Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65(PAK) and the JNK/SAPK MAP kinase cascade
Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65(PAK) and the JNK/SAPK MAP kinase cascade
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DOI：
10.1016/s0092-8674(00)81371-9
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发表时间：
1996-11-01
期刊：
影响因子：
64.5
通讯作者：
Hall, A
中科院分区：
文献类型：
--
作者：
Lamarche, N;Tapon, N;Hall, A
Rac和Cdc 42调节哺乳动物细胞中的多种反应，包括板状伪足和丝状伪足的形成、JNK MAP激酶级联的激活和G1细胞周期进展的诱导。Pac也是Ras诱导的恶性转化所需的下游靶标之一。含有Y 40 C效应位点取代的Pac和Cdc 42与Ser/Thr激酶p65（PAK）不再完整，并且不能激活JNK MAP激酶途径。然而，它们仍然诱导细胞骨架变化和G1细胞周期进展。另一方面，含有F37 A效应位点取代的Rac不再与Ser/Thr激酶p160（ROCK）相互作用，并且不能诱导板状伪足或G1进展。我们的结论是，Pac和Cdc 42控制MAP激酶途径和肌动蛋白细胞骨架组织独立通过不同的下游目标。
Rac and Cdc42 regulate a variety of responses in mammalian cells including formation of lamellipodia and filopodia, activation of the JNK MAP kinase cascade, and induction of G1 cell cycle progression. Pac is also one of the downstream targets required for Ras-induced malignant transformation. Pac and Cdc42 containing a Y40C effector site substitution no longer intact with the Ser/Thr kinase p65(PAK) and are unable to activate the JNK MAP kinase pathway. However, they still induce cytoskeletal changes and G1 cell cycle progression. Rac containing an F37A effector site substitution, on the other hand, no longer interacts with the Ser/Thr kinase p160(ROCK) and is unable to induce lamellipodia or G1 progression. We conclude that Pac and Cdc42 control MAP kinase pathways and actin cytoskeleton organization independently through distinct downstream targets.