Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이영한 | - |
dc.date.accessioned | 2021-01-08T01:51:05Z | - |
dc.date.available | 2021-01-08T01:51:05Z | - |
dc.date.issued | 2002-03 | - |
dc.identifier.citation | The Journal of Biological Chemistry, v. 277, no. 22, page. 19697-19702 | en_US |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://www.jbc.org/content/277/22/19697.short | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/156732 | - |
dc.description.abstract | The 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.sponsorship | This 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.iso | en_US | en_US |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | en_US |
dc.title | Interaction of elongation factor-1 alpha and plecstrin homology domain of phospholipase C-gamma1 with activating its activity | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.1074/jbc.M111206200 | - |
dc.relation.journal | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.contributor.googleauthor | Chang, Jong-Soo | - |
dc.contributor.googleauthor | Seok, Heon | - |
dc.contributor.googleauthor | Kwon, Taeg-Kyu | - |
dc.contributor.googleauthor | Min, Do Sik | - |
dc.contributor.googleauthor | Ahn, Bong-Hyun | - |
dc.contributor.googleauthor | Lee, Young Han | - |
dc.contributor.googleauthor | Suh, Ju-Won | - |
dc.contributor.googleauthor | Kim, Jong-Woo | - |
dc.contributor.googleauthor | Iwashita, Shintaro | - |
dc.contributor.googleauthor | Omor, Akira | - |
dc.contributor.googleauthor | Ichinose, Sachiyo | - |
dc.contributor.googleauthor | Numata, Osamu | - |
dc.contributor.googleauthor | Seo, Jeong-Kon | - |
dc.contributor.googleauthor | Oh, Yong-Seok | - |
dc.contributor.googleauthor | Suh, Pann-Ghill | - |
dc.relation.code | 2009204730 | - |
dc.sector.campus | E | - |
dc.sector.daehak | COLLEGE OF SCIENCE & TECHNOLOGY[E] | - |
dc.sector.department | DIVISION OF MOLECULAR & LIFE SCIENCE | - |
dc.identifier.pid | younghan | - |
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