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The Liprin Homology Domain Is Essential for the Homomeric Interaction of SYD-2/Liprin-α Protein in Presynaptic Assembly
| Title: | The Liprin Homology Domain Is Essential for the Homomeric Interaction of SYD-2/Liprin-α Protein in Presynaptic Assembly |
| Authors: | Taru, Hidenori Browse this author →KAKEN DB | | Jin, Yishi Browse this author |
| Issue Date: | 9-Nov-2011 |
| Publisher: | Society for Neuroscience |
| Journal Title: | Journal of Neuroscience |
| Volume: | 31 |
| Issue: | 45 |
| Start Page: | 16261 |
| End Page: | 16268 |
| Publisher DOI: | 10.1523/JNEUROSCI.0002-11.2011 |
| 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. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/49183 |
| Appears in Collections: | 創成研究機構 (Creative Research Institution) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 多留 偉功
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