通过黏着连接点感知肌动蛋白动力学。
Sensing Actin Dynamics through Adherens Junctions.
机构信息
Department of Dermatology, Northwestern University, The Feinberg School of Medicine, Chicago, IL 60611, USA.
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Zuckerman Mind Brain and Behavior Institute, Columbia University, New York, NY 10032, USA.
出版信息
Cell Rep. 2020 Feb 25;30(8):2820-2833.e3. doi: 10.1016/j.celrep.2020.01.106.
We study punctate adherens junctions (pAJs) to determine how short-lived cadherin clusters and relatively stable actin bundles interact despite differences in dynamics. We show that pAJ-linked bundles consist of two distinct regions-the bundle stalk (AJ-BS) and a tip (AJ-BT) positioned between cadherin clusters and the stalk. The tip differs from the stalk in a number of ways: it is devoid of the actin-bundling protein calponin, and exhibits a much faster F-actin turnover rate. While F-actin in the stalk displays centripetal movement, the F-actin in the tip is immobile. The F-actin turnover in both the tip and stalk is dependent on cadherin cluster stability, which in turn is regulated by F-actin. The close bidirectional coupling between the stability of cadherin and associated F-actin shows how pAJs, and perhaps other AJs, allow cells to sense and coordinate the dynamics of the actin cytoskeleton in neighboring cells-a mechanism we term "dynasensing."
我们研究点状粘着连接（pAJ），以确定尽管动力学存在差异，但短暂的钙黏蛋白簇和相对稳定的肌动蛋白束如何相互作用。我们表明，pAJ 连接的束由两个不同的区域组成 - 束干（AJ-BS）和位于钙黏蛋白簇和干之间的尖端（AJ-BT）。尖端在许多方面与干不同：它不含肌动蛋白束蛋白钙调蛋白，并且表现出更快的 F-肌动蛋白周转率。虽然干中的 F-肌动蛋白显示向心运动，但尖端中的 F-肌动蛋白是不动的。尖端和干中的 F-肌动蛋白周转率都依赖于钙黏蛋白簇的稳定性，而钙黏蛋白簇的稳定性又受到 F-肌动蛋白的调节。钙黏蛋白和相关 F-肌动蛋白稳定性之间的紧密双向偶联表明，pAJ 甚至其他 AJ 如何使细胞能够感知和协调相邻细胞中肌动蛋白细胞骨架的动力学 - 我们称之为“dynasensing”的机制。
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