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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Functional roles of glutamic acid E143 and E705 residues in the N-terminus and transmembrane domain 7 of Anoctamin 1 in calcium and noxious heat sensing

  • Choi, Jonghyun (College of Pharmacy, CHA University) ;
  • Jang, Yongwoo (Department of Psychiatry, McLean Hospital, Harvard Medical School) ;
  • Kim, Haedong (College of Pharmacy, CHA University) ;
  • Wee, Jungwon (Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University) ;
  • Cho, Sinyoung (College of Pharmacy, CHA University) ;
  • Son, Woo Sung (College of Pharmacy, CHA University) ;
  • Kim, Sung Min (Department of Physical Education, College of Performing Arts and Sport, Hanyang University) ;
  • Yang, Young Duk (College of Pharmacy, CHA University)
  • Received : 2017.10.20
  • Accepted : 2018.01.05
  • Published : 2018.05.31
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Abstract

Anoctamin 1 (ANO1) is an anion channel that is activated by changes in cytosolic $Ca^{2+}$ concentration and noxious heat. Although the critical roles of ANO1 have been elucidated in various cell types, the control of its gating mechanisms by $Ca^{2+}$ and heat remain more elusive. To investigate critical amino acid residues for modulation of $Ca^{2+}$ and heat sensing, we constructed a randomized mutant library for ANO1. Among 695 random mutants, reduced $Ca^{2+}$ sensitivity was observed in two mutants (mutant 84 and 87). Consequently, the E143A mutant showed reduced sensitivity to $Ca^{2+}$ but not to high temperatures, whereas the E705V mutant exhibited reduced sensitivity to both $Ca^{2+}$ and noxious heat. These results suggest that the glutamic acids (E) at 143 and 705 residues in ANO1 are critical for modulation of $Ca^{2+}$ and/or heat responses. Furthermore, these findings help to provide a better understanding of the $Ca^{2+}$-mediated activation and heat-sensing mechanism of ANO1.

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