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Rap2 and TNIK control Plexin-dependent tiled synaptic innervation in C. elegans .
- Source :
-
ELife [Elife] 2018 Jul 31; Vol. 7. Date of Electronic Publication: 2018 Jul 31. - Publication Year :
- 2018
-
Abstract
- During development, neurons form synapses with their fate-determined targets. While we begin to elucidate the mechanisms by which extracellular ligand-receptor interactions enhance synapse specificity by inhibiting synaptogenesis, our knowledge about their intracellular mechanisms remains limited. Here we show that Rap2 GTPase ( rap-2 ) and its effector, TNIK ( mig-15 ), act genetically downstream of Plexin ( plx-1 ) to restrict presynaptic assembly and to form tiled synaptic innervation in C. elegans . Both constitutively GTP- and GDP-forms of rap-2 mutants exhibit synaptic tiling defects as plx-1 mutants, suggesting that cycling of the RAP-2 nucleotide state is critical for synapse inhibition. Consistently, PLX-1 suppresses local RAP-2 activity. Excessive ectopic synapse formation in mig-15 mutants causes a severe synaptic tiling defect. Conversely, overexpression of mig-15 strongly inhibited synapse formation, suggesting that mig-15 is a negative regulator of synapse formation. These results reveal that subcellular regulation of small GTPase activity by Plexin shapes proper synapse patterning in vivo.<br />Competing Interests: XC, AS, AH, MK, EF, NW, BM, HM, KM No competing interests declared<br /> (© 2018, Chen et al.)
- Subjects :
- Animals
Caenorhabditis elegans chemistry
Caenorhabditis elegans genetics
Caenorhabditis elegans Proteins genetics
Guanosine Diphosphate chemistry
Guanosine Triphosphate chemistry
Mutation
Nerve Tissue Proteins genetics
Neurogenesis genetics
Neurons chemistry
Protein Serine-Threonine Kinases genetics
Receptors, Cell Surface genetics
Signal Transduction genetics
Synapses chemistry
Synapses genetics
Synapses pathology
rap GTP-Binding Proteins genetics
Caenorhabditis elegans Proteins chemistry
Nerve Tissue Proteins chemistry
Protein Serine-Threonine Kinases chemistry
Receptors, Cell Surface chemistry
rap GTP-Binding Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 2050-084X
- Volume :
- 7
- Database :
- MEDLINE
- Journal :
- ELife
- Publication Type :
- Academic Journal
- Accession number :
- 30063210
- Full Text :
- https://doi.org/10.7554/eLife.38801