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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 272 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 265 | - |
dc.citation.title | EXPERIMENTAL AND MOLECULAR MEDICINE | - |
dc.citation.volume | 38 | - |
dc.contributor.author | Kim, Sung-Kuk | - |
dc.contributor.author | Choi, Jang Hyun | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Chang, Jong-Soo | - |
dc.date.accessioned | 2023-12-22T10:06:25Z | - |
dc.date.available | 2023-12-22T10:06:25Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2006-06 | - |
dc.description.abstract | Phosphoinositide-specific phospholipase C-γ1 (PLC-γ1) has two pleckstrin homology (PH) domains: an amino-terminal domain (PH1) and a split PH domain (PH2). Here, we show that overlay assay of bovine brain tubulin pool with glutathione-S-transferase (GST)-PLC-γ1 PH domain fusion proteins, followed by matrix-assisted laser-desorption ionization-time of flight mass spectrometry (MALDI-TOF MS), identified 68-kDa neurofilament light chain (NF-L) as a binding protein of amino-terminal PH domain of PLC-γ1. NF-L is known as a component of neuronal intermediate filaments, which are responsible for supporting the structure of myelinated axons in neuron. PLC-γ1 and NF-L colocalized in the neurite in PC12 cells upon nerve growth factor stimulation. In vitro binding assay and immunoprecipitation analysis also showed a specific interaction of both proteins in differentiated PC12 cells. The phosphatidylinositol 4, 5-bisphosphate [PI(4,5)P2] hydrolyzing activity of PLC-γ1 was slightly decreased in the presence of purified NF-L in vitro, suggesting that NF-L inhibits PLC-γ1. Our results suggest that PLC-γ1-associated NF-L sequesters the phospholipid from the PH domain of PLC-γ1. | - |
dc.identifier.bibliographicCitation | EXPERIMENTAL AND MOLECULAR MEDICINE, v.38, no.3, pp.265 - 272 | - |
dc.identifier.issn | 1226-3613 | - |
dc.identifier.scopusid | 2-s2.0-33745847751 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5667 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33745847751 | - |
dc.identifier.wosid | 000238925500010 | - |
dc.language | 영어 | - |
dc.publisher | KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY | - |
dc.title | Pleckstrin homology domain of phospholipase C-gamma 1 directly binds to 68-kDa neurofilament light chain | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | neurofilament protein L | - |
dc.subject.keywordAuthor | PC12 cells | - |
dc.subject.keywordAuthor | phospholipase C gamma | - |
dc.subject.keywordAuthor | phosphatidylinositol 4,5-diphosphate | - |
dc.subject.keywordAuthor | protein interaction mapping | - |
dc.subject.keywordPlus | AMYOTROPHIC-LATERAL-SCLEROSIS | - |
dc.subject.keywordPlus | SLOW AXONAL-TRANSPORT | - |
dc.subject.keywordPlus | PH DOMAIN | - |
dc.subject.keywordPlus | INTERMEDIATE-FILAMENTS | - |
dc.subject.keywordPlus | BETA-TUBULIN | - |
dc.subject.keywordPlus | MOUSE MODEL | - |
dc.subject.keywordPlus | DISEASE | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | C-GAMMA-1 | - |
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