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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2003-5-12
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pubmed:abstractText |
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 (IP(3)) formation and Ca(2+) 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 IP(3) formation and Ca(2+) 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/phospholipase D2
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
pubmed-author:HurEun-MiEM,
pubmed-author:JangIl HoIH,
pubmed-author:KimIl ShinIS,
pubmed-author:KimJong HyunJH,
pubmed-author:KimKyong-TaiKT,
pubmed-author:LeeChang SupCS,
pubmed-author:LeeSukmookS,
pubmed-author:ParkJong BaeJB,
pubmed-author:RyuSung HoSH,
pubmed-author:SuhPann-GhillPG,
pubmed-author:YagisawaHitoshiH
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18184-90
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12646582-Amino Acid Motifs,
pubmed-meshheading:12646582-Animals,
pubmed-meshheading:12646582-COS Cells,
pubmed-meshheading:12646582-Calcium,
pubmed-meshheading:12646582-Cell Division,
pubmed-meshheading:12646582-Dose-Response Relationship, Drug,
pubmed-meshheading:12646582-Epidermal Growth Factor,
pubmed-meshheading:12646582-Glutathione,
pubmed-meshheading:12646582-Humans,
pubmed-meshheading:12646582-Immunoblotting,
pubmed-meshheading:12646582-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:12646582-Mutation,
pubmed-meshheading:12646582-Phospholipase C gamma,
pubmed-meshheading:12646582-Phospholipase D,
pubmed-meshheading:12646582-Phosphorylation,
pubmed-meshheading:12646582-Precipitin Tests,
pubmed-meshheading:12646582-Proline,
pubmed-meshheading:12646582-Protein Binding,
pubmed-meshheading:12646582-Protein Structure, Tertiary,
pubmed-meshheading:12646582-Rats,
pubmed-meshheading:12646582-Recombinant Fusion Proteins,
pubmed-meshheading:12646582-Signal Transduction,
pubmed-meshheading:12646582-Transfection,
pubmed-meshheading:12646582-Type C Phospholipases,
pubmed-meshheading:12646582-Tyrosine,
pubmed-meshheading:12646582-src Homology Domains
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pubmed:year |
2003
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pubmed:articleTitle |
The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling.
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pubmed:affiliation |
Department of Life Science and Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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