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解析作为来自……的首个丝切蛋白的EhActo的生物学特性

Unravelling the Biology of EhActo as the First Cofilin From .

作者信息

Kumar Nitesh, Rath Pragyan Parimita, Aggarwal Priyanka, Maiti Sankar, Bhavesh Neel Sarovar, Gourinath Samudrala

机构信息

Department of Pathology, Indira Gandhi Institute of Medical Sciences, Patna, India.

International Centre for Genetic Engineering and Biotechnology, New Delhi, India.

出版信息

Front Cell Dev Biol. 2022 Feb 25;10:785680. doi: 10.3389/fcell.2022.785680. eCollection 2022.

DOI:10.3389/fcell.2022.785680
PMID:35281106
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8914023/
Abstract

Actin-depolymerising factors (ADF) are a known family of proteins that regulate actin dynamics. Actin regulation is critical for primitive eukaryotes since it drives their key cellular processes. , a protist human pathogen harbours eleven proteins within this family, however, with no actin depolymerising protein reported to date. We present here the NMR model of EhActo, the first Cofilin from that severs actin filaments and also participates in cellular events like phagocytosis and pseudopod formation. The model typically represents the ADF-homology domain compared to other cofilins. Uniquely, EhActo lacks the critical Serine3 residue present in all known actophorins mediating its phospho-regulation. The second mode of regulation that cofilin's are subjected to is via their interaction with 14-3-3 proteins through the phosphorylated Serine residue and a consensus binding motif. We found a unique interaction between EhActo and 14-3-3 without the presence of the consensus motif or the phosphorylated Serine. These interesting results present unexplored newer mechanisms functional in this pathogen to regulate actophorin. Through our structural and biochemical studies we have deciphered the mechanism of action of EhActo, implicating its role in amoebic biology.

摘要

肌动蛋白解聚因子（ADF）是一类已知的调节肌动蛋白动力学的蛋白质家族。肌动蛋白调节对原始真核生物至关重要，因为它驱动着它们的关键细胞过程。疟原虫，一种原生动物人类病原体，在这个家族中有11种蛋白质，然而，迄今为止尚未报道有肌动蛋白解聚蛋白。我们在此展示了EhActo的核磁共振模型，它是疟原虫中首个切断肌动蛋白丝并参与吞噬作用和伪足形成等细胞事件的丝切蛋白。与其他丝切蛋白相比，该模型典型地代表了ADF同源结构域。独特的是，EhActo缺乏所有已知介导其磷酸化调节的肌动蛋白结合蛋白中存在的关键丝氨酸3残基。丝切蛋白受到的第二种调节方式是通过其磷酸化的丝氨酸残基和一个共有结合基序与14-3-3蛋白相互作用。我们发现EhActo与14-3-3之间存在独特的相互作用，而不存在共有基序或磷酸化丝氨酸。这些有趣的结果揭示了该病原体中尚未探索的调节肌动蛋白结合蛋白的新机制。通过我们的结构和生化研究，我们已经破译了EhActo的作用机制，表明其在阿米巴生物学中的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/0ddf427e9356/fcell-10-785680-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/9f02c0c45b1a/fcell-10-785680-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/c1bb0fbb5f89/fcell-10-785680-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/a032e088e295/fcell-10-785680-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/f3352eb8b962/fcell-10-785680-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/7392ab2bafbb/fcell-10-785680-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/2cc6768a10da/fcell-10-785680-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/7c5cf89429aa/fcell-10-785680-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/0ddf427e9356/fcell-10-785680-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/9f02c0c45b1a/fcell-10-785680-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/c1bb0fbb5f89/fcell-10-785680-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/a032e088e295/fcell-10-785680-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/f3352eb8b962/fcell-10-785680-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/7392ab2bafbb/fcell-10-785680-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/2cc6768a10da/fcell-10-785680-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/7c5cf89429aa/fcell-10-785680-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a324/8914023/0ddf427e9356/fcell-10-785680-g008.jpg

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