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首页> 外文期刊>Molecular cell >A reciprocal interdependence between Nck and PI(4,5)P(2) promotes localized N-WASp-mediated actin polymerization in living cells.
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A reciprocal interdependence between Nck and PI(4,5)P(2) promotes localized N-WASp-mediated actin polymerization in living cells.

机译：Nck和PI（4,5）P（2）之间的相互依赖促进了活细胞中的局部N-WASp介导的肌动蛋白聚合。

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摘要

Modulation of actin dynamics through the N-WASp/Arp2/3 pathway is important in cell locomotion, membrane trafficking, and pathogen infection. Here, we demonstrate that Nck is essential for actin remodeling stimulated by phosphatidylinositol 4,5 bisphosphate (PI(4,5)P(2)) and, conversely, that PI(4,5)P(2) is necessary for localized actin polymerization induced by Nck in vivo. Nck knockdown or knockout suppressed actin comets induced by phosphatidylinositol 5-kinase (PIP5K), and PIP5K stimulated tyrosine phosphorylation of an Nck SH2 domain binding partner, suggesting that Nck couples phosphotyrosine- and phosphoinositide-dependent signals. We show that PI(4,5)P(2) and PIP5K are both enriched at actin comets induced by Nck aggregates and that formation of actin comets was strongly inhibited by coclustering with an inositol 5-phosphatase domain to decrease local PI(4,5)P(2) levels. The extent of Nck-induced actin polymerization was also modulated by PI(4,5)P(2)-sensitive N-WASp mutants. This study uncovers a strong reciprocal interdependence between Nck and PI(4,5)P(2) in promoting localized N-WASp-mediated actin polymerization in cells.
机译：通过N-WASp / Arp2 / 3途径对肌动蛋白动力学的调节在细胞运动，膜运输和病原体感染中很重要。在这里，我们证明Nck对于磷脂酰肌醇4,5双磷酸（PI（4,5）P（2））刺激的肌动蛋白重塑至关重要，相反，PI（4,5）P（2）对于局部肌动蛋白是必需的Nck在体内诱导聚合反应。 Nck敲低或敲除抑制了磷脂酰肌醇5激酶（PIP5K）和PIP5K刺激的Nck SH2域结合伴侣的酪氨酸磷酸化肌动蛋白彗星，表明Nck偶联了磷酸酪氨酸和磷酸肌醇依赖性信号。我们显示PI（4,5）P（2）和PIP5K都富集在Nck聚集体诱导的肌动蛋白彗星上，肌动蛋白彗星的形成受到与肌醇5-磷酸酶结构域共聚以降低局部PI（4， 5）P（2）级别。 Nck诱导肌动蛋白聚合的程度也受到PI（4,5）P（2）敏感N-WASp突变体的调节。这项研究发现Nck和PI（4,5）P（2）在促进细胞中的局部N-WASp介导的肌动蛋白聚合之间有很强的相互依赖关系。

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