Using ALS to understand profilin 1's diverse roles in cellular physiology.

Halli L Lindamood, Tatiana M Liu, Tracy-Ann Read, Eric A Vitriol
{"title":"Using ALS to understand profilin 1's diverse roles in cellular physiology.","authors":"Halli L Lindamood, Tatiana M Liu, Tracy-Ann Read, Eric A Vitriol","doi":"10.1002/cm.21896","DOIUrl":null,"url":null,"abstract":"<p><p>Profilin is an actin monomer-binding protein whose role in actin polymerization has been studied for nearly 50 years. While its principal biochemical features are now well understood, many questions remain about how profilin controls diverse processes within the cell. Dysregulation of profilin has been implicated in a broad range of human diseases, including neurodegeneration, inflammatory disorders, cardiac disease, and cancer. For example, mutations in the profilin 1 gene (PFN1) can cause amyotrophic lateral sclerosis (ALS), although the precise mechanisms that drive neurodegeneration remain unclear. While initial work suggested proteostasis and actin cytoskeleton defects as the main pathological pathways, multiple novel functions for PFN1 have since been discovered that may also contribute to ALS, including the regulation of nucleocytoplasmic transport, stress granules, mitochondria, and microtubules. Here, we will review these newly discovered roles for PFN1, speculate on their contribution to ALS, and discuss how defects in actin can contribute to these processes. By understanding profilin 1's involvement in ALS pathogenesis, we hope to gain insight into this functionally complex protein with significant influence over cellular physiology.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-07-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cytoskeleton (Hoboken, N.J.)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/cm.21896","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Profilin is an actin monomer-binding protein whose role in actin polymerization has been studied for nearly 50 years. While its principal biochemical features are now well understood, many questions remain about how profilin controls diverse processes within the cell. Dysregulation of profilin has been implicated in a broad range of human diseases, including neurodegeneration, inflammatory disorders, cardiac disease, and cancer. For example, mutations in the profilin 1 gene (PFN1) can cause amyotrophic lateral sclerosis (ALS), although the precise mechanisms that drive neurodegeneration remain unclear. While initial work suggested proteostasis and actin cytoskeleton defects as the main pathological pathways, multiple novel functions for PFN1 have since been discovered that may also contribute to ALS, including the regulation of nucleocytoplasmic transport, stress granules, mitochondria, and microtubules. Here, we will review these newly discovered roles for PFN1, speculate on their contribution to ALS, and discuss how defects in actin can contribute to these processes. By understanding profilin 1's involvement in ALS pathogenesis, we hope to gain insight into this functionally complex protein with significant influence over cellular physiology.

利用 ALS 了解 profilin 1 在细胞生理学中的各种作用。
profilin 是一种肌动蛋白单体结合蛋白,人们对它在肌动蛋白聚合中的作用已经研究了近 50 年。虽然现在人们对它的主要生化特征已经有了很好的了解,但对于肌动蛋白如何控制细胞内的各种过程仍有许多疑问。profilin 的失调与多种人类疾病有关,包括神经变性、炎症性疾病、心脏病和癌症。例如,profilin 1 基因(PFN1)突变可导致肌萎缩性脊髓侧索硬化症(ALS),但驱动神经变性的确切机制仍不清楚。虽然最初的研究认为蛋白稳态和肌动蛋白细胞骨架缺陷是主要的病理途径,但后来发现了 PFN1 的多种新功能,这些功能也可能导致 ALS,包括调节核细胞质转运、应激颗粒、线粒体和微管。在此,我们将回顾这些新发现的 PFN1 作用,推测它们对 ALS 的贡献,并讨论肌动蛋白的缺陷如何导致这些过程。通过了解 profilin 1 在渐冻症发病机制中的参与,我们希望能深入了解这种对细胞生理学有重大影响的功能复杂的蛋白质。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信