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肌动蛋白结合蛋白与肌动蛋白丝的带刺末端相互作用，控制动态不稳定性、封端、分支和运动性。

Profilin Interaction with Actin Filament Barbed End Controls Dynamic Instability, Capping, Branching, and Motility.

作者信息

Pernier Julien, Shekhar Shashank, Jegou Antoine, Guichard Bérengère, Carlier Marie-France

机构信息

Cytoskeleton Dynamics and Motility Group, I2BC, CNRS, Gif-sur-Yvette 91198, France.

Cytoskeleton Dynamics and Motility Group, I2BC, CNRS, Gif-sur-Yvette 91198, France.

出版信息

Dev Cell. 2016 Jan 25;36(2):201-14. doi: 10.1016/j.devcel.2015.12.024.

DOI:10.1016/j.devcel.2015.12.024
PMID:26812019
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4729542/
Abstract

Cell motility and actin homeostasis depend on the control of polarized growth of actin filaments. Profilin, an abundant regulator of actin dynamics, supports filament assembly at barbed ends by binding G-actin. Here, we demonstrate how, by binding and destabilizing filament barbed ends at physiological concentrations, profilin also controls motility, cell migration, and actin homeostasis. Profilin enhances filament length fluctuations. Profilin competes with Capping Protein at barbed ends, which generates a lower amount of profilin-actin than expected if barbed ends were tightly capped. Profilin competes with barbed end polymerases, such as formins and VopF, and inhibits filament branching by WASP-Arp2/3 complex by competition for filament barbed ends, accounting for its as-yet-unknown effects on motility and metastatic cell migration observed in this concentration range. In conclusion, profilin is a major coordinator of polarized growth of actin filaments, controlled by competition between barbed end cappers, trackers, destabilizers, and filament branching machineries.

摘要

细胞运动性和肌动蛋白稳态依赖于肌动蛋白丝极化生长的调控。丝切蛋白是肌动蛋白动力学的一种丰富调节因子，通过结合G-肌动蛋白来支持丝在带刺末端的组装。在此，我们证明了丝切蛋白如何通过在生理浓度下结合并破坏丝的带刺末端，来控制细胞运动性、细胞迁移和肌动蛋白稳态。丝切蛋白增强了丝长度的波动。丝切蛋白在带刺末端与封端蛋白竞争，这导致生成的丝切蛋白-肌动蛋白的量低于如果带刺末端被紧密封端时预期的量。丝切蛋白与带刺末端聚合酶（如formin和VopF）竞争，并通过与丝的带刺末端竞争来抑制WASP-Arp2/3复合物介导的丝分支，这解释了在该浓度范围内观察到的其对细胞运动性和转移性细胞迁移的未知影响。总之，丝切蛋白是肌动蛋白丝极化生长的主要协调者，由带刺末端封端蛋白、追踪蛋白、去稳定剂和丝分支机制之间的竞争所控制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/da17c77c44b6/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/2476b0328608/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/088e2245c17c/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/8145a42518d3/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/9a004fee4568/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/ce99b2671b76/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/bed2d1ab026e/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/355f931c0a1e/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/da17c77c44b6/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/2476b0328608/fx1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/088e2245c17c/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/8145a42518d3/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/9a004fee4568/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/ce99b2671b76/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/bed2d1ab026e/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/355f931c0a1e/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b1b/4729542/da17c77c44b6/gr7.jpg

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