Myosin XIX
Myosin XIX
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DOI：
10.1007/978-3-030-38062-5_20
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发表时间：
2020-01-01
期刊：
影响因子：
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通讯作者：
Quintero, Omar A.
中科院分区：
文献类型：
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作者：
Bocanegra, Jennifer L.;Adikes, Rebecca;Quintero, Omar A.
在世纪之交，广泛可用的基因组数据库的诞生导致了许多以前未知的肌球蛋白基因的鉴定，以及包括MYO19在内的新型肌球蛋白的鉴定。进一步的序列分析揭示了XIX类肌球蛋白独特的进化历史。MYO19在从脊椎动物到一些单细胞生物的物种中都有发现，而在一些包含传统实验模式生物的谱系中已经丢失。运动域中独特的序列表明，特定类别的机械力化学可能与其作为线粒体相关马达的细胞功能有关。过去10年的研究表明，MYO19是一种肌动蛋白激活的ATPase，能够基于肌动蛋白进行运输，对运动域中一些保守差异的研究表明，它们在MYO19运动活动中具有重要意义。与货物结合的MyMOMA尾部结构域包含两种不同的与线粒体外膜成分相互作用的机制，MYO19表达的扰动导致线粒体运动和动力学的改变，从而影响细胞功能。本章总结了该领域的现状，并强调了潜在的新的研究方向。
The birth of widely available genomic databases at the turn of the millennium led to the identification of many previously unknown myosin genes and identification of novel classes of myosin, including MYO19. Further sequence analysis has revealed the unique evolutionary history of class XIX myosins. MYO19 is found in species ranging from vertebrates to some unicellular organisms, while it has been lost from some lineages containing traditional experimental model organisms. Unique sequences in the motor domain suggest class-specific mechanochemistry that may relate to its cellular function as a mitochondria-associated motor. Work over the past 10 years has demonstrated that MYO19 is an actin-activated ATPase capable of actin-based transport, and investigation of some of the conserved differences within the motor domain indicate their importance in MYO19 motor activity. The cargo-binding MyMOMA tail domain contains two distinct mechanisms of interaction with mitochondrial outer membrane components, and perturbation of MYO19 expression leads to alterations in mitochondrial movement and dynamics that impact cell function. This chapter summarizes the current state of the field and highlights potential new directions of inquiry.