酰基辅酶a结合蛋白AcbdA是过氧化物酶体在细粒曲霉早期核内体上搭便车所必需的。

IF 2.7 3区 生物学 Q3 CELL BIOLOGY
Bellana Driscoll, Madison B Fountain, Isabella N Gates, Reihane Abdollahi, Allison M Langley, Matthew B Owens, Jenna R Christensen, John Salogiannis
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引用次数: 0

摘要

微管上的马达驱动运输对于细胞器在细胞内的分布至关重要。最常见的是,细胞器运动是由装载接头介导的,装载接头是细胞器表面的蛋白质,直接招募基于微管的马达。最近发现了另一种被称为搭便车的机制:一些细胞器移动,不是通过直接招募马达,而是通过膜接触点附着在马达驱动的囊泡上,并沿着微管搭便车。在真菌和动物中观察到细胞器搭便车。在丝状真菌中,几乎所有的过氧化物酶体都在早期核内体(EEs)上搭便车移动。在真菌细粒曲霉中,ee相关连接蛋白PxdA和DipA对于建立过氧化物酶体运动所需的ee -过氧化物酶体膜接触位点至关重要。过氧化物酶体膜蛋白是否存在调控过氧化物酶体在EEs上搭便车尚不清楚。通过正向诱变筛选,我们发现了一种含有酰基辅酶a结合(ACB)结构域的蛋白AcbdA/AN1062,该蛋白通过其尾锚定的跨膜结构域(TMD)定位于过氧化物酶体。删除AcbdA基因或仅删除其n端ACB结构域会干扰过氧化物酶体的运动和分布。重要的是,AcbdA对于EEs的移动或在EEs上招募PxdA和DipA不是必需的。脂肪酸(FA)诱导的过氧化物酶体运动的增加需要AcbdA,这表明过氧化物酶体搭乘EEs与FA代谢有关。突变保守的FFAT基序,预测与内质网(ER)相互作用,对过氧化物酶体的运动没有影响。综上所述,我们的数据表明AcbdA是过氧化物酶体在EEs上搭便车所需的过氧化物酶体膜蛋白。AcbdA参与过氧化物酶体搭便车代表了与Acbd4/5蛋白已知功能的分歧,并为我们对Acbd4/5蛋白家族功能的理解增加了层次。[媒体:见文][媒体:见文][媒体:见文]。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Acyl-coA binding protein AcbdA is required for peroxisome hitchhiking on early endosomes in Aspergillus nidulans.

Motor-driven transport on microtubules is critical for distributing organelles throughout the cell. Most commonly, organelle movement is mediated by cargo adaptors, proteins on the surface of an organelle that directly recruit microtubule-based motors. An alternative mechanism called hitchhiking was recently discovered: some organelles move, not by recruiting the motors directly, but instead by using membrane contact sites to attach to motor-driven vesicles and hitchhike along microtubules. Organelle hitchhiking is observed across fungi and animals. In filamentous fungi, nearly all peroxisomes move by hitchhiking on early endosomes (EEs). In the fungus Aspergillus nidulans, EE-associated linker proteins PxdA and DipA are critical for establishing EE-peroxisome membrane contact sites required for peroxisome movement. Whether peroxisome-membrane proteins exist that regulate peroxisome hitchhiking on EEs is not known. Through a forward mutagenesis screen, we discovered an acyl-coA binding (ACB) domain-containing protein AcbdA/AN1062 that localizes to peroxisomes via its tail-anchored transmembrane domain (TMD). Deleting the AcbdA gene or only its N-terminal ACB domain perturbs the movement and distribution of peroxisomes. Importantly, AcbdA is not required for the movement of EEs or for the recruitment of PxdA and DipA on EEs. Fatty acid (FA)-induced increases in peroxisome movement require AcbdA, suggesting that peroxisome hitchhiking on EEs is coupled to FA metabolism. Mutating a conserved FFAT motif, predicted to interact with the endoplasmic reticulum (ER), has no effect on peroxisome movement. Taken together, our data indicate that AcbdA is a peroxisome-membrane protein required for peroxisome hitchhiking on EEs. AcbdA's involvement in peroxisome hitchhiking represents a divergence from known functions of Acbd4/5 proteins and adds layers to our understanding of the functionality of the Acbd4/5 family of proteins. [Media: see text] [Media: see text] [Media: see text].

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来源期刊
Molecular Biology of the Cell
Molecular Biology of the Cell 生物-细胞生物学
CiteScore
6.00
自引率
6.10%
发文量
402
审稿时长
2 months
期刊介绍: MBoC publishes research articles that present conceptual advances of broad interest and significance within all areas of cell, molecular, and developmental biology. We welcome manuscripts that describe advances with applications across topics including but not limited to: cell growth and division; nuclear and cytoskeletal processes; membrane trafficking and autophagy; organelle biology; quantitative cell biology; physical cell biology and mechanobiology; cell signaling; stem cell biology and development; cancer biology; cellular immunology and microbial pathogenesis; cellular neurobiology; prokaryotic cell biology; and cell biology of disease.
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