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dc.contributor.author이영한-
dc.date.accessioned2021-01-08T01:51:05Z-
dc.date.available2021-01-08T01:51:05Z-
dc.date.issued2002-03-
dc.identifier.citationThe Journal of Biological Chemistry, v. 277, no. 22, page. 19697-19702en_US
dc.identifier.issn0021-9258-
dc.identifier.urihttps://www.jbc.org/content/277/22/19697.short-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/156732-
dc.description.abstractThe pleckstrin homology (PH) domain is a small motif for membrane targeting in the signaling molecules. Phospholipase C (PLC)-γ1 has two putative PH domains, an NH2-terminal and a split PH domain. Here we report studies on the interaction of the PH domain of PLC-γ1 with translational elongation factor (EF)-1α, which has been shown to be a phosphatidylinositol 4-kinase activator. By pull-down of cell extract with the glutathione S-transferase (GST) fusion proteins with various domains of PLC-γ1 followed by peptide sequence analysis, we identified EF-1α as a binding partner of a split PH domain of PLC-γ1. Analysis by site-directed mutagenesis of the PH domain revealed that the β2-sheet of a split PH domain is critical for the interaction with EF-1α. Moreover, Dot-blot assay shows that a split PH domain specifically binds to phosphoinositides including phosphatidylinositol 4-phosphate and phosphatidylinositol 4, 5-bisphosphate (PIP2). So the PH domain of PLC-γ1 binds to both EF-1α and PIP2. The binding affinity of EF-1α to the GST·PH domain fusion protein increased in the presence of PIP2, although PIP2 does not bind to EF-1α directly. This suggests that EF-1α may control the binding affinity between the PH domain and PIP2. PLC-γ1 is substantially activated in the presence of EF-1α with a bell-shaped curve in relation to the molar ratio between them, whereas a double point mutant PLC-γ1 (Y509A/F510A) that lost its binding affinity to EF-1α shows basal level activity. Taken together, our data show that EF-1α plays a direct role in phosphoinositide metabolism of cellular signaling by regulating PLC-γ1 activity via a split PH domain.en_US
dc.description.sponsorshipThis work was supported by Grant 2000-015-DP0317 from the Korea Research Foundation (to J.-S. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.en_US
dc.language.isoen_USen_US
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCen_US
dc.titleInteraction of elongation factor-1 alpha and plecstrin homology domain of phospholipase C-gamma1 with activating its activityen_US
dc.typeArticleen_US
dc.identifier.doi10.1074/jbc.M111206200-
dc.relation.journalJOURNAL OF BIOLOGICAL CHEMISTRY-
dc.contributor.googleauthorChang, Jong-Soo-
dc.contributor.googleauthorSeok, Heon-
dc.contributor.googleauthorKwon, Taeg-Kyu-
dc.contributor.googleauthorMin, Do Sik-
dc.contributor.googleauthorAhn, Bong-Hyun-
dc.contributor.googleauthorLee, Young Han-
dc.contributor.googleauthorSuh, Ju-Won-
dc.contributor.googleauthorKim, Jong-Woo-
dc.contributor.googleauthorIwashita, Shintaro-
dc.contributor.googleauthorOmor, Akira-
dc.contributor.googleauthorIchinose, Sachiyo-
dc.contributor.googleauthorNumata, Osamu-
dc.contributor.googleauthorSeo, Jeong-Kon-
dc.contributor.googleauthorOh, Yong-Seok-
dc.contributor.googleauthorSuh, Pann-Ghill-
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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