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LIM 结构域激酶的调控与信号传导。

Regulation and signaling of the LIM domain kinases.

作者信息

Casanova-Sepúlveda Gabriela, Boggon Titus J

机构信息

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.

Department of Pharmacology, Yale University, New Haven, Connecticut, USA.

出版信息

Bioessays. 2025 Jan;47(1):e2400184. doi: 10.1002/bies.202400184. Epub 2024 Oct 3.

DOI:10.1002/bies.202400184
PMID:39361252
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11663136/
Abstract

The LIM domain kinases (LIMKs) are important actin cytoskeleton regulators. These proteins, LIMK1 and LIMK2, are nodes downstream of Rho GTPases and are the key enzymes that phosphorylate cofilin/actin depolymerization factors to regulate filament severing. They therefore perform an essential role in cascades that control actin depolymerization. Signaling of the LIMKs is carefully regulated by numerous inter- and intra-molecular mechanisms. In this review, we discuss recent findings that improve the understanding of LIM domain kinase regulation mechanisms. We also provide an up-to-date review of the role of the LIM domain kinases, their architectural features, how activity is impacted by other proteins, and the implications of these findings for human health and disease.

摘要

LIM结构域激酶(LIMKs)是重要的肌动蛋白细胞骨架调节因子。这些蛋白,即LIMK1和LIMK2,是Rho GTP酶下游的节点,并且是磷酸化丝切蛋白/肌动蛋白解聚因子以调节细丝切断的关键酶。因此,它们在控制肌动蛋白解聚的级联反应中发挥着重要作用。LIMKs的信号传导受到众多分子间和分子内机制的精细调节。在这篇综述中,我们讨论了最近的研究结果,这些结果增进了我们对LIM结构域激酶调节机制的理解。我们还提供了关于LIM结构域激酶的作用、其结构特征、活性如何受到其他蛋白影响以及这些发现对人类健康和疾病的影响的最新综述。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/c02081e769f2/nihms-2023799-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/176c8b35f822/nihms-2023799-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/a44bcfa6850c/nihms-2023799-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/7cbc820774fe/nihms-2023799-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/8ac4ad9fa6ce/nihms-2023799-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/c02081e769f2/nihms-2023799-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/176c8b35f822/nihms-2023799-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/a44bcfa6850c/nihms-2023799-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/7cbc820774fe/nihms-2023799-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/8ac4ad9fa6ce/nihms-2023799-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f8b4/11663136/c02081e769f2/nihms-2023799-f0005.jpg

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Front Physiol. 2024 Dec 18;15:1506356. doi: 10.3389/fphys.2024.1506356. eCollection 2024.
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Engineering memory with an extrinsically disordered kinase.用外在无序的激酶工程记忆。
Sci Adv. 2023 Nov 17;9(46):eadh1110. doi: 10.1126/sciadv.adh1110. Epub 2023 Nov 15.
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Dorsal visual stream and LIMK1: hemideletion, haplotype, and enduring effects in children with Williams syndrome.背侧视觉通路与 LIMK1:威廉姆斯综合征患儿的半缺失、单体型和持久影响。
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