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首页> 外文期刊>Journal of Cellular Physiology >Relationship of p21-activated kinase (PAK) and filopodia to persistence and oncogenic transformation.
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Relationship of p21-activated kinase (PAK) and filopodia to persistence and oncogenic transformation.

机译：短暂快速脉冲刺激导致蛋白激酶21的关系)丝状伪足的持久性和致癌转换。

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Previously, we found that oncogenically transformed cells had fewer filopodia and more large, p21-activated kinase (PAK)-dependent features than normal cells. These large protrusions (LPs) were increased in cells expressing RhoA(N19) with Cdc42-associated kinase (ACK). Here, we determine how GTPase-mediated mechanisms of focal contact (FC) regulation affect these protrusions. Constructs encoding various proteins were introduced into cells which were then studied by microscopy and computerized image processing and analysis. Constructs that prevented PAK recruitment by PAK-interacting exchange factor (PIX) or restricted PAK residence time on FCs decreased both protrusions. Thus, filopodia were also PAK-dependent. A comparison of FC distribution in cells expressing PAK in the presence or absence of PAK kinase inhibitor domain (KID) suggested that PAK enlarged FCs without affecting the prevalence of either protrusion. KID or Nck expression increased LPs but not filopodia. Nck failed to synergize with KID or ACK and RhoA(N19) in enhancing LPs. Nck and KID synergistically enhanced filopodia, possibly because Nck recruited PAK to FCs while KID prevented their dissociation by PAK-mediated autophosphorylation. Coexpression of Nck, ACK, and RhoA(N19) abrogated filopodia and replicated the transformed phenotype. Since Nck recruitment of PAK is implicated in persistence of directional movement, we studied the PAK-Nck interface. Filopodia were eliminated by the Nck PAK-binding domain and LPs by the PAK Nck-binding domain. The results suggested that filopodia formation has more stringent requirements than LP formation, and Nck and PAK are used differently in the protrusions. Loss of filopodia in transformed cells may reflect defective regulation of GTPase mechanisms.
机译：以前,我们发现oncogenically转化细胞丝状伪足较少等等短暂快速脉冲刺激导致蛋白激酶21大型)端依赖比正常的细胞功能。在细胞突起(LPs)增加与Cdc42-associated激酶表达RhoA (N19)(ACK)。焦接触(FC)监管机制影响这些突起。介绍了各种蛋白质进入细胞然后研究了显微镜和电脑吗图像处理和分析。预防PAK PAK-interacting招聘交换因子(沥青)或限制PAK住宅时间在FCs下降两个突起。丝状伪足也PAK-dependent。在细胞表达PAK FC的分布PAK激酶抑制剂的存在与否域(孩子)建议PAK FCs肿大在不影响的流行突出。但不是丝状伪足。孩子和ACK RhoA (N19)提高有限合伙人。和孩子表现为协同作用增强的丝状伪足,可能是因为Nck招募PAK FCs的同时孩子阻止他们PAK-mediated离解自身磷酸化。和RhoA (N19)废除丝状伪足和复制转换后的表型。持久性的PAK有牵连定向运动,我们研究了PAK-Nck接口。PAK Nck-binding PAK-binding域和有限合伙人域。比LP形成有更严格的要求形成,Nck PAK使用不同的突起。转化细胞可能反映了缺陷GTPase监管机制。

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