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DC Field | Value | Language |
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dc.citation.endPage | 6905 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 6897 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 280 | - |
dc.contributor.author | Chang, JS | - |
dc.contributor.author | Kim, SK | - |
dc.contributor.author | Kwon, TK | - |
dc.contributor.author | Bae, SS | - |
dc.contributor.author | Min, DS | - |
dc.contributor.author | Lee, YH | - |
dc.contributor.author | Kim, SO | - |
dc.contributor.author | Seo, Jeong Kon | - |
dc.contributor.author | Choi, Jang Hyun | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.date.accessioned | 2023-12-22T10:38:44Z | - |
dc.date.available | 2023-12-22T10:38:44Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2005-02 | - |
dc.description.abstract | Phosphoinositide-specific phospholipase C-γ1 (PLC-γ1) has two pleckstrin homology (PH) domains, an N-terminal domain and a split PH domain. Here we show that pull down of NIH3T3 cell extracts with PLC-γ1 PH domain-glutathione S-transferase fusion proteins, followed by matrix-assisted laser desorption ionization-time of flight-mass spectrometry, identified β-tubulin as a binding protein of both PLC-γ1 PH domains. Tubulin is a main component of microtubules and mitotic spindle fibers, which are composed of α- and β-tubulin heterodimers in all eukaryotic cells. PLC-γ1 and β-tubulin colocalized in the perinuclear region in COS-7 cells and cotranslocated to the plasma membrane upon agonist stimulation. Membrane-targeted translocation of depolymerized tubulin by agonist stimulation was also supported by immunoprecipitation analyses. The phosphatidylinositol 4,5-bisphosphate (PIP2) hydrolyzing activity of PLC-γ1 was substantially increased in the presence of purified tubulin in vitro, whereas the activity was not promoted by bovine serum albumin, suggesting that β-tubulin activates PLC-γ1. Furthermore, indirect immunofluorescent microscopy showed that PLC-γ1 was highly concentrated in mitotic spindle fibers, suggesting that PLC-γ1 is involved in spindle fiber formation. The effect of PLC-γ1 in microtubule formation was assessed by overexpression and silencing PLC-γ1 in COS-7 cells, which resulted in altered microtubule dynamics in vivo. Cells overexpressing PLC-γ1 showed higher microtubule densities than controls, whereas PLC-γ1 silencing with small interfering RNAs led to decreased microtubule network densities as compared with control cells. Taken together, our results suggest that PLC-γ1 and β-tubulin transmodulate each other, i.e. that PLC-γ1 modulates microtubule assembly by β-tubulin, and β-tubulin promotes PLC-γ1 activity. | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.280, no.8, pp.6897 - 6905 | - |
dc.identifier.doi | 10.1074/jbc.M406350200 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.scopusid | 2-s2.0-20044388738 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5672 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=20044388738 | - |
dc.identifier.wosid | 000227332700079 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | Pleckstrin homology domains of phospholipase C-gamma 1 directly interact with beta-tubulin for activation of phospholipase C-gamma 1 and reciprocal modulation of beta-tubulin function in microtubule assembly | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | PROTEIN-KINASE-C | - |
dc.subject.keywordPlus | NUCLEOTIDE EXCHANGE FACTOR | - |
dc.subject.keywordPlus | GROWTH-FACTOR RECEPTOR | - |
dc.subject.keywordPlus | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | - |
dc.subject.keywordPlus | POLYMERIZATION DYNAMICS | - |
dc.subject.keywordPlus | SIGNALING MOLECULES | - |
dc.subject.keywordPlus | ARACHIDONIC-ACID | - |
dc.subject.keywordPlus | ALPHA-SUBUNITS | - |
dc.subject.keywordPlus | GAMMA-SUBUNITS | - |
dc.subject.keywordPlus | PH DOMAINS | - |
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