KMID : 0624620100430030199
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BMB Reports 2010 Volume.43 No. 3 p.199 ~ p.204
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Novel p104 protein regulates cell proliferation through PI3K inhibition and p27Kip1 expression
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Han Seung-Jin
Lee Jung-Hyun Choi Ki-Young Hong Seung-Hwan
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Abstract
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The protein p104 was first isolated as a binding partner of the Src homology domain of phospholipase C¥ã1, and has been shown to associate with p85¥á, Grb2. The ectopic expression of p104 reduced cellular growth rate, which was also achieved with the overexpression of only the proline-rich region of p104. The proline-rich region of p104 has been found to inhibit the colony formation of platelet-derived growth factor BB-stimulated NIH3T3 cells and MCF7 cancer cells on soft agar. Mutagenesis analysis showed that the second and third proline-rich regions are essential for growth control, as well as for interaction with p85¥á. Overexpression of p104 increased the level of the cyclin-dependent kinase inhibitor, p27Kip1, and inhibited the activity of phosphoinositide 3-kinase (PI3K). In summary, p104 interacts with p85¥á and is involved in the regulation of p27Kip1 expression for the reduction of cellular proliferation.
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KEYWORD
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Binding protein, PI3K, p104, p27Kip1, SH3 domain
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