Orai1 is an essential pore subunit of the CRAC channel

By M. Prakriya, S. Feske, Y. Gwack, Sonal Srikanth, Anjana Rao, P. Hogan. Nature, 2006

1,410 citations recorded by the source corpus.

Subfields: Biochemistry, Cellular and Molecular Neuroscience, Sensory Systems

View Paper: https://www.semanticscholar.org/paper/85a5a3262078f517dcd445cad7ce3483671e0b46

How researchers see this paper

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In Cellular and Molecular Neuroscience

1. R. Lewis
2. E. Carafoli
3. Tito Calì
4. Denis Ottolini
5. M. Brini
6. M. Prakriya

In Sensory Systems

1. R. Lewis
2. M. Prakriya
3. S. Feske
4. Anjana Rao
5. P. Hogan

Citations in the corpus

• Dual functions for the endoplasmic reticulum calcium sensors STIM1 and STIM2 in T cell activation and tolerance (2008, background): “Mutational and electrophysiological analyses have identified drosophila Orai and human ORAI1 as pore subunits of the CRAC channe”
• The Epithelial Cell-derived Atopic Dermatitis Cytokine TSLP Activates Neurons to Induce Itch (2013, neutral): “ORAI1/NFAT Regulates TSLP Release in Keratinocytes ORAI1 was first identified as the channel that mediates storeoperated Ca influx required for NFAT-dependent cytokine expression during immune cell activation; loss of function mutations in ORAI1 and STIM1 lead to severe combined immunodeficiencies i”
• Neuronal calcium signaling: function and dysfunction (2014, background): “The first two channel types have been known about for a long time, but the molecular identity and the mechanism of action of the last channels were only resolved in 2006, when their pore-forming subunit ORAI was cloned [5].”
• STIM1 Clusters and Activates CRAC Channels via Direct Binding of a Cytosolic Domain to Orai1 (2009, neutral): “CAD evoked a sustained [Ca]i elevation that was dependent on extracellular Ca (Figure 2C), was suppressed by CRAC channel inhibitors like 2-APB and 10 mM La (Figures S3A and S3B), and was not observed in cells coexpressing a dominant-negative nonconductive Orai1 mutant, Orai1E106A (Prakriya et al., ”
• Molecular Basis of Calcium Signaling in Lymphocytes: STIM and ORAI (2010, background): “The ORAI1 monomer is a ~33-kDa plasma membrane protein with four transmembrane helices (Figure 5); glycosylation increases its apparent molecular weight on SDS gels (24, 89).”
• Store-Operated Calcium Channels. (2015, neutral): “Thus E190 and the acidic residues in the I–II loop do not form high-affinity Ca(2) binding sites as was originally thought (297, 396), but rather E106 in the centrally located TM1 segment solely underlies Ca(2) selectivity.”