The interaction domains of transient receptor potential canonical (TRPC)1/4 and TRPC1/5 heteromultimeric channels
DC Field | Value | Language |
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dc.contributor.author | Myeong, Jongyun | - |
dc.contributor.author | Ko, Juyeon | - |
dc.contributor.author | Hong, Chansik | - |
dc.contributor.author | Yang, Dongki | - |
dc.contributor.author | Lee, Kyu Pil | - |
dc.contributor.author | Jeon, Ju-hong | - |
dc.contributor.author | So, Insult | - |
dc.date.available | 2020-02-28T01:43:55Z | - |
dc.date.created | 2020-02-06 | - |
dc.date.issued | 2016-06-03 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/8166 | - |
dc.description.abstract | Transient receptor potential canonical (TRPC) family contains a non-selective cation channel, and four TRPC subunits form a functional tetrameric channel. TRPC4/5 channels form not only the homotetrameric channel but also a heterotetrameric channel with TRPC1. We investigated the interaction domain required for TRPC1/4 or TRPC1/5 heteromultimeric channels using FRET and the patch-clamp technique. TRPC1 only localized at the plasma membrane (PM) when it was coexpressed with TRPC4 or TRPC5. The TRPC1/4 or TRPC1/5 heteromultimeric showed the typical outward rectifying IN curve. When TRPC1 and TRPC4 form a heteromeric channel, the N-terminal coiled-coil domain (CCD) and C-terminal 725-745 region of TRPC1 interact with the N-terminal CCD and C-terminal 700-728 region of TRPC4. However, when TRPC1 and TRPC5 form a heteromeric channel, the N-terminal CCD and C-terminal 673-725 region of TRPC1 interact with the N-terminal CCD and C-terminal 707-735 region of TRPC5. In conclusion, the N-terminal CCD of TRPC channels is essential for the heteromultimeric structure of TRPC channels, whereas specific C-terminal regions are required for unique heteromerization between subgroups of TRPC channels. (C) 2016 Elsevier Inc. All rights reserved. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.subject | G-ALPHA(I) | - |
dc.title | The interaction domains of transient receptor potential canonical (TRPC)1/4 and TRPC1/5 heteromultimeric channels | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000377150100009 | - |
dc.identifier.doi | 10.1016/j.bbrc.2016.04.138 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.474, no.3, pp.476 - 481 | - |
dc.identifier.scopusid | 2-s2.0-84964906569 | - |
dc.citation.endPage | 481 | - |
dc.citation.startPage | 476 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 474 | - |
dc.citation.number | 3 | - |
dc.contributor.affiliatedAuthor | Yang, Dongki | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | TRPC channel | - |
dc.subject.keywordAuthor | Tetrameric structure | - |
dc.subject.keywordAuthor | Forster Resonance Energy Transfer (FRET) | - |
dc.subject.keywordPlus | G-ALPHA(I) | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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