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Ena/VASP 蛋白的心血管功能：过去、现在及未来。

Cardiovascular Functions of Ena/VASP Proteins: Past, Present and Beyond.

机构信息

Institute for Vascular Signalling, Centre for Molecular Medicine, Goethe University, 60596 Frankfurt am Main, Germany.

German Centre of Cardiovascular Research (DZHK), Partner Site Rhein-Main, 60596 Frankfurt am Main, Germany.

出版信息

Cells. 2023 Jun 28;12(13):1740. doi: 10.3390/cells12131740.

DOI:10.3390/cells12131740
PMID:37443774
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10340426/
Abstract

Actin binding proteins are of crucial importance for the spatiotemporal regulation of actin cytoskeletal dynamics, thereby mediating a tremendous range of cellular processes. Since their initial discovery more than 30 years ago, the enabled/vasodilator-stimulated phosphoprotein (Ena/VASP) family has evolved as one of the most fascinating and versatile family of actin regulating proteins. The proteins directly enhance actin filament assembly, but they also organize higher order actin networks and link kinase signaling pathways to actin filament assembly. Thereby, Ena/VASP proteins regulate dynamic cellular processes ranging from membrane protrusions and trafficking, and cell-cell and cell-matrix adhesions, to the generation of mechanical tension and contractile force. Important insights have been gained into the physiological functions of Ena/VASP proteins in platelets, leukocytes, endothelial cells, smooth muscle cells and cardiomyocytes. In this review, we summarize the unique and redundant functions of Ena/VASP proteins in cardiovascular cells and discuss the underlying molecular mechanisms.

摘要

肌动蛋白结合蛋白对于肌动蛋白细胞骨架动力学的时空调节至关重要，从而介导了大量的细胞过程。自 30 多年前首次发现以来，增强蛋白/血管扩张刺激磷蛋白（Ena/VASP）家族已成为最迷人、用途最广泛的肌动蛋白调节蛋白家族之一。这些蛋白直接增强肌动蛋白丝的组装，但它们也组织更高阶的肌动蛋白网络，并将激酶信号通路与肌动蛋白丝组装联系起来。因此，Ena/VASP 蛋白调节从膜突和运输、细胞-细胞和细胞-基质黏附，到机械张力和收缩力的产生等各种动态细胞过程。在血小板、白细胞、内皮细胞、平滑肌细胞和心肌细胞中，人们对 Ena/VASP 蛋白的生理功能有了重要的认识。在这篇综述中，我们总结了 Ena/VASP 蛋白在心血管细胞中的独特和冗余功能，并讨论了潜在的分子机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/fd3233d3f2a4/cells-12-01740-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/0aa1cf33d944/cells-12-01740-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/f3adbb88e6a7/cells-12-01740-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/6af3fadd8ae2/cells-12-01740-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/f62bb6cb23d2/cells-12-01740-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/5ce33cdc1978/cells-12-01740-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/6b84edb5080b/cells-12-01740-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/8936f51a6bea/cells-12-01740-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/6280404890a2/cells-12-01740-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/9a88befd95b6/cells-12-01740-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/fd3233d3f2a4/cells-12-01740-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/0aa1cf33d944/cells-12-01740-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/f3adbb88e6a7/cells-12-01740-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/6af3fadd8ae2/cells-12-01740-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/f62bb6cb23d2/cells-12-01740-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/5ce33cdc1978/cells-12-01740-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/6b84edb5080b/cells-12-01740-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/8936f51a6bea/cells-12-01740-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/6280404890a2/cells-12-01740-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/9a88befd95b6/cells-12-01740-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2718/10340426/fd3233d3f2a4/cells-12-01740-g010.jpg

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Front Cell Dev Biol. 2022 Oct 3;10:1008898. doi: 10.3389/fcell.2022.1008898. eCollection 2022.
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