Cytoskeletal Components Define Protein Location to Membrane Microdomains*
Cytoskeletal Components Define Protein Location to Membrane Microdomains*
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DOI：
10.1074/mcp.m114.046904
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发表时间：
2015-06
影响因子：
7
通讯作者：
Witold Szymanski;Henrik Zauber;A. Erban;M. Górka;X. Wu;W. Schulze
中科院分区：
文献类型：
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作者：
Witold Szymanski;Henrik Zauber;A. Erban;M. Górka;X. Wu;W. Schulze
质膜是一个重要的隔室，在外部或内部刺激下，其成分会发生动态变化。假设有序低密度（DRM）和无序高密度（DSM）膜相中蛋白质的动态亚区室需要与细胞骨架成分相互作用。在这里，我们系统地分析了肌动蛋白或微管蛋白破坏对膜密度相之间蛋白质分布的影响。我们使用蛋白质组筛选来鉴定亚膜位置改变的候选蛋白质，然后对拟南芥进行生化或细胞生物学表征。我们发现几种蛋白质，例如质膜 ATP 酶、受体激酶或 remorin，在细胞骨架破坏时导致膜密度相之间的差异分布。此外，在大多数情况下，观察到了相反的效果：肌动蛋白丝的破坏很大程度上导致蛋白质从 DRM 到 DSM 膜部分的重新分配，而微管蛋白的破坏导致膜上蛋白质的总体耗尽。我们得出的结论是，肌动蛋白丝对于蛋白质在不同膜相之间的动态运动是必需的，并且微管对于微结构域的形成不一定重要，但它们可以控制膜相中存在的蛋白质量。
The plasma membrane is an important compartment that undergoes dynamic changes in composition upon external or internal stimuli. The dynamic subcompartmentation of proteins in ordered low-density (DRM) and disordered high-density (DSM) membrane phases is hypothesized to require interactions with cytoskeletal components. Here, we systematically analyzed the effects of actin or tubulin disruption on the distribution of proteins between membrane density phases. We used a proteomic screen to identify candidate proteins with altered submembrane location, followed by biochemical or cell biological characterization in Arabidopsis thaliana. We found that several proteins, such as plasma membrane ATPases, receptor kinases, or remorins resulted in a differential distribution between membrane density phases upon cytoskeletal disruption. Moreover, in most cases, contrasting effects were observed: Disruption of actin filaments largely led to a redistribution of proteins from DRM to DSM membrane fractions while disruption of tubulins resulted in general depletion of proteins from the membranes. We conclude that actin filaments are necessary for dynamic movement of proteins between different membrane phases and that microtubules are not necessarily important for formation of microdomains as such, but rather they may control the protein amount present in the membrane phases.