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Cooperative activation of PI3K by Ras and Rho family small GTPases.

Abstract：

:Phosphoinositide 3-kinases (PI3Ks) and Ras and Rho family small GTPases are key regulators of cell polarization, motility, and chemotaxis. They influence each other's activities by direct and indirect feedback processes that are only partially understood. Here, we show that 21 small GTPase homologs activate PI3K. Using a microscopy-based binding assay, we show that K-Ras, H-Ras, and five homologous Ras family small GTPases function upstream of PI3K by directly binding the PI3K catalytic subunit, p110. In contrast, several Rho family small GTPases activated PI3K by an indirect cooperative positive feedback that required a combination of Rac, CDC42, and RhoG small GTPase activities. Thus, a distributed network of Ras and Rho family small GTPases induces and reinforces PI3K activity, explaining past challenges to elucidate the specific relevance of different small GTPases in regulating PI3K and controlling cell polarization and chemotaxis.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Yang HW,Shin MG,Lee S,Kim JR,Park WS,Cho KH,Meyer T,Heo WD

doi

10.1016/j.molcel.2012.05.007

subject

Has Abstract

pub_date

2012-07-27 00:00:00

pages

281-90

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(12)00390-5

journal_volume

47

pub_type

杂志文章

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