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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
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scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex

机译：疤痕，WASp相关蛋白，通过Arp2 / 3复合物激活肌动蛋白丝的成核

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摘要

The Asp2/3 complex, a stable assembly of two actin-related proteins (Asp2 and Arp3) with five other subunits, caps the pointed end of actin filaments and nucleates actin polymerization with low efficiency. WASP and Scar are two similar Proteins that bind the p21 subunit of the Asp2/3 complex, but their effect on the nucleation activity of the complex was not known. We report that full-length, recombinant human Scar protein, as well as N-terminally truncated Scar Proteins, enhance nucleation by the Arp2/3 complex. By themselves, these proteins either have no effect or inhibit actin pelymerization. The actin monomer-binding W domain and the p2I-binding A domain from the C terminus of Scar are both required to activate Arp2/3 complex. A protein-rich domain in the middle of Scar enhances the activity of the W and A domains. Preincubating Scar and Arp2/3 complex with actin filaments overcomes the initial lag in polymerization, suggesting that efficient nucleation by the Arp2/3 complex requires assembly on the side of a preexisting filament- a dendritic nucleation mechanism. The Arp2/3 complex with full-length Scar, Scar containing P, W, and A domains, or Scar containing W and A domains overcomes inhibition of nucleation by the actin monomer-binding protein profilin, giving active nucleation over a low background of spontaneous nucleation. These results show that Scar and, likely, related proteins, such as the Cdc42 targets WASP and N-WASp, are `endogenous activations of actin polymerizationby the arap2/3 comples.
机译：Asp2 / 3复合物是两个肌动蛋白相关蛋白（Asp2和Arp3）与其他五个亚基的稳定装配，它覆盖了肌动蛋白丝的尖端，使肌动蛋白聚合效率低下。 WASP和Scar是两种相似的蛋白，它们结合Asp2 / 3复合物的p21亚基，但是它们对复合物成核活性的影响尚不清楚。我们报告全长，重组人疤痕蛋白，以及N末端截短的疤痕蛋白，增强了Arp2 / 3复合物的成核作用。这些蛋白质本身不起作用或抑制肌动蛋白聚合。激活丝氨酸C3末端的肌动蛋白单体结合W结构域和p2I结合A结构域都需要激活Arp2 / 3复合物。疤痕中间的富含蛋白质的结构域增强了W和A结构域的活性。将Scar和Arp2 / 3复合物与肌动蛋白丝一起预孵育克服了聚合反应中的最初滞后现象，这表明Arp2 / 3复合物的有效成核需要在预先存在的细丝侧进行组装-树突状成核机制。具有全长疤痕，包含P，W和A结构域的疤痕或包含W和A结构域的疤痕的Arp2 / 3复合物克服了肌动蛋白单体结合蛋白profilin对成核的抑制作用，从而在低自发背景下提供了主动成核成核。这些结果表明，疤痕以及可能相关的蛋白质（例如，Cdc42靶标WASP和N-WASp）是arap2 / 3化合物对肌动蛋白聚合反应的内源性激活。

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