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首页> 外文期刊>Molecular and Cellular Biology >The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia.
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The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia.

机译：GTPase激活蛋白n-chimaerin与Rac1和Cdc42Hs协同作用，诱导了lamellipodia和丝状伪足的形成。

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n-Chimaerin is a GTPase-activating protein (GAP) mainly for Rac1 and less so for Cdc42Hs in vitro. The GAP activity of n-chimaerin is regulated by phospholipids and phorbol esters. Microinjection of Rac1 and Cdc42Hs into mammalian cells induces formation of the actin-based structures lamellipodia and filopodia, respectively, with the former being prevented by coinjection of the chimaerin GAP domain. Strikingly, microinjection of the full-length n-chimaerin into fibroblasts and neuroblastoma cells induces the simultaneous formation of lamellipodia and filopodia. These structures undergo cycles of dissolution and formation, resembling natural morphological events occurring at the leading edge of fibroblasts and neuronal growth cones. The effects of n-chimaerin on formation of lamellipodia and filopodia were inhibited by dominant negative Rac1(T17N) and Cdc42Hs(T17N), respectively. n-Chimaerin's effects were also inhibited by coinjection with Rho GDP dissociation inhibitor or by treatment with phorbol ester. A mutant n-chimaerin with no GAP activity and impaired p21 binding was ineffective in inducing morphological changes, while a mutant lacking GAP activity alone was effective. Microinjected n-chimaerin colocalized in situ with F-actin. Taken together, these results suggest that n-chimaerin acts synergistically with Rac1 and Cdc42Hs to induce actin-based morphological changes and that this action involves Rac1 and Cdc42Hs binding but not GAP activity. Thus, GAPs may have morphological functions in addition to downregulation of GTPases.
机译：n-Chimaerin是一种GTPase激活蛋白（GAP），主要用于Rac1，而对于Cdc42Hs则较少。 n-chimaerin的GAP活性受磷脂和佛波酯的调节。将Rac1和Cdc42Hs微量注射到哺乳动物细胞中分别诱导了基于肌动蛋白的结构片状脂蛋白和丝状伪足的形成，而前者通过共注射chimaerin GAP域来防止。引人注目的是，将全长正-chierererin显微注射到成纤维细胞和神经母细胞瘤细胞中会诱导同时形成片状脂蛋白和丝状伪足。这些结构经历溶解和形成的循环，类似于在成纤维细胞和神经元生长锥的前沿发生的自然形态事件。显性阴性Rac1（T17N）和Cdc42Hs（T17N）分别抑制n-chimaerin对片状脂蛋白和丝状伪足形成的影响。通过Rho GDP解离抑制剂的共同注射或佛波酯的治疗也可抑制n-Chimaerin的作用。没有GAP活性和受损的p21结合的突变体n-chimaerin在诱导形态变化方面无效，而仅缺乏GAP活性的突变体则有效。显微注射的n-chimaerin与F-肌动蛋白原位共定位。综上所述，这些结果表明，n-chimaerin与Rac1和Cdc42Hs协同作用，诱导基于肌动蛋白的形态变化，并且该作用涉及Rac1和Cdc42Hs的结合，但不涉及GAP活性。因此，除了GTPase的下调外，GAP还可能具有形态学功能。

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