4.7 Review

Liprin-α-Mediated Assemblies and Their Roles in Synapse Formation

Journal

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fcell.2021.653381

Keywords

SYD2; scaffold protein; presynaptic active zone; LLPS; protein structure; coiled coil; protein– protein interaction

Funding

  1. National Natural Science Foundation of China [31971131, 31770791, 31870757]
  2. Natural Science Foundation of Guangdong Province [2016A030312016]
  3. Shenzhen-Hong Kong Institute of Brain Science, Shenzhen Fundamental Research Institutions [2021SHIB0002]

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Brain functions such as memory and learning rely on specialized cellular junctions called synapses, where liprin-alpha proteins play a crucial role in coordinating various synaptic proteins. Genetic and biochemical studies have provided insights into the functions of liprin-alpha in synapse formation. Recent structural findings are beginning to uncover the molecular basis of synaptic assembly.
Brain's functions, such as memory and learning, rely on synapses that are highly specialized cellular junctions connecting neurons. Functional synapses orchestrate the assembly of ion channels, receptors, enzymes, and scaffold proteins in both pre- and post-synapse. Liprin-alpha proteins are master scaffolds in synapses and coordinate various synaptic proteins to assemble large protein complexes. The functions of liprin-alpha s in synapse formation have been largely uncovered by genetic studies in diverse model systems. Recently, emerging structural and biochemical studies on liprin-alpha proteins and their binding partners begin to unveil the molecular basis of the synaptic assembly. This review summarizes the recent structural findings on liprin-alpha s, proposes the assembly mechanism of liprin-alpha-mediated complexes, and discusses the liprin-alpha-organized assemblies in the regulation of synapse formation and function.

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