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Oncogenic K-ras segregates at spatially distinct plasma membrane signaling platforms according to its phosphorylation status.

J Cell Sci.. 2013-10;  126(Pt 20):4553-9
BarcelÓ C, Paco N, Beckett AJ, Alvarez-Moya B, Garrido E, Gelabert M, Tebar F, Jaumot M, Prior I, Agell N. Departament de Biologia Cellular, Immunologia i NeurociÈncies, Institut d'Investigacions BiomÈdiques August Pi i Sunyer (IDIBAPS), Facultat de Medicina. Universitat de Barcelona, C/ Casanova 143, 08036 Barcelona, Spain.
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摘要

Activating mutations in the K-Ras small GTPase are extensively found in human tumors. Although these mutations induce the generation of a constitutively GTP-loaded, active form of K-Ras, phosphorylation at Ser181 within the C-terminal hypervariable region can modulate oncogenic K-Ras function without affecting the in vitro affinity for its effector Raf-1. In striking contrast, K-Ras phosphorylated at Ser181 shows increased interaction in cells with the active form of Raf-1 and with p110α, the catalytic subunit of PI 3-kinase. Because the majority of phosphorylated K-Ras is located at the plasma membrane, different localization within this membrane according to the phosphorylation status was explored. Dens... More

关键词

K-Ras; Nanoclusters; PI 3-kinase; PI3K; PKC; Phosphorylation; Raf