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DC Field | Value | Language |
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dc.citation.endPage | 18190 | - |
dc.citation.number | 20 | - |
dc.citation.startPage | 18184 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 278 | - |
dc.contributor.author | Jang, Il Ho | - |
dc.contributor.author | Lee, Sukmook | - |
dc.contributor.author | Park, Jong Bae | - |
dc.contributor.author | Kim, Jong Hyun | - |
dc.contributor.author | Lee, Chang Sup | - |
dc.contributor.author | Hur, Eun-Mi | - |
dc.contributor.author | Kim, Il Shin | - |
dc.contributor.author | Kim, Kyong-Tai | - |
dc.contributor.author | Yagisawa, Hitoshi | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Ryu, Sung Ho | - |
dc.date.accessioned | 2023-12-22T11:12:09Z | - |
dc.date.available | 2023-12-22T11:12:09Z | - |
dc.date.created | 2015-08-17 | - |
dc.date.issued | 2003-05 | - |
dc.description.abstract | The epidermal growth factor (EGF) receptor has an important role in cellular proliferation, and the enzymatic activity of phospholipase C (PLC)-gamma1 is regarded to be critical for EGF-induced mitogenesis. In this study, we report for the first time a phospholipase complex composed of PLC-gamma1 and phospholipase D2 (PLD2). PLC-gamma1 is co-immunoprecipitated with PLD2 in COS-7 cells. The results of in vitro binding analysis and co-immunoprecipitation analysis in COS-7 cells show that the Src homology (SH) 3 domain of PLC-gamma1 binds to the proline-rich motif within the Phox homology (PX) domain of PLD2. The interaction between PLC-gamma1 and PLD2 is EGF stimulation-dependent and potentiates EGF-induced inositol 1,4,5-trisphosphate (IP3) formation and Ca2+ increase. Mutating Pro-145 and Pro-148 within the PX domain of PLD2 to leucines disrupts the interaction between PLC-gamma1 and PLD2 and fails to potentiate EGF-induced IP3 formation and Ca2+ increase. However, neither PLD2 wild type nor PLD2 mutant affects the EGF-induced tyrosine phosphorylation of PLC-gamma1. These findings suggest that, upon EGF stimulation, PLC-gamma1 directly interacts with PLD2 and this interaction is important for PLC-gamma1 activity | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.278, no.20, pp.18184 - 18190 | - |
dc.identifier.doi | 10.1074/jbc.M208438200 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.scopusid | 2-s2.0-0038381419 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/16521 | - |
dc.identifier.url | http://www.jbc.org/content/278/20/18184.long | - |
dc.identifier.wosid | 000182838300078 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.title | The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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