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Nudel binds Cdc42GAP to modulate Cdc42 activity at the leading edge of migrating cells

机译：Nudel结合Cdc42GAP来调节迁移细胞前沿的Cdc42活性

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摘要

Cdc42GAP promotes inactivation of Cdc42, a small GTPase whose activation at the leading edge by guanine nucleotide exchange factors is critical for cell migration. How Cdc42GAP is regulated to ensure proper levels of active Cdc42 is poorly understood. Here we show that Nudel, a cytoplasmic dynein regulator, competes with Cdc42 for binding Cdc42GAP. Consequently, Nudel can inhibit Cdc42GAP-mediated inactivation of Cdc42 in a dose-dependent manner. Both Nudel and Cdc42GAP exhibit leading-edge localization in migrating cells. The localization of Nudel requires its phosphorylation by Erk1/2. Depleting Nudel by RNAi or overexpression of a nonphosphorylatable mutant abolishes Cdc42 activation and cell migration. Our data thus uncover Nudel as a regulator of Cdc42 during cell migration. Nudel facilitates cell migration by sequestering Cdc42GAP at the leading edge to stabilize active Cdc42 in response to extracellular stimuli. Excess active Cdc42 may in turn control its own activity by recruiting Cdc42GAP from Nudel.
机译：Cdc42GAP促进Cdc42的失活，Cdc42是一种小GTP酶，其鸟嘌呤核苷酸交换因子在前沿激活对细胞迁移至关重要。如何对Cdc42GAP进行调节以确保适当水平的活性Cdc42知之甚少。在这里，我们显示细胞质动力蛋白调节剂Nudel与Cdc42竞争结合Cdc42GAP。因此，Nudel可以剂量依赖性方式抑制Cdc42GAP介导的Cdc42失活。 Nudel和Cdc42GAP均在迁移细胞中表现出前沿定位。 Nudel的定位需要被Erk1 / 2磷酸化。通过RNAi消耗Nudel或不可磷酸化突变体的过表达消除了Cdc42激活和细胞迁移。因此，我们的数据揭示了Nudel在细胞迁移过程中作为Cdc42的调节剂。 Nudel通过隔离前沿的Cdc42GAP来稳定细胞中的活性Cdc42，从而促进细胞迁移，从而响应细胞外刺激。通过从Nudel募集Cdc42GAP，过多的活动Cdc42可能进而控制其自身的活动。

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