Send to

Choose Destination
BMB Rep. 2018 May;51(5):236-241.

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.

Author information

College of Pharmacy, CHA University, Sungnam 13488, Korea.
Department of Psychiatry, McLean Hospital, Harvard Medical School, Belmont, MA 02478, USA.
Department of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul 08826, Korea.
Department of Physical Education, College of Performing Arts and Sport, Hanyang University, Seoul 04763; Department of Active Aging Industry, Graduate School, Hanyang University, Seoul 04763, Korea.


Anoctamin 1 (ANO1) is an anion channel that is activated by changes in cytosolic Ca2+ concentration and noxious heat. Although the critical roles of ANO1 have been elucidated in various cell types, the control of its gating mechanisms by Ca2+ and heat remain more elusive. To investigate critical amino acid residues for modulation of Ca2+ and heat sensing, we constructed a randomized mutant library for ANO1. Among 695 random mutants, reduced Ca2+ sensitivity was observed in two mutants (mutant 84 and 87). Consequently, the E143A mutant showed reduced sensitivity to Ca2+ but not to high temperatures, whereas the E705V mutant exhibited reduced sensitivity to both Ca2+ and noxious heat. These results suggest that the glutamic acids (E) at 143 and 705 residues in ANO1 are critical for modulation of Ca2+ and/or heat responses. Furthermore, these findings help to provide a better understanding of the Ca2+-mediated activation and heat-sensing mechanism of ANO1. [BMB Reports 2018; 51(5): 236-241].

[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Korean Society for Biochemistry and Molecular Biology Icon for PubMed Central
Loading ...
Support Center