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dc.contributor.author이영한-
dc.date.accessioned2019-09-04T01:01:19Z-
dc.date.available2019-09-04T01:01:19Z-
dc.date.issued2005-02-
dc.identifier.citationJOURNAL OF BIOLOGICAL CHEMISTRY, v. 280, No. 8, Page. 6897-6905en_US
dc.identifier.issn0021-9258-
dc.identifier.urihttp://www.jbc.org/content/280/8/6897.short-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/110159-
dc.description.abstractPhosphoinositide-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.en_US
dc.language.isoen_USen_US
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCen_US
dc.titlePleckstrin homology domains of phospholipase C-gamma1 directly interact with beta-tubulin for activation of phospholipase C-gamma1 and reciprocal modulation of beta-tubulin function in microtubule assemblyen_US
dc.typeArticleen_US
dc.identifier.doi10.1074/jbc.M406350200-
dc.relation.journalJOURNAL OF BIOLOGICAL CHEMISTRY-
dc.contributor.googleauthorChang, JS-
dc.contributor.googleauthorKim, SK-
dc.contributor.googleauthorKwon, TK-
dc.contributor.googleauthorBae, SS-
dc.contributor.googleauthorMin, DS-
dc.contributor.googleauthorLee, YH-
dc.contributor.googleauthorKim, SO-
dc.contributor.googleauthorSeo, JK-
dc.contributor.googleauthorChoi, JH-
dc.contributor.googleauthorSuh, PG-
dc.relation.code2009204730-
dc.sector.campusE-
dc.sector.daehakCOLLEGE OF SCIENCE & TECHNOLOGY[E]-
dc.sector.departmentDIVISION OF MOLECULAR & LIFE SCIENCE-
dc.identifier.pidyounghan-
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COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E](과학기술융합대학) > ETC
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