Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 장용우 | - |
dc.date.accessioned | 2019-12-08T05:40:56Z | - |
dc.date.available | 2019-12-08T05:40:56Z | - |
dc.date.issued | 2018-05 | - |
dc.identifier.citation | BMB REPORTS, v. 51, no. 5, page. 236-241 | en_US |
dc.identifier.issn | 1976-6696 | - |
dc.identifier.issn | 1976-670X | - |
dc.identifier.uri | http://www.bmbreports.org/journal/view.html?doi=10.5483/BMBRep.2018.51.5.199 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/118845 | - |
dc.description.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. | en_US |
dc.description.sponsorship | This research was supported by a grant from the National Research Foundation (NRF) of Korea (NRF-2015R1C1A1A02037682, Y Yang). Also, this work was partly supported by the GRRC program of Gyeonggi province (GRRC-CHA2017-A02, Validity and Safety Evaluation of Regional Specialized Resources). | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY | en_US |
dc.subject | Anoctamin 1 | en_US |
dc.subject | Calcium sensitivity | en_US |
dc.subject | Heat sensitivity | en_US |
dc.subject | Random mutation | en_US |
dc.title | 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 | en_US |
dc.type | Article | en_US |
dc.relation.no | 5 | - |
dc.relation.volume | 51 | - |
dc.identifier.doi | 10.5483/BMBRep.2018.51.5.199 | - |
dc.relation.page | 236-241 | - |
dc.relation.journal | BMB REPORTS | - |
dc.contributor.googleauthor | Choi, Jonghyun | - |
dc.contributor.googleauthor | Jang, Yongwoo | - |
dc.contributor.googleauthor | Kim, Haedong | - |
dc.contributor.googleauthor | Wee, Jungwon | - |
dc.contributor.googleauthor | Cho, Sinyoung | - |
dc.contributor.googleauthor | Son, Woo Sung | - |
dc.contributor.googleauthor | Kim, Sung Min | - |
dc.contributor.googleauthor | Yang, Young Duk | - |
dc.relation.code | 2018010537 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF ENGINEERING[S] | - |
dc.sector.department | DIVISION OF ELECTRICAL AND BIOMEDICAL ENGINEERING | - |
dc.identifier.pid | ywjang | - |
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