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Distinct gating mechanism of SOC channel involving STIM-Orai coupling and an intramolecular interaction of Orai in Caenorhabditis elegans.
Proc Natl Acad Sci U S A. 2018 05 15; 115(20):E4623-E4632.PN

Abstract

Store-operated calcium entry (SOCE), an important mechanism of Ca2+ signaling in a wide range of cell types, is mediated by stromal interaction molecule (STIM), which senses the depletion of endoplasmic reticulum Ca2+ stores and binds and activates Orai channels in the plasma membrane. This inside-out mechanism of Ca2+ signaling raises an interesting question about the evolution of SOCE: How did these two proteins existing in different cellular compartments evolve to interact with each other? We investigated the gating mechanism of Caenorhabditis elegans Orai channels. Our analysis revealed a mechanism of Orai gating by STIM binding to the intracellular 2-3 loop of Orai in C. elegans that is radically different from Orai gating by STIM binding to the N and C termini of Orai in mammals. In addition, we found that the conserved hydrophobic amino acids in the 2-3 loop of Orai1 are important for the oligomerization and gating of channels and are regulated via an intramolecular interaction mechanism mediated by the N and C termini of Orai1. This study identifies a previously unknown SOCE mechanism in C. elegans and suggests that, while the STIM-Orai interaction is conserved between invertebrates and mammals, the gating mechanism for Orai channels differs considerably.

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Authors+Show Affiliations

Kim KM
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Wijerathne T
Department of Physiology, College of Veterinary Medicine, Chungnam National University, 34143 Daejeon, Republic of Korea.
Hur JH
Optical Biomed Imaging Center, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Kang UJ
School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Kim IH
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Kweon YC
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Lee AR
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Jeong SJ
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Lee SK
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Lee YY
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Sim BW
National Primate Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea. Futuristic Animal Resource and Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea.
Lee JH
National Primate Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea. Futuristic Animal Resource and Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea.
Baig C
School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea.
Kim SU
National Primate Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea. Futuristic Animal Resource and Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea.
Chang KT
National Primate Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea. Futuristic Animal Resource and Research Center, Korea Research Institute of Bioscience and Biotechnology, 34141 Daejeon, Republic of Korea.
Lee KP
Department of Physiology, College of Veterinary Medicine, Chungnam National University, 34143 Daejeon, Republic of Korea.
Park CY
Department of Biological Sciences, School of Life Sciences, Ulsan National Institute of Science and Technology, 44919 Ulsan, Republic of Korea; cypark@unist.ac.kr.

MeSH

Amino Acid SequenceAnimalsCaenorhabditis elegansCalciumCalcium ChannelsCalcium SignalingCell MembraneEndoplasmic ReticulumEvolution, MolecularHEK293 CellsHumansIon Channel GatingORAI1 ProteinSequence HomologyStromal Interaction Molecule 1

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

29712850

Citation

Kim, Kyu Min, et al. "Distinct Gating Mechanism of SOC Channel Involving STIM-Orai Coupling and an Intramolecular Interaction of Orai in Caenorhabditis Elegans." Proceedings of the National Academy of Sciences of the United States of America, vol. 115, no. 20, 2018, pp. E4623-E4632.
Kim KM, Wijerathne T, Hur JH, et al. Distinct gating mechanism of SOC channel involving STIM-Orai coupling and an intramolecular interaction of Orai in Caenorhabditis elegans. Proc Natl Acad Sci USA. 2018;115(20):E4623-E4632.
Kim, K. M., Wijerathne, T., Hur, J. H., Kang, U. J., Kim, I. H., Kweon, Y. C., Lee, A. R., Jeong, S. J., Lee, S. K., Lee, Y. Y., Sim, B. W., Lee, J. H., Baig, C., Kim, S. U., Chang, K. T., Lee, K. P., & Park, C. Y. (2018). Distinct gating mechanism of SOC channel involving STIM-Orai coupling and an intramolecular interaction of Orai in Caenorhabditis elegans. Proceedings of the National Academy of Sciences of the United States of America, 115(20), E4623-E4632. https://doi.org/10.1073/pnas.1714986115
Kim KM, et al. Distinct Gating Mechanism of SOC Channel Involving STIM-Orai Coupling and an Intramolecular Interaction of Orai in Caenorhabditis Elegans. Proc Natl Acad Sci USA. 2018 05 15;115(20):E4623-E4632. PubMed PMID: 29712850.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Distinct gating mechanism of SOC channel involving STIM-Orai coupling and an intramolecular interaction of Orai in Caenorhabditis elegans. AU - Kim,Kyu Min, AU - Wijerathne,Tharaka, AU - Hur,Jin-Hoe, AU - Kang,Uk Jung, AU - Kim,Ihn Hyeong, AU - Kweon,Yeong Cheon, AU - Lee,Ah Reum, AU - Jeong,Su Ji, AU - Lee,Sang Kwon, AU - Lee,Yoon Young, AU - Sim,Bo-Woong, AU - Lee,Jong-Hee, AU - Baig,Chunggi, AU - Kim,Sun-Uk, AU - Chang,Kyu-Tae, AU - Lee,Kyu Pil, AU - Park,Chan Young, Y1 - 2018/04/30/ PY - 2018/5/2/pubmed PY - 2018/8/29/medline PY - 2018/5/2/entrez KW - Ca2+ signaling KW - Caenorhabditis elegans KW - Orai1 KW - SOCE KW - STIM1 SP - E4623 EP - E4632 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc. Natl. Acad. Sci. U.S.A. VL - 115 IS - 20 N2 - Store-operated calcium entry (SOCE), an important mechanism of Ca2+ signaling in a wide range of cell types, is mediated by stromal interaction molecule (STIM), which senses the depletion of endoplasmic reticulum Ca2+ stores and binds and activates Orai channels in the plasma membrane. This inside-out mechanism of Ca2+ signaling raises an interesting question about the evolution of SOCE: How did these two proteins existing in different cellular compartments evolve to interact with each other? We investigated the gating mechanism of Caenorhabditis elegans Orai channels. Our analysis revealed a mechanism of Orai gating by STIM binding to the intracellular 2-3 loop of Orai in C. elegans that is radically different from Orai gating by STIM binding to the N and C termini of Orai in mammals. In addition, we found that the conserved hydrophobic amino acids in the 2-3 loop of Orai1 are important for the oligomerization and gating of channels and are regulated via an intramolecular interaction mechanism mediated by the N and C termini of Orai1. This study identifies a previously unknown SOCE mechanism in C. elegans and suggests that, while the STIM-Orai interaction is conserved between invertebrates and mammals, the gating mechanism for Orai channels differs considerably. SN - 1091-6490 UR - https://www.unboundmedicine.com/medline/citation/29712850/Distinct_gating_mechanism_of_SOC_channel_involving_STIM_Orai_coupling_and_an_intramolecular_interaction_of_Orai_in_Caenorhabditis_elegans_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=29712850 DB - PRIME DP - Unbound Medicine ER -