BetaPix-a enhances the activity of phospholipase Cgamma1 by binding SH3 domain in breast cancer

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Bae, Ji-Yeon; Ahn, Soo-Jung; Lee, Jeong Eon; Kim, Jung-Eun; Han, Mi-Ryung; Han, Wonshik; Kim, Seok Won; Shin, Hyuk Jai; Lee, Seung Joon; Park, Dongeun; Noh, Dong-Young
Issue Date
John Wiley & Sons
J Cell Biochem. 2005 Apr 1;94(5):1010-6
AnimalsBlotting, WesternBreast Neoplasms/*enzymology/pathologyCell Cycle Proteins/*physiologyFemaleGuanine Nucleotide Exchange Factors/*physiologyHumansHydrolysisImmunohistochemistryMiceNIH 3T3 CellsPhospholipase C gammaProtein BindingType C Phospholipases/*metabolismsrc Homology Domains
Phospholipase C-gamma1 (PLCgamma1) plays a critical role in cell growth and proliferation by generating the second messengers, diacylglycerol and 1, 4, 5-inositol triphosphate. To investigate the roles of Src homology domain 2 and domain 3 of PLCgamma1 in PLCgamma1-mediated cell signaling, we characterized some proteins binding to these domains in the MCF7 and MDA-MB-231 breast cancer cell lines. Of the several proteins that bind to glutathione-S-transferase-SH2/SH2/SH3, we identified an 85 kDa protein that binds to the SH3 domain of PLCgamma1 as the guanine nucleotide exchange factor, p21-activated protein kinase-interacting exchange factor-a (betaPix-a). BetaPix-a co-immunoprecipitated with PLCgamma1 in breast cancer tissues extracts and in MCF7 and MDA-MB-231 cell extracts. In addition, PDGF-stimulated PLCgamma1 activity was elevated in betaPix-a-overexpressing NIH3T3 cells. Our results suggest that betaPix-a binds to the Src homology domain 3 of PLCgamma1 and promotes tumor growth in breast cancer by enhancing the activity PLCgamma1.
0730-2312 (Print)
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