The class V myosin interactome of the human pathogen Aspergillus fumigatus reveals novel interactions with COPII vesicle transport proteins.

The class V myosin interactome of the human pathogen Aspergillus fumigatus reveals novel interactions with COPII vesicle transport proteins.
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DOI:
10.1016/j.bbrc.2020.04.111
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发表时间:
2020-06
影响因子:
3.1
通讯作者:
H. Renshaw;P. R. Juvvadi;D. C. Cole;W. Steinbach
H. Renshaw;P. R. Juvvadi;D. C. Cole;W. Steinbach
中科院分区:
生物学4区
文献类型:
--
作者:
H. Renshaw;P. R. Juvvadi;D. C. Cole;W. Steinbach

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人类真菌病原体烟曲霉可导致免疫功能低下个体的危及生命的侵袭性曲霉病。对宿主环境的适应是烟曲霉生存不可或缺的一部分,需要短距离和长距离囊泡运输的协调,以在整个真菌中移动重要成分。我们以前报道了MyoE,唯一的V类肌球蛋白,对烟曲霉菌丝生长和毒力的重要性。V类肌球蛋白是基于肌动蛋白的运载货物的马达蛋白,其含有用于特定货物的独特结合位点。肌球蛋白V携带的特定货物尚未在任何真菌中确定,以前的研究仅确定了与V类肌球蛋白相互作用的单一组分。在这里,我们利用质谱为基础的全蛋白质组学方法,以确定MyoE相互作用的蛋白质在烟曲霉的第一次。几个蛋白质先前显示通过物理和遗传方法与肌球蛋白V相互作用得到证实,验证了我们的蛋白质组学分析。重要的是,我们确定了新的MyoE相互作用蛋白,包括细胞骨架网络的成员,细胞壁合成,钙信号和一组外壳蛋白复合物II(COPII)蛋白参与内质网(ER)到高尔基体的运输。此外,我们分析了COPII蛋白UsoA(Uso1),SrgE(Sec31)和SrgF(Sec23)的定位模式,这表明MyoE在ER到高尔基体运输中的潜在作用。
The human fungal pathogenAspergillus fumigatuscauses life-threatening invasive aspergillosis in immunocompromised individuals. Adaptation to the host environment is integral to survival ofA. fumigatusand requires the coordination of short- and long-distance vesicular transport to move essential components throughout the fungus. We previously reported the importance of MyoE, the only class V myosin, for hyphal growth and virulence ofA. fumigatus. Class V myosins are actin-based, cargo-carrying motor proteins that contain unique binding sites for specific cargo. Specific cargo carried by myosin V has not been identified in any fungus, and previous studies have only identified single components that interact with class V myosins. Here we utilized a mass spectrometry-based whole proteomic approach to identify MyoE interacting proteins inA. fumigatusfor the first time. Several proteins previously shown to interact with myosin V through physical and genetic approaches were confirmed, validating our proteomic analysis. Importantly, we identified novel MyoE-interacting proteins, including members of the cytoskeleton network, cell wall synthesis, calcium signaling and a group of coat protein complex II (COPII) proteins involved in the endoplasmic reticulum (ER) to Golgi transport. Furthermore, we analyzed the localization patterns of the COPII proteins, UsoA (Uso1), SrgE (Sec31), and SrgF (Sec23), which suggested a potential role for MyoE in ER to Golgi trafficking.