Department of Physiology, Northwestern University Feinberg School of Medicine, Chicago, IL, 60611, USA.
Department of Neurology, Northwestern University Feinberg School of Medicine, Chicago, IL, 60611, USA.
Mol Psychiatry. 2021 Jun;26(6):1775-1789. doi: 10.1038/s41380-020-00991-1. Epub 2021 Jan 4.
Homer1 is a synaptic scaffold protein that regulates glutamatergic synapses and spine morphogenesis. HOMER1 knockout (KO) mice show behavioral abnormalities related to psychiatric disorders, and HOMER1 has been associated with psychiatric disorders such as addiction, autism disorder (ASD), schizophrenia (SZ), and depression. However, the mechanisms by which it promotes spine stability and its global function in maintaining the synaptic proteome has not yet been fully investigated. Here, we used computational approaches to identify global functions for proteins containing the Homer1-interacting PPXXF motif within the postsynaptic compartment. Ankyrin-G was one of the most topologically important nodes in the postsynaptic peripheral membrane subnetwork, and we show that one of the PPXXF motifs, present in the postsynaptically-enriched 190 kDa isoform of ankyrin-G (ankyrin-G 190), is recognized by the EVH1 domain of Homer1. We use proximity ligation combined with super-resolution microscopy to map the interaction of ankyrin-G and Homer1 to distinct nanodomains within the spine head and correlate them with spine head size. This interaction motif is critical for ankyrin-G 190's ability to increase spine head size, and for the maintenance of a stable ankyrin-G pool in spines. Intriguingly, lack of Homer1 significantly upregulated the abundance of ankyrin-G, but downregulated Shank3 in cortical crude plasma membrane fractions. In addition, proteomic analysis of the cortex in HOMER1 KO and wild-type (WT) mice revealed a global reshaping of the postsynaptic proteome, surprisingly characterized by extensive upregulation of synaptic proteins. Taken together, we show that Homer1 and its protein interaction motif have broad global functions within synaptic protein-protein interaction networks. Enrichment of disease risk factors within these networks has important implications for neurodevelopmental disorders including bipolar disorder, ASD, and SZ.
Homer1 是一种突触支架蛋白,可调节谷氨酸能突触和脊柱形态发生。 Homer1 敲除 (KO) 小鼠表现出与精神障碍相关的行为异常,并且 Homer1 与精神障碍如成瘾、自闭症障碍 (ASD)、精神分裂症 (SZ) 和抑郁症有关。然而,它促进脊柱稳定性的机制及其在维持突触蛋白质组中的全局功能尚未得到充分研究。在这里,我们使用计算方法来识别在后突触隔室中包含 Homer1 相互作用的 PPXXF 基序的蛋白质的全局功能。锚蛋白-G 是突触后周边膜子网中的拓扑最重要的节点之一,我们表明,锚蛋白-G 中存在的一个 PPXXF 基序(在后突触中丰富的 190kDa 同工型锚蛋白-G(ankyrin-G 190))被 Homer1 的 EVH1 结构域识别。我们使用邻近连接结合超分辨率显微镜来映射锚蛋白-G 和 Homer1 之间的相互作用到脊柱头部的不同纳米域,并将它们与脊柱头部大小相关联。这种相互作用基序对于 ankryn-G 190 增加脊柱头部大小的能力以及在脊柱中保持稳定的 ankryn-G 池至关重要。有趣的是,缺乏 Homer1 会显著增加 ankryn-G 的丰度,但会降低皮质粗质膜部分中的 Shank3 含量。此外,对 HOMER1 KO 和野生型 (WT) 小鼠大脑皮层的蛋白质组学分析显示,突触后蛋白质组的全局重塑,令人惊讶的是,突触蛋白广泛上调。总之,我们表明 Homer1 及其蛋白质相互作用基序在后突触蛋白质-蛋白质相互作用网络中具有广泛的全局功能。这些网络中疾病风险因素的富集对包括双相情感障碍、ASD 和 SZ 在内的神经发育障碍具有重要意义。