Physiological functions of the TRPM4 channels via protein interactions
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, Chang-Hoon | - |
dc.contributor.author | Lee, Young-Sun | - |
dc.contributor.author | Kim, Eunju | - |
dc.contributor.author | Hwang, Eun Mi | - |
dc.contributor.author | Park, Jae-Yong | - |
dc.date.accessioned | 2021-09-04T19:49:31Z | - |
dc.date.available | 2021-09-04T19:49:31Z | - |
dc.date.created | 2021-06-15 | - |
dc.date.issued | 2015-01-31 | - |
dc.identifier.issn | 1976-6696 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/94602 | - |
dc.description.abstract | Transient Receptor Potential, Melastatin-related, member 4 (TRPM4) channels are Ca2+-activated Ca2+-impermeable cation channels. These channels are expressed in various types of mammalian tissues including the brain and are implicated in many diverse physiological and pathophysiological conditions. In the past several years, the trafficking processes and regulatory mechanism of these channels and their interacting proteins have been uncovered. Here in this minireview, we summarize the current understanding of the trafficking mechanism of TRPM4 channels on the plasma membrane as well as heteromeric complex formation via protein interactions. We also describe physiological implications of protein-TRPM4 interactions and suggest TRPM4 channels as therapeutic targets in many related diseases. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY | - |
dc.subject | GATED ION CHANNELS | - |
dc.subject | NEUROTRANSMITTER RECEPTORS | - |
dc.subject | GLYCOSYLATION | - |
dc.subject | TRAFFICKING | - |
dc.subject | MELASTATIN | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | MODULATION | - |
dc.subject | EXPRESSION | - |
dc.subject | NEURONS | - |
dc.subject | CELLS | - |
dc.title | Physiological functions of the TRPM4 channels via protein interactions | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Park, Jae-Yong | - |
dc.identifier.doi | 10.5483/BMBRep.2015.48.1.252 | - |
dc.identifier.scopusid | 2-s2.0-84922324783 | - |
dc.identifier.wosid | 000351719600001 | - |
dc.identifier.bibliographicCitation | BMB REPORTS, v.48, no.1, pp.1 - 5 | - |
dc.relation.isPartOf | BMB REPORTS | - |
dc.citation.title | BMB REPORTS | - |
dc.citation.volume | 48 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 1 | - |
dc.citation.endPage | 5 | - |
dc.type.rims | ART | - |
dc.type.docType | Review | - |
dc.identifier.kciid | ART001958434 | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | GATED ION CHANNELS | - |
dc.subject.keywordPlus | NEUROTRANSMITTER RECEPTORS | - |
dc.subject.keywordPlus | GLYCOSYLATION | - |
dc.subject.keywordPlus | TRAFFICKING | - |
dc.subject.keywordPlus | MELASTATIN | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | MODULATION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | NEURONS | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordAuthor | Glycosylation | - |
dc.subject.keywordAuthor | Heteromerization | - |
dc.subject.keywordAuthor | Phosphorylation | - |
dc.subject.keywordAuthor | SUMOylation | - |
dc.subject.keywordAuthor | Trafficking | - |
dc.subject.keywordAuthor | TRPM4 | - |
dc.subject.keywordAuthor | 14-3-gamma | - |
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