Revisiting I-BAR Proteins at Central Synapses.
Revisiting I-BAR Proteins at Central Synapses.
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DOI：
10.3389/fncir.2021.787436
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发表时间：
2021
影响因子：
3.5
通讯作者：
Westbrook GL
中科院分区：
文献类型：
--
作者：
Chatzi C;Westbrook GL
树突棘是中枢神经系统（CNS）兴奋性突触的突触后特征，作为电和化学隔室，以及受体循环和信号分子定位的支架，已被广泛研究。脊柱的形状、数量和分子组成的动态变化，以及它们如何受到神经活动的调节，对突触的功效、突触的可塑性以及最终的学习和记忆都至关重要。树突棘起源于细胞膜的外突，但与非神经元细胞的膜突研究相比，这方面的脊柱形成和稳定并不是研究的主要焦点。我们在这里回顾了一个参与突触膜曲率的蛋白家族，BAR （Bin-Amphiphysin-Rvs）结构域蛋白。逆BAR （I-BAR）蛋白亚家族感知并引入向外的膜曲率，并作为细胞膜和细胞骨架之间的桥梁。我们重点研究了在中枢神经系统中表达的三种I-BAR结构域蛋白：Mtss2、MIM和IRSp53，它们基于自我结合的能力促进负的凹曲率。最近的研究表明，它们在突触形成和突触可塑性方面具有不同的功能。i - bar的作用也由与其他信号组件的串扰形成，形成可以以电路依赖的方式发挥作用的信号平台。我们讨论了另一个潜在的重要特征-一些BAR结构域蛋白通过异齐聚影响其他家族成员功能的能力。了解突触I-BAR蛋白表达的时空分辨率及其相互作用，有助于深入了解中枢神经系统活动依赖性神经可塑性与网络重布线之间的相互作用。
Dendritic spines, the distinctive postsynaptic feature of central nervous system (CNS) excitatory synapses, have been studied extensively as electrical and chemical compartments, as well as scaffolds for receptor cycling and positioning of signaling molecules. The dynamics of the shape, number, and molecular composition of spines, and how they are regulated by neural activity, are critically important in synaptic efficacy, synaptic plasticity, and ultimately learning and memory. Dendritic spines originate as outward protrusions of the cell membrane, but this aspect of spine formation and stabilization has not been a major focus of investigation compared to studies of membrane protrusions in non-neuronal cells. We review here one family of proteins involved in membrane curvature at synapses, the BAR (Bin-Amphiphysin-Rvs) domain proteins. The subfamily of inverse BAR (I-BAR) proteins sense and introduce outward membrane curvature, and serve as bridges between the cell membrane and the cytoskeleton. We focus on three I-BAR domain proteins that are expressed in the central nervous system: Mtss2, MIM, and IRSp53 that promote negative, concave curvature based on their ability to self-associate. Recent studies suggest that each has distinct functions in synapse formation and synaptic plasticity. The action of I-BARs is also shaped by crosstalk with other signaling components, forming signaling platforms that can function in a circuit-dependent manner. We discuss another potentially important feature—the ability of some BAR domain proteins to impact the function of other family members by heterooligomerization. Understanding the spatiotemporal resolution of synaptic I-BAR protein expression and their interactions should provide insights into the interplay between activity-dependent neural plasticity and network rewiring in the CNS.
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影响因子：
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作者：
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