ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011
The Liprin homology domain is essential for the homomeric interaction of SYD-2/Liprin-α protein in presynaptic assembly.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 51 citations in OpenAlex.
- Semi-automatic 3D-quantification of in-vivo synapse formation.BMC bioinformatics · 2026Article
- Genome-wide analysis reveals pathways important for the development and maturation of excitatory synaptic connections to GABAergic neurons.G3 (Bethesda, Md.) · 2026Article
- Submembrane liprin-α1 clusters spatially localize insulin granule fusion.The Journal of cell biology · 2025Article
- Potential phosphorylation of Liprin-α1 at threonine 701 regulates integrin-mediated cell motility.PloS one · 2025Article
- LRK-1/LRRK2 and AP-3 regulate trafficking of synaptic vesicle precursors through active zone protein SYD-2/Liprin-α.PLoS genetics · 2024Article
- A syndromic neurodevelopmental disorder caused by rare variants in PPFIA3.American journal of human genetics · 2024Article
- SAD-1 kinase controls presynaptic phase separation by relieving SYD-2/Liprin-α autoinhibition.PLoS biology · 2023Article
- Article
- Presynaptic Cytomatrix Proteins.Advances in neurobiology · 2023Article
- Liprins in oncogenic signaling and cancer cell adhesion.Oncogene · 2021Review
- UNC-2 CaV2 Channel Localization at Presynaptic Active Zones Depends on UNC-10/RIM and SYD-2/Liprin-α inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Liprin-α-Mediated Assemblies and Their Roles in Synapse Formation.Frontiers in cell and developmental biology · 2021Review
- PTP-3 phosphatase promotes intramolecular folding of SYD-2 to inactivate kinesin-3 UNC-104 in neurons.Molecular biology of the cell · 2020Article
- Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity.Nature communications · 2020Article
- RIMB-1/RIM-Binding Protein and UNC-10/RIM Redundantly Regulate Presynaptic Localization of the Voltage-Gated Calcium Channel inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Vertebrate Presynaptic Active Zone Assembly: a Role Accomplished by Diverse Molecular and Cellular Mechanisms.Molecular neurobiology · 2018Review
- Liprin-α3 controls vesicle docking and exocytosis at the active zone of hippocampal synapses.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Active zone proteins are transported via distinct mechanisms regulated by Par-1 kinase.PLoS genetics · 2017Article
- Presynaptic spinophilin tunes neurexin signalling to control active zone architecture and function.Nature communications · 2015Article
- Structural and Biochemical Basis for the Inhibitory Effect of Liprin-α3 on Mouse Diaphanous 1 (mDia1) Function.The Journal of biological chemistry · 2015Article
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Authors and funding
2 authors at 2 institutions in 3 countries.
Funding
Abstract
Synapses are asymmetric structures that are specialized for neuronal signal transduction. A unique set of proteins is present at the presynaptic active zone, which is a core structure essential for neurotransmitter release. In Caenorhabditis elegans HSN neurons, SYD-2, a Liprin-α family protein, acts together with a GAP protein SYD-1 to promote presynaptic assembly. Previous studies have shown that elevating the activity of syd-2 can bypass the requirement of syd-1. Liprin-α proteins are composed of coiled-coil-rich regions in the N-terminal half, which mediate interactions with adapter proteins at the presynaptic active zone, and three SAM domains in the C terminus, which bind proteins such as LAR receptor tyrosine phosphatase. To address the molecular mechanism by which SYD-2 activity is regulated, we performed structure-function studies. By monitoring the ability of SYD-2 transgenes to rescue syd-2(lf) and to suppress syd-1(lf) phenotypes in HSN neuron synapses, we identified the N-terminal half of SYD-2 as minimally required for rescuing syd-2(lf) phenotypes. A highly conserved short coiled-coil segment named Liprin Homology 1 (LH1) domain is both necessary and sufficient to suppress syd-1(lf) defects. We show that the LH1 domain forms a dimer and promotes further oligomerization and/or complex formation of SYD-2/Liprin-α proteins. The role of the LH1 domain in presynaptic assembly can be partially complemented by artificial dimerization. These findings suggest a model by which the self-assembly of SYD-2/Liprin-α proteins mediated by the coiled-coil LH1 domain is one of the key steps to the accumulation of presynaptic components at nascent synaptic junctions.
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