EF-hand like Region in the N-terminus of Anoctamin 1 Modulates Channel Activity by Ca2+ and Voltage
DC Field | Value | Language |
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dc.contributor.author | Tak, Min Ho | - |
dc.contributor.author | Jang, Yong woo | - |
dc.contributor.author | Son, Woo Sung | - |
dc.contributor.author | Yang, Young Duk | - |
dc.contributor.author | Oh, Uhtaek | - |
dc.date.accessioned | 2022-07-09T01:23:34Z | - |
dc.date.available | 2022-07-09T01:23:34Z | - |
dc.date.created | 2021-05-12 | - |
dc.date.issued | 2019-11 | - |
dc.identifier.issn | 1226-2560 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/146860 | - |
dc.description.abstract | Anoctamin1 (ANO1) also known as TMEM16A is a transmembrane protein that functions as a Ca2+ activated chloride channel. Recently, the structure determination of a fungal Nectria haematococca TMEM16 (nhTMEM16) scramblase by X-ray crystallography and a mouse ANO1 by cryo-electron microscopy has provided the insight in molecular architecture underlying phospholipid scrambling and Ca2+ binding. Because the Ca2+ binding motif is embedded inside channel protein according to defined structure, it is still unclear how intracellular Ca2+ moves to its deep binding pocket effectively. Here we show that EF-hand like region containing multiple acidic amino acids at the N-terminus of ANO1 is a putative site regulating the activity of ANO1 by Ca2+ and voltage. The EF-hand like region of ANO1 is highly homologous to the canonical EF hand loop in calmodulin that contains acidic residues in key Ca2+-coordinating positions in the canonical EF hand. Indeed, deletion and Ala-substituted mutation of this region resulted in a significant reduction in the response to Ca2+ and changes in its key biophysical properties evoked by voltage pulses. Furthermore, only ANO1 and ANO2, and not the other TMEM16 isoforms, contain the EF-hand like region and are activated by Ca2+. Moreover, the molecular modeling analysis supports that EF-hand like region could play a key role during Ca2+ transfer. Therefore, these findings suggest that EF-hand like region in ANO1 coordinates with Ca2+ and modulate the activation by Ca2+ and voltage. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | KOREAN SOC BRAIN & NEURAL SCIENCE, KOREAN SOC NEURODEGENERATIVE DISEASE | - |
dc.title | EF-hand like Region in the N-terminus of Anoctamin 1 Modulates Channel Activity by Ca2+ and Voltage | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Jang, Yong woo | - |
dc.identifier.doi | 10.5607/en.2019.28.6.658 | - |
dc.identifier.scopusid | 2-s2.0-85078014390 | - |
dc.identifier.wosid | 000505803500002 | - |
dc.identifier.bibliographicCitation | EXPERIMENTAL NEUROBIOLOGY, v.28, no.6, pp.658 - 669 | - |
dc.relation.isPartOf | EXPERIMENTAL NEUROBIOLOGY | - |
dc.citation.title | EXPERIMENTAL NEUROBIOLOGY | - |
dc.citation.volume | 28 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 658 | - |
dc.citation.endPage | 669 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.identifier.kciid | ART002547697 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Research & Experimental Medicine | - |
dc.relation.journalResearchArea | Neurosciences & Neurology | - |
dc.relation.journalWebOfScienceCategory | Medicine, Research & Experimental | - |
dc.relation.journalWebOfScienceCategory | Neurosciences | - |
dc.subject.keywordPlus | CHLORIDE CHANNELS | - |
dc.subject.keywordPlus | TMEM16A | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | AMBER | - |
dc.subject.keywordAuthor | Anoctamin-1 | - |
dc.subject.keywordAuthor | Chloride channels | - |
dc.subject.keywordAuthor | Calcium | - |
dc.subject.keywordAuthor | Mutagenesis | - |
dc.subject.keywordAuthor | Site-directed | - |
dc.identifier.url | https://www.en-journal.org/journal/view.html?doi=10.5607/en.2019.28.6.658 | - |
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