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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early stage of endocytosis
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The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early stage of endocytosis

机译：WASP / Las17p相互作用蛋白Bzz1p在内吞作用的早期阶段与Myo5p一起起作用

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摘要

The formation of actin filaments is crucial for endocytosis and other interrelated cellular phenomena such as motility, polarized morphogenesis, and cytokinesis. In this paper we have investigated the role of the WASP/Las17-interacting protein Bzz1p in endocytosis and trafficking to the vacuole. We and others have recently shown that Bzz1p is an actin patch protein that interacts directly with Las17p via a SH3-polyproline interaction. Bzz1p functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. In an in vitro bead assay, GST-Bzz1p fusion protein triggers a functional actin polymerization machinery through its two C-terminal SH3 domains. In this paper we implicate Bzz1p with the type I myosins both in fluid-phase and in the internalization step of receptor-mediated endocytosis. As deduced from their localization as GFP fusions, the vacuolar delivery of endocytic and biosynthetic cargoes as well as the multivesicular body pathway appear unaffected. We further elucidate Bzz1p direct participation in actin polymerization by demonstrating that each of the SH3 domains of Bzz1p individually is able to trigger actin polymerization in a cell-free system dependent on Arp2/3, Las17p, Vrp1p, and the type I myosins. Taken together, our results show that Bzz1p participates, essentially via its SH3 domains, in early steps of endocytosis together with known actin nucleation activators.
机译：肌动蛋白丝的形成对于内吞作用和其他相互关联的细胞现象（例如运动性，极化形态发生和胞质分裂）至关重要。在本文中，我们研究了与WASP / Las17相互作用的蛋白Bzz1p在胞吞和向液泡运输中的作用。我们和其他人最近显示，Bzz1p是一种肌动蛋白补丁蛋白，可通过SH3-polyproline相互作用直接与Las17p相互作用。 Bzz1p与I型肌球蛋白一起发挥功能，以在NaCl胁迫后恢复肌动蛋白细胞骨架的极性。在体外珠检测中，GST-Bzz1p融合蛋白通过其两个C末端SH3域触发功能性肌动蛋白聚合机制。在本文中，我们在受体介导的内吞作用的液相和内化步骤中都将Bzz1p掺入了I型肌球蛋白。从它们作为GFP融合物的定位推断，内吞和生物合成货物的液泡递送以及多囊体途径似乎没有受到影响。我们通过证明Bzz1p的每个SH3结构域分别能够在依赖Arp2 / 3，Las17p，Vrp1p和I型肌球蛋白的无细胞系统中触发肌动蛋白聚合，进一步阐明Bzz1p直接参与肌动蛋白聚合反应。两者合计，我们的结果表明，Bzz1p基本上通过其SH3结构域与已知的肌动蛋白成核激活剂一起参与了内吞作用的早期步骤。

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