Abstract
ORAI1 constitutes the pore-forming subunit of the calcium release-activated calcium (CRAC) channel, a prototypical store-operated channel that is essential for the activation of cells of the immune system. Here we describe a convenient yet powerful cross-linking approach to examine the pore architecture of CRAC channels using ORAI1 proteins engineered to contain one or two cysteine residues. The generalizable cross-linking in situ approach can also be readily extended to study other integral membrane proteins expressed in various types of cells.
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Acknowledgments
We thank the financial supports from the National Institutes of Health grant (R01GM112003, R21GM126532 and R01HL134780), the Welch Foundation (BE-1913), the American Cancer Society (RSG-16-215-01 TBE), the Cancer Prevention and Research Institute of Texas (RR140053), the American Heart Association (16IRG27250155), and the John S. Dunn Foundation and by an allocation from the Texas A&M University Health Science Center Startup Fund.
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Ma, G., He, L., Jing, J., Tan, P., Huang, Y., Zhou, Y. (2018). Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel. In: Penna, A., Constantin, B. (eds) The CRAC Channel. Methods in Molecular Biology, vol 1843. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8704-7_13
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DOI: https://doi.org/10.1007/978-1-4939-8704-7_13
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