DC Field | Value | Language |
---|---|---|
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, JK | - |
dc.contributor.author | Choi, JH | - |
dc.contributor.author | Suh, PG | - |
dc.date.accessioned | 2016-04-01T02:15:02Z | - |
dc.date.available | 2016-04-01T02:15:02Z | - |
dc.date.created | 2009-02-28 | - |
dc.date.issued | 2005-02-25 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.other | 2005-OAK-0000004905 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/24752 | - |
dc.description.abstract | Phosphoinositide-specific phospholipase C-gamma1 (PLC-gamma1) 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-gamma1 PH domain-glutathione S-transferase fusion proteins, followed by matrix-assisted laser desorption ionization-time of flight-mass spectrometry, identified beta-tubulin as a binding protein of both PLC-gamma1 PH domains. Tubulin is a main component of microtubules and mitotic spindle fibers, which are composed of alpha- and beta-tubulin heterodimers in all eukaryotic cells. PLC-gamma1 and beta-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-gamma1 was substantially increased in the presence of purified tubulin in vitro, whereas the activity was not promoted by bovine serum albumin, suggesting that beta-tubulin activates PLC-gamma1. Furthermore, indirect immunofluorescent microscopy showed that PLC-gamma1 was highly concentrated in mitotic spindle fibers, suggesting that PLC-gamma1 is involved in spindle fiber formation. The effect of PLC-gamma1 in microtubule formation was assessed by overexpression and silencing PLC-gamma1 in COS-7 cells, which resulted in altered microtubule dynamics in vivo. Cells overexpressing PLC-gamma1 showed higher microtubule densities than controls, whereas PLC-gamma1 silencing with small interfering RNAs led to decreased microtubule network densities as compared with control cells. Taken together, our results suggest that PLC-gamma1 and beta-tubulin transmodulate each other, i.e. that PLC-gamma1 modulates microtubule assembly by beta-tubulin, and beta-tubulin promotes PLC-gamma1 activity. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLO | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.subject | PROTEIN-KINASE-C | - |
dc.subject | NUCLEOTIDE EXCHANGE FACTOR | - |
dc.subject | GROWTH-FACTOR RECEPTOR | - |
dc.subject | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | - |
dc.subject | POLYMERIZATION DYNAMICS | - |
dc.subject | SIGNALING MOLECULES | - |
dc.subject | ARACHIDONIC-ACID | - |
dc.subject | ALPHA-SUBUNITS | - |
dc.subject | GAMMA-SUBUNITS | - |
dc.subject | PH DOMAINS | - |
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.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1074/JBC.M4063502 | - |
dc.author.google | Chang, JS | - |
dc.author.google | Kim, SK | - |
dc.author.google | Kwon, TK | - |
dc.author.google | Bae, SS | - |
dc.author.google | Min, DS | - |
dc.author.google | Lee, YH | - |
dc.author.google | Kim, SO | - |
dc.author.google | Seo, JK | - |
dc.author.google | Choi, JH | - |
dc.author.google | Suh, PG | - |
dc.relation.volume | 280 | - |
dc.relation.issue | 8 | - |
dc.relation.startpage | 6897 | - |
dc.relation.lastpage | 6905 | - |
dc.contributor.id | 10052640 | - |
dc.relation.journal | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.280, no.8, pp.6897 - 6905 | - |
dc.identifier.wosid | 000227332700079 | - |
dc.date.tcdate | 2019-02-01 | - |
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.affiliatedAuthor | Suh, PG | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 31 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | NUCLEOTIDE EXCHANGE FACTOR | - |
dc.subject.keywordPlus | PROTEIN-KINASE-C | - |
dc.subject.keywordPlus | PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE | - |
dc.subject.keywordPlus | SIGNALING MOLECULES | - |
dc.subject.keywordPlus | GAMMA-SUBUNITS | - |
dc.subject.keywordPlus | PH DOMAIN | - |
dc.subject.keywordPlus | OVEREXPRESSION | - |
dc.subject.keywordPlus | MEMBRANE | - |
dc.subject.keywordPlus | BINDS | - |
dc.subject.keywordPlus | SEQUENCES | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
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