Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Kim, Kwon Woo | - |
dc.contributor.author | Hwang, Junmo | - |
dc.contributor.author | Kim, Dong-Hyun | - |
dc.contributor.author | Park, Hyungju | - |
dc.contributor.author | Im, Hyun Ho | - |
dc.date.accessioned | 2023-07-12T12:10:20Z | - |
dc.date.available | 2023-07-12T12:10:20Z | - |
dc.date.created | 2023-04-04 | - |
dc.date.issued | 2023-02 | - |
dc.identifier.issn | 1976-6696 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11750/46132 | - |
dc.description.abstract | BEST family is a class of Ca2+-activated Cl-channels evolutionary well conserved from bacteria to human. The human BEST paralogs (BEST1-BEST4) share significant amino acid sequence homology in the N-terminal region, which forms the transmembrane helicases and contains the direct calcium-binding site, Ca2+-clasp. But the cytosolic C-terminal region is less conserved in the paralogs. Interestingly, this domain-specific sequence conservation is also found in the BEST1 orthologs. However, the functional role of the C-terminal region in the BEST channels is still poorly understood. Thus, we aimed to understand the functional role of the C-terminal region in the human and mouse BEST1 channels by using electrophysiological recordings. We found that the calcium-dependent activation of BEST1 channels can be modulated by the C-terminal region. The C-terminal deletion hBEST1 reduced the Ca2+- dependent current activation and the hBEST1-mBEST1 chimera showed a significantly reduced calcium sensitivity to hBEST1 in the HEK293 cells. And the C-terminal domain could regulate cellular expression and plasma membrane targeting of BEST1 channels. Our results can provide a basis for understanding the C-terminal roles in the structure-function of BEST family proteins. [BMB Reports 2023; 56(3): 172-177] © 2023 by the The Korean Society for Biochemistry and Molecular Biology | - |
dc.language | English | - |
dc.publisher | 생화학분자생물학회 | - |
dc.title | Cytosolic domain regulates the calcium sensitivity and surface expression of BEST1 channels in the HEK293 cells | - |
dc.type | Article | - |
dc.identifier.doi | 10.5483/BMBRep.2022-0170 | - |
dc.identifier.scopusid | 2-s2.0-85150953806 | - |
dc.identifier.bibliographicCitation | BMB Reports, v.56, no.3, pp.172 - 177 | - |
dc.identifier.kciid | ART002943802 | - |
dc.description.isOpenAccess | TRUE | - |
dc.subject.keywordAuthor | Bestrophin | - |
dc.subject.keywordAuthor | Ca2+-dependent activation | - |
dc.subject.keywordAuthor | Functional modulation | - |
dc.subject.keywordAuthor | Surface expression | - |
dc.subject.keywordAuthor | Whole-cell recording | - |
dc.subject.keywordPlus | BESTROPHIN CL-CHANNELS | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | ASTROCYTES | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.citation.endPage | 177 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 172 | - |
dc.citation.title | BMB Reports | - |
dc.citation.volume | 56 | - |
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