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 sensingopen access
- Authors
- Choi, Jonghyun; Jang, Yongwoo; Kim, Haedong; Wee, Jungwon; Cho, Sinyoung; Son, Woo Sung; Kim, Sung Min; Yang, Young Duk
- Issue Date
- May-2018
- Publisher
- KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
- Keywords
- Anoctamin 1; Calcium sensitivity; Heat sensitivity; Random mutation
- Citation
- BMB REPORTS, v.51, no.5, pp.236 - 241
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- BMB REPORTS
- Volume
- 51
- Number
- 5
- Start Page
- 236
- End Page
- 241
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/150879
- DOI
- 10.5483/BMBRep.2018.51.5.199
- ISSN
- 1976-6696
- Abstract
- 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.
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Collections - 서울 예술·체육대학 > 서울 체육학과 > 1. Journal Articles
- 서울 의과대학 > 서울 약리학교실 > 1. Journal Articles
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