai1 channels by STIM proteins." Proceedings of the National Academy of Sciences 115, no. 15 (2018): E3398—E3407. http://dx.doi.org/10.1073/pnas.1720810115.

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The transmembrane docking of endoplasmic reticulum (ER) Ca2+-sensing STIM proteins with plasma membrane (PM) Orai Ca2+ channels is a critical but poorly understood step in Ca2+ signal generation. STIM1 protein dimers unfold to expose a discrete STIM–Orai activating region (SOAR1) that tethers and activates Orai1 channels within discrete ER–PM junctions. We reveal that each monomer within the SOAR dimer interacts independently with single Orai1 subunits to mediate cross-linking between Orai1 channels. Superresolution imaging and mobility measured by fluorescence recovery after photobleaching re

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Arora, Samriddhi, Jyoti Tanwar, Nutan Sharma, Suman Saurav, and Rajender K. Motiani. "Orai3 Regulates Pancreatic Cancer Metastasis by Encoding a Functional Store Operated Calcium Entry Channel." Cancers 13, no. 23 (2021): 5937. http://dx.doi.org/10.3390/cancers13235937.

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Store operated Ca2+ entry (SOCE) mediated by Orai1/2/3 channels is a highly regulated and ubiquitous Ca2+ influx pathway. Although the role of Orai1 channels is well studied, the significance of Orai2/3 channels is still emerging in nature. In this study, we performed extensive bioinformatic analysis of publicly available datasets and observed that Orai3 expression is inversely associated with the mean survival time of PC patients. Orai3 expression analysis in a battery of PC cell lines corroborated its differential expression profile. We then carried out thorough Ca2+ imaging experiments in s

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Ibrahim, Dakik, Vandier, et al. "Expression Profiling of Calcium Channels and Calcium-Activated Potassium Channels in Colorectal Cancer." Cancers 11, no. 4 (2019): 561. http://dx.doi.org/10.3390/cancers11040561.

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Background: Colorectal cancer (CRC) is a highly devastating cancer. Ca2+-dependent channels are now considered key regulators of tumor progression. In this study, we aimed to investigate the association of non-voltage gated Ca2+ channels and Ca2+-dependent potassium channels (KCa) with CRC using the transcriptional profile of their genes. Methods: We selected a total of 35 genes covering KCa channels KCNN1–4, KCNMA1 and their subunits KCNMB1–4, endoplasmic reticulum (ER) calcium sensors STIM1 and STIM2, Ca2+ channels ORAI1–3 and the family of cation channels TRP (TRPC1–7, TRPA1, TRPV1/2,4–6 an

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Azimi, Iman, Michael Milevskiy, Silke Chalmers, et al. "ORAI1 and ORAI3 in Breast Cancer Molecular Subtypes and the Identification of ORAI3 as a Hypoxia Sensitive Gene and a Regulator of Hypoxia Responses." Cancers 11, no. 2 (2019): 208. http://dx.doi.org/10.3390/cancers11020208.

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The remodeling of specific calcium-permeable ion channels is a feature of some breast cancer subtypes. ORAI1 is a protein that forms a calcium-permeable ion channel responsible for store-operated calcium entry (SOCE) in a variety of cell types. ORAI3, a related isoform, is not a regulator of SOCE in most cell types. However, ORAI3 does control SOCE in many estrogen receptor-positive breast cancer cell lines, where it also controls proliferation. ORAI1 is a well-characterized regulator of the proliferation and migration of many basal breast cancer cells; however, the role of ORAI3 in these type

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Segin, Sebastian, Michael Berlin, Christin Richter, et al. "Cardiomyocyte-Specific Deletion of Orai1 Reveals Its Protective Role in Angiotensin-II-Induced Pathological Cardiac Remodeling." Cells 9, no. 5 (2020): 1092. http://dx.doi.org/10.3390/cells9051092.

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Pathological cardiac remodeling correlates with chronic neurohumoral stimulation and abnormal Ca2+ signaling in cardiomyocytes. Store-operated calcium entry (SOCE) has been described in adult and neonatal murine cardiomyocytes, and Orai1 proteins act as crucial ion-conducting constituents of this calcium entry pathway that can be engaged not only by passive Ca2+ store depletion but also by neurohumoral stimuli such as angiotensin-II. In this study, we, therefore, analyzed the consequences of Orai1 deletion for cardiomyocyte hypertrophy in neonatal and adult cardiomyocytes as well as for other

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Kappel, Sven, Tatiana Kilch, Roland Baur, Martin Lochner, and Christine Peinelt. "The Number and Position of Orai3 Units within Heteromeric Store-Operated Ca2+ Channels Alter the Pharmacology of ICRAC." International Journal of Molecular Sciences 21, no. 7 (2020): 2458. http://dx.doi.org/10.3390/ijms21072458.

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Store-operated heteromeric Orai1/Orai3 channels have been discussed in the context of aging, cancer, and immune cell differentiation. In contrast to homomeric Orai1 channels, they exhibit a different pharmacology upon application of reactive oxygen species (ROS) or 2-aminoethoxydiphenyl borate (2-APB) in various cell types. In endogenous cells, subunit composition and arrangement may vary and cannot be defined precisely. In this study, we used patch-clamp electrophysiology to investigate the 2-APB profile of store-operated and store-independent homomeric Orai1 and heteromeric Orai1/Orai3 conca

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Vashisht, Ayushi, Mohamed Trebak, and Rajender K. Motiani. "STIM and Orai proteins as novel targets for cancer therapy. A Review in the Theme: Cell and Molecular Processes in Cancer Metastasis." American Journal of Physiology-Cell Physiology 309, no. 7 (2015): C457—C469. http://dx.doi.org/10.1152/ajpcell.00064.2015.

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Calcium (Ca2+) regulates a plethora of cellular functions including hallmarks of cancer development such as cell cycle progression and cellular migration. Receptor-regulated calcium rise in nonexcitable cells occurs through store-dependent as well as store-independent Ca2+ entry pathways. Stromal interaction molecules (STIM) and Orai proteins have been identified as critical constituents of both these Ca2+ influx pathways. STIMs and Orais have emerged as targets for cancer therapeutics as their altered expression and function have been shown to contribute to tumorigenesis. Recent data demonstr

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Robitaille, Mélanie, Shao Ming Chan, Amelia A. Peters, et al. "ORAI1-Regulated Gene Expression in Breast Cancer Cells: Roles for STIM1 Binding, Calcium Influx and Transcription Factor Translocation." International Journal of Molecular Sciences 23, no. 11 (2022): 5867. http://dx.doi.org/10.3390/ijms23115867.

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A remodeling of calcium homeostasis, including calcium influx via store-operated calcium entry (SOCE), is a feature of breast cancers. SOCE is critical to maintain calcium balance in the endoplasmic reticulum calcium store and is an important mechanism for calcium signaling in a variety of cell types, including breast cancer cells. The canonical mechanism of SOCE is stromal interacting molecule 1 (STIM1)-mediated activation of ORAI. Elevated ORAI1 expression is a feature of basal breast cancer cells. However, the role of ORAI1 in the regulation of transcription in breast cancer cells of the ba

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Nguyen, Nhung T., Weidong Han, Wen‐Ming Cao, et al. "Store‐Operated Calcium Entry Mediated by ORAI and STIM." Comprehensive Physiology 8, no. 3 (2018): 981–1002. https://doi.org/10.1002/j.2040-4603.2018.tb00032.x.

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ABSTRACTThe calcium release‐activated calcium (CRAC) channel, composed of ORAI and stromal interaction molecules (STIM), represents a prototypical example of store‐operated calcium entry in mammals. The ORAI‐STIM signaling occurs at membrane contact sites formed by close appositions between the endoplasmic reticulum (ER) and the plasma membrane. ORAI1 is a four‐pass transmembrane protein that forms a highly calcium‐selective ion channel in the plasma membrane. STIM1 is an ER‐resident, a single‐pass transmembrane protein that serves as a calcium sensor within the ER lumen and a potent activator

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DeHaven, Wayne I., Jeremy T. Smyth, Rebecca R. Boyles, and James W. Putney. "Calcium Inhibition and Calcium Potentiation of Orai1, Orai2, and Orai3 Calcium Release-activated Calcium Channels." Journal of Biological Chemistry 282, no. 24 (2007): 17548–56. http://dx.doi.org/10.1074/jbc.m611374200.

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Perni, Stefano, Joseph L. Dynes, Andriy V. Yeromin, Michael D. Cahalan, and Clara Franzini-Armstrong. "Nanoscale patterning of STIM1 and Orai1 during store-operated Ca2+ entry." Proceedings of the National Academy of Sciences 112, no. 40 (2015): E5533—E5542. http://dx.doi.org/10.1073/pnas.1515606112.

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Stromal interacting molecule (STIM) and Orai proteins constitute the core machinery of store-operated calcium entry. We used transmission and freeze–fracture electron microscopy to visualize STIM1 and Orai1 at endoplasmic reticulum (ER)–plasma membrane (PM) junctions in HEK 293 cells. Compared with control cells, thin sections of STIM1-transfected cells possessed far more ER elements, which took the form of complex stackable cisternae and labyrinthine structures adjoining the PM at junctional couplings (JCs). JC formation required STIM1 expression but not store depletion, induced here by thaps

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Zhu, D., R. He, W. Yu та ін. "ORAI3 contributes to hypoxia-inducible factor 1/2α-sensitive colon cell migration". Physiology International 108, № 2 (2021): 221–37. http://dx.doi.org/10.1556/2060.2021.00137.

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AbstractBackgroundHypoxia is a pivotal initiator of tumor angiogenesis and growth through the stabilization of hypoxia-inducible factors (HIFs). This study set out to examine the involvement of HIF-1α and HIF-2α in colon cancer and ascertained whether ORAI3 was involved in the pathway.Materials and methodsPatients and murine models as well as human colorectal adenocarcinoma tumor (CW2) cells were included to examine the levels of ORAI1/3 and HIF-1/2α levels. Calcium imaging was utilized to ascertain the activity of calcium channel. Scratch assay was used to assess the migration capacity of the

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Qin, Ying, Qinggang Meng, Qunhua Wang, et al. "Pregnancy-Specific Glycoprotein 9 Enhances Store-Operated Calcium Entry and Nitric Oxide Release in Human Umbilical Vein Endothelial Cells." Diagnostics 13, no. 6 (2023): 1134. http://dx.doi.org/10.3390/diagnostics13061134.

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We explored changes in pregnancy-specific glycoprotein 9 (PSG9) levels in the serum of patients with preeclampsia and the effects and underlying mechanisms of PSG9 effects on calcium (Ca2+) homeostasis and nitric oxide (NO) release in human umbilical vein endothelial cells (HUVECs). Western blotting was used to detect protein expression levels, and an NO fluorescence probe was used to examine NO production. Intracellular Ca2+ concentrations were measured using a Ca2+-sensitive fluorescent dye under a fluorescence microscope. Compared with those in healthy pregnant women, serum PSG9 levels were

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Bokhobza, Alexandre, Nathalie Ziental-Gelus, Laurent Allart, Oksana Iamshanova, and Fabien Vanden Abeele. "Impact of SOCE Abolition by ORAI1 Knockout on the Proliferation, Adhesion, and Migration of HEK-293 Cells." Cells 10, no. 11 (2021): 3016. http://dx.doi.org/10.3390/cells10113016.

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Store-operated calcium entry (SOCE) provided through channels formed by ORAI proteins is a major regulator of several cellular processes. In immune cells, it controls fundamental processes such as proliferation, cell adhesion, and migration, while in cancer, SOCE and ORAI1 gene expression are dysregulated and lead to abnormal migration and/or cell proliferation. In the present study, we used the CRISPR/Cas9 technique to delete the ORAI1 gene and to identify its role in proliferative and migrative properties of the model cell line HEK-293. We showed that ORAI1 deletion greatly reduced SOCE. The

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Udappusamy, Vino, Nirmal Kumar Ramasamy, Nithya Thangam S, et al. "ORAI1 Gene and Calcium Deficiency in Oral Cancer: An Overview." Oriental Journal Of Chemistry 41, no. 2 (2025): 551–54. https://doi.org/10.13005/ojc/410224.

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Oral cancer, which includes malignancies of the lip, tongue, and mouth, ranks as the sixth most prevalent cancer globally, with approximately 355,000 new cases and 177,000 deaths annually. Over the past 25 years, its incidence has risen significantly among young individuals and women, while the decline in mortality rates remains minimal. Among these cases, oral squamous cell carcinomas (OSCCs) account for nearly 90%, originating primarily from squamous cells in the oral cavity and lips. Nutritional deficiencies, particularly inadequate levels of vitamins D, C, B, and A, along with protein-ener

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Sanchez-Collado, Lopez, Jardin, et al. "Adenylyl Cyclase Type 8 Overexpression Impairs Phosphorylation-Dependent Orai1 Inactivation and Promotes Migration in MDA-MB-231 Breast Cancer Cells." Cancers 11, no. 11 (2019): 1624. http://dx.doi.org/10.3390/cancers11111624.

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Orai1 plays a major role in store-operated Ca2+ entry (SOCE) in triple-negative breast cancer (TNBC) cells. This channel is inactivated via different mechanisms, including protein kinase C (PKC) and protein kinase A (PKA)-dependent phosphorylation at Ser-27 and Ser-30 or Ser-34, respectively, which shapes the Ca2+ responses to agonists. The Ca2+ calmodulin-activated adenylyl cyclase type 8 (AC8) was reported to interact directly with Orai1, thus mediating a dynamic interplay between the Ca2+- and cyclic adenosine monophosphate (cAMP)-dependent signaling pathways. Here, we show that the breast

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Schindl, R., I. Frischauf, J. Bergsmann, et al. "Plasticity in Ca2+ selectivity of Orai1/Orai3 heteromeric channel." Proceedings of the National Academy of Sciences 106, no. 46 (2009): 19623–28. http://dx.doi.org/10.1073/pnas.0907714106.

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Yeromin, Andriy V., Olga Safrina, and Michael D. Cahalan. "Ph Dependence of Orai1 and Orai3 Store-Operated Current." Biophysical Journal 106, no. 2 (2014): 315a. http://dx.doi.org/10.1016/j.bpj.2013.11.1824.

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Wu, Minnie M., Elizabeth D. Covington, and Richard S. Lewis. "Single-molecule analysis of diffusion and trapping of STIM1 and Orai1 at endoplasmic reticulum–plasma membrane junctions." Molecular Biology of the Cell 25, no. 22 (2014): 3672–85. http://dx.doi.org/10.1091/mbc.e14-06-1107.

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Following endoplasmic reticulum (ER) Ca2+ depletion, STIM1 and Orai1 complexes assemble autonomously at ER–plasma membrane (PM) junctions to trigger store-operated Ca2+ influx. One hypothesis to explain this process is a diffusion trap in which activated STIM1 diffusing in the ER becomes trapped at junctions through interactions with the PM, and STIM1 then traps Orai1 in the PM through binding of its calcium release-activated calcium activation domain. We tested this model by analyzing STIM1 and Orai1 diffusion using single-particle tracking, photoactivation of protein ensembles, and Monte Car

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Schaff, Ulrich Y., Neha Dixit, Emily Procyk, Itsukyo Yamayoshi, Tiffany Tse, and Scott I. Simon. "Orai1 regulates intracellular calcium, arrest, and shape polarization during neutrophil recruitment in shear flow." Blood 115, no. 3 (2010): 657–66. http://dx.doi.org/10.1182/blood-2009-05-224659.

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Abstract Orai1 was reported to function as a calcium channel subunit that facilitates store operated calcium entry (SOCE) in T cells and is necessary for formation of the immune synapse. We reasoned that SOCE via Orai1 might regulate PMNs activation during recruitment to inflamed endothelium. Orai1 function was assessed by real-time imaging of calcium transients as PMNs were stimulated to roll, arrest, and migrate on E-selectin and ICAM-1 in shear flow. Calcium entry was significantly reduced when Orai1 function was impaired by heterozygous knockout in a mouse model or by siRNA knockdown in HL

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Rana, Anshul, Michelle Yen, Amir Masoud Sadaghiani, et al. "Alternative splicing converts STIM2 from an activator to an inhibitor of store-operated calcium channels." Journal of Cell Biology 209, no. 5 (2015): 653–70. http://dx.doi.org/10.1083/jcb.201412060.

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Store-operated calcium entry (SOCE) regulates a wide variety of essential cellular functions. SOCE is mediated by STIM1 and STIM2, which sense depletion of ER Ca2+ stores and activate Orai channels in the plasma membrane. Although the amplitude and dynamics of SOCE are considered important determinants of Ca2+-dependent responses, the underlying modulatory mechanisms are unclear. In this paper, we identify STIM2β, a highly conserved alternatively spliced isoform of STIM2, which, in contrast to all known STIM isoforms, is a potent inhibitor of SOCE. Although STIM2β does not by itself strongly b

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Pethö, Zoltan, Ilka Neumann, Andrea Oeckinghaus, Albrecht Schwab, and Rieke Schleinhege. "Abstract 63: Orai1 regulates collagen secretion in pancreatic stellate cells and is enriched in fibrotic cancer-associated fibroblasts in PDAC." Cancer Research 85, no. 8_Supplement_1 (2025): 63. https://doi.org/10.1158/1538-7445.am2025-63.

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Introduction: Pancreatic ductal adenocarcinoma (PDAC) is characterized by a desmoplastic stroma driven by pancreatic stellate cells (PSCs) and cancer-associated fibroblasts (CAFs). The Ca2+-permeable ion channel ORAI1 is known to influence PSC proliferation and activation, but its role in collagen secretion and tumor fibrosis remains unclear. Experimental Procedures: Using the PSC cell line PS-1, we developed and validated a high-throughput fibrosis assay based on the collagen-binding peptide CNA-35-tdTomato. Collagen secretion was assessed following treatment with transforming growth factor β

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Cai, Xiangyu, Yandong Zhou, Xianming Wang, et al. "Orai1 Concatemers Reveal a Hexameric Orai1 Channel Assembly." Biophysical Journal 110, no. 3 (2016): 264a—265a. http://dx.doi.org/10.1016/j.bpj.2015.11.1444.

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Alansary, Dalia, Ivan Bogeski, and Barbara A. Niemeyer. "Facilitation of Orai3 targeting and store-operated function by Orai1." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1853, no. 7 (2015): 1541–50. http://dx.doi.org/10.1016/j.bbamcr.2015.03.007.

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Rychkov, Grigori Y., Fiona H. Zhou, Melissa K. Adams, Stuart M. Brierley, Linlin Ma, and Greg J. Barritt. "Orai1‐ and Orai2‐, but not Orai3‐mediated I _CRAC is regulated by intracellular pH." Journal of Physiology 600, no. 3 (2021): 623–43. http://dx.doi.org/10.1113/jp282502.

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Ramanagoudr-Bhojappa, Ramanagouda, Yong Miao та Monika Vig. "High affinity associations with α-SNAP enable calcium entry via Orai1 channels". PLOS ONE 16, № 10 (2021): e0258670. http://dx.doi.org/10.1371/journal.pone.0258670.

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Molecular steps that activate store-operated calcium entry (SOCE) via Orai channel supramolecular complex remain incompletely defined. We have earlier shown that α-SNAP regulates the on-site functional assembly and calcium selectivity of Orai1 channels. Here we investigate the molecular basis of its association with Orai, Stim and find that the affinity of α-SNAP for Orai and Stim is substantially higher than previously reported affinities between Stim and Orai sub-domains. α-SNAP binds the coiled-coil 3 (CC3) sub-domain of Stim1. Mutations of Tryptophan 430 in Stim1-CC3 disrupted α-SNAP assoc

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Quintana, Ariel, Vangipurapu Rajanikanth, Suzette Farber-Katz, et al. "TMEM110 regulates the maintenance and remodeling of mammalian ER–plasma membrane junctions competent for STIM–ORAI signaling." Proceedings of the National Academy of Sciences 112, no. 51 (2015): E7083—E7092. http://dx.doi.org/10.1073/pnas.1521924112.

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The stromal interaction molecule (STIM)–ORAI calcium release-activated calcium modulator (ORAI) pathway controls store-dependent calcium entry, a major mechanism of physiological calcium signaling in mammalian cells. The core elements of the pathway are the regulatory protein STIM1, located in the endoplasmic reticulum (ER) membrane, the calcium channel ORAI1 in the plasma membrane, and sites of close contact between the ER and the plasma membrane that permit the two proteins to interact. Research on calcium signaling has centered on STIM1, ORAI1, and a few proteins that directly modulate STIM

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Shen, Yihan, Nagendra Babu Thillaiappan, and Colin W. Taylor. "The store-operated Ca2+ entry complex comprises a small cluster of STIM1 associated with one Orai1 channel." Proceedings of the National Academy of Sciences 118, no. 10 (2021): e2010789118. http://dx.doi.org/10.1073/pnas.2010789118.

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Increases in cytosolic Ca2+ concentration regulate diverse cellular activities and are usually evoked by opening of Ca2+ channels in intracellular Ca2+ stores and the plasma membrane (PM). For the many signals that evoke formation of inositol 1,4,5-trisphosphate (IP3), IP3 receptors coordinate the contributions of these two Ca2+ sources by mediating Ca2+ release from the endoplasmic reticulum (ER). Loss of Ca2+ from the ER then activates store-operated Ca2+ entry (SOCE) by causing dimers of STIM1 to cluster and unfurl cytosolic domains that interact with the PM Ca2+ channel, Orai1, causing its

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Yeung, Priscilla S. W., Megumi Yamashita, Christopher E. Ing, Régis Pomès, Douglas M. Freymann, and Murali Prakriya. "Mapping the functional anatomy of Orai1 transmembrane domains for CRAC channel gating." Proceedings of the National Academy of Sciences 115, no. 22 (2018): E5193—E5202. http://dx.doi.org/10.1073/pnas.1718373115.

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Store-operated Orai1 channels are activated through a unique inside-out mechanism involving binding of the endoplasmic reticulum Ca2+ sensor STIM1 to cytoplasmic sites on Orai1. Although atomic-level details of Orai structure, including the pore and putative ligand binding domains, are resolved, how the gating signal is communicated to the pore and opens the gate is unknown. To address this issue, we used scanning mutagenesis to identify 15 residues in transmembrane domains (TMs) 1–4 whose perturbation activates Orai1 channels independently of STIM1. Cysteine accessibility analysis and molecul

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Yu, Tao, Xi Li, Qianqian Luo, et al. "S417 in the CC3 region of STIM1 is critical for STIM1-Orai1 binding and CRAC channel activation." Life Science Alliance 6, no. 4 (2023): e202201623. http://dx.doi.org/10.26508/lsa.202201623.

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Store-operated Ca2+entry (SOCE) is a universal Ca2+influx pathway that is important for the function of many cell types. SOCE is controlled by the interaction of the ER Ca2+sensor STIM1 with the plasma membrane Ca2+channel Orai1. S417 is located in the third coiled-coil (CC3) domain of the C-terminus of STIM1. We found that single-point mutation of this residue (S417G) abolished STIM1 C-terminus interactions with Orai1. Mutation of S417 also abolished CAD-Orai1 binding and Orai1 channel activation, eliminated STIM1 puncta formation, and co-localization with Orai1 and SOCE. 2-APB was found to r

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Hodeify, Rawad, Manjula Nandakumar, Maryam Own, et al. "The CCT chaperonin is a novel regulator of Ca2+ signaling through modulation of Orai1 trafficking." Science Advances 4, no. 9 (2018): eaau1935. http://dx.doi.org/10.1126/sciadv.aau1935.

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Store-operated Ca2+ entry (SOCE) encodes a range of cellular responses downstream of Ca2+ influx through the SOCE channel Orai1. Orai1 recycles at the plasma membrane (PM), with ~40% of the total Orai1 pool residing at the PM at steady state. The mechanisms regulating Orai1 recycling remain poorly understood. We map the domains in Orai1 that are required for its trafficking to and recycling at the PM. We further identify, using biochemical and proteomic approaches, the CCT [chaperonin-containing TCP-1 (T-complex protein 1)] chaperonin complex as a novel regulator of Orai1 recycling by primaril

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