PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast.
PI4P and Rab inputs collaborate in myosin-V-dependent transport of secretory compartments in yeast.
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DOI：
10.1016/j.devcel.2010.11.006
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发表时间：
2011-01-18
影响因子：
11.8
通讯作者：
Bretscher, Anthony
中科院分区：
文献类型：
--
作者：
Santiago-Tirado, Felipe H.;Legesse-Miller, Aster;Schott, Daniel;Bretscher, Anthony
细胞极性涉及特定膜和大分子在正确的时间运输到正确的位置。在出芽酵母中，分泌囊泡由肌球蛋白v Myo2p运输到细胞生长的部位。我们发现磷脂酰肌醇4-磷酸（PI4P）存在于后期分泌室中，对它们与Myo2p的关联和转运至关重要。此外，trans -高尔基网络（TGN） Rab Ypt31/32p和分泌囊泡Rab Sec4p都直接但明显地与Myo2p结合，这些相互作用也是分泌室运输所必需的。增强Myo2p与PI4P的相互作用绕过了与Ypt31/32p和Sec4p相互作用的要求。结合其他遗传数据，结果表明Rab蛋白和PI4P在分泌区室与Myo2p的关联中协同作用。因此，我们证明了一个巧合检测机制协调了来自PI4P和适当的Rab的输入，以进行分泌室运输。
Cell polarity involves transport of specific membranes and macromolecules at the right time to the right place. In budding yeast, secretory vesicles are transported by the myosin-V Myo2p to sites of cell growth. We show that phosphatidylinositol 4-phosphate (PI4P) is present in late secretory compartments and is critical for their association with, and transport by, Myo2p. Further, the Trans-Golgi network (TGN) Rab Ypt31/32p and secretory vesicle Rab Sec4p each bind directly, but distinctly, to Myo2p, and these interactions are also required for secretory compartment transport. Enhancing Myo2p's interaction with PI4P bypasses the requirement for interaction with Ypt31/32p and Sec4p. Together with additional genetic data, the results indicate that Rab proteins and PI4P collaborate in the association of secretory compartments with Myo2p. Thus, we show that a coincidence detection mechanism coordinates inputs from PI4P and the appropriate Rab for secretory compartment transport.
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