Journal articles: 'C. elegans synapse'

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Fenyves, Bánk G., Gábor S. Szilágyi, Zsolt Vassy, Csaba Sőti, and Peter Csermely. "Synaptic polarity and sign-balance prediction using gene expression data in the Caenorhabditis elegans chemical synapse neuronal connectome network." PLOS Computational Biology 16, no. 12 (December 21, 2020): e1007974. http://dx.doi.org/10.1371/journal.pcbi.1007974.

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Graph theoretical analyses of nervous systems usually omit the aspect of connection polarity, due to data insufficiency. The chemical synapse network of Caenorhabditis elegans is a well-reconstructed directed network, but the signs of its connections are yet to be elucidated. Here, we present the gene expression-based sign prediction of the ionotropic chemical synapse connectome of C. elegans (3,638 connections and 20,589 synapses total), incorporating available presynaptic neurotransmitter and postsynaptic receptor gene expression data for three major neurotransmitter systems. We made predictions for more than two-thirds of these chemical synapses and observed an excitatory-inhibitory (E:I) ratio close to 4:1 which was found similar to that observed in many real-world networks. Our open source tool (http://EleganSign.linkgroup.hu) is simple but efficient in predicting polarities by integrating neuronal connectome and gene expression data.

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Broadie, Kendal S., and Janet E. Richmond. "Establishing and sculpting the synapse in Drosophila and C. elegans." Current Opinion in Neurobiology 12, no. 5 (October 2002): 491–98. http://dx.doi.org/10.1016/s0959-4388(02)00359-8.

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Allen, Peter B., Allyson E. Sgro, Daniel L. Chao, Byron E. Doepker, J. Scott Edgar, Kang Shen, and Daniel T. Chiu. "Single-synapse ablation and long-term imaging in live C. elegans." Journal of Neuroscience Methods 173, no. 1 (August 2008): 20–26. http://dx.doi.org/10.1016/j.jneumeth.2008.05.007.

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Kreyden, Victoria A., Elly B. Mawi, Kristen M. Rush, and Jennifer R. Kowalski. "UBC-9 Acts in GABA Neurons to Control Neuromuscular Signaling in C. elegans." Neuroscience Insights 15 (January 2020): 263310552096279. http://dx.doi.org/10.1177/2633105520962792.

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Regulation of excitatory to inhibitory signaling balance is essential to nervous system health and is maintained by numerous enzyme systems that modulate the activity, localization, and abundance of synaptic proteins. SUMOylation is a key post-translational regulator of protein function in diverse cells, including neurons. There, its role in regulating synaptic transmission through pre- and postsynaptic effects has been shown primarily at glutamatergic central nervous system synapses, where the sole SUMO-conjugating enzyme Ubc9 is a critical player. However, whether Ubc9 functions globally at other synapses, including inhibitory synapses, has not been explored. Here, we investigated the role of UBC-9 and the SUMOylation pathway in controlling the balance of excitatory cholinergic and inhibitory GABAergic signaling required for muscle contraction in Caenorhabditis elegans. We found inhibition or overexpression of UBC-9 in neurons modestly increased muscle excitation. Similar and even stronger phenotypes were seen with UBC-9 overexpression specifically in GABAergic neurons, but not in cholinergic neurons. These effects correlated with accumulation of synaptic vesicle-associated proteins at GABAergic presynapses, where UBC-9 and the C. elegans SUMO ortholog SMO-1 localized, and with defects in GABA-dependent behaviors. Experiments involving expression of catalytically inactive UBC-9 [UBC-9(C93S)], as well as co-expression of UBC-9 and SMO-1, suggested wild type UBC-9 overexpressed alone may act via substrate sequestration in the absence of sufficient free SUMO, underscoring the importance of tightly regulated SUMO enzyme function. Similar effects on muscle excitation, GABAergic signaling, and synaptic vesicle localization occurred with overexpression of the SUMO activating enzyme subunit AOS-1. Together, these data support a model in which UBC-9 and the SUMOylation system act at presynaptic sites in inhibitory motor neurons to control synaptic signaling balance in C. elegans. Future studies will be important to define UBC-9 targets at this synapse, as well as mechanisms by which UBC-9 and the SUMO pathway are regulated.

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Hendi, Ardalan, Mizuki Kurashina, and Kota Mizumoto. "Intrinsic and extrinsic mechanisms of synapse formation and specificity in C. elegans." Cellular and Molecular Life Sciences 76, no. 14 (April 29, 2019): 2719–38. http://dx.doi.org/10.1007/s00018-019-03109-1.

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Klassen, Matthew P., and Kang Shen. "Wnt Signaling Positions Neuromuscular Connectivity by Inhibiting Synapse Formation in C. elegans." Cell 130, no. 4 (August 2007): 704–16. http://dx.doi.org/10.1016/j.cell.2007.06.046.

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Zheng, Zhongfan, Xiumei Zhang, Junqiang Liu, Ping He, Shan Zhang, Yongning Zhang, Jie Gao, et al. "GABAergic synapses suppress intestinal innate immunity via insulin signaling in Caenorhabditis elegans." Proceedings of the National Academy of Sciences 118, no. 20 (May 10, 2021): e2021063118. http://dx.doi.org/10.1073/pnas.2021063118.

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GABAergic neurotransmission constitutes a major inhibitory signaling mechanism that plays crucial roles in central nervous system physiology and immune cell immunomodulation. However, its roles in innate immunity remain unclear. Here, we report that deficiency in the GABAergic neuromuscular junctions (NMJs) of Caenorhabditis elegans results in enhanced resistance to pathogens, whereas pathogen infection enhances the strength of GABAergic transmission. GABAergic synapses control innate immunity in a manner dependent on the FOXO/DAF-16 but not the p38/PMK-1 pathway. Our data reveal that the insulin-like peptide INS-31 level was dramatically decreased in the GABAergic NMJ GABAAR-deficient unc-49 mutant compared with wild-type animals. C. elegans with ins-31 knockdown or loss of function exhibited enhanced resistance to Pseudomonas aeruginosa PA14 exposure. INS-31 may act downstream of GABAergic NMJs and in body wall muscle to control intestinal innate immunity in a cell-nonautonomous manner. Our results reveal a signaling axis of synapse–muscular insulin–intestinal innate immunity in vivo.

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Baran, Renee, Liliana Castelblanco, Garland Tang, Ian Shapiro, Alexandr Goncharov, and Yishi Jin. "Motor Neuron Synapse and Axon Defects in a C. elegans Alpha-Tubulin Mutant." PLoS ONE 5, no. 3 (March 11, 2010): e9655. http://dx.doi.org/10.1371/journal.pone.0009655.

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Kovács, István A., Dániel L. Barabási, and Albert-László Barabási. "Uncovering the genetic blueprint of the C. elegans nervous system." Proceedings of the National Academy of Sciences 117, no. 52 (December 14, 2020): 33570–77. http://dx.doi.org/10.1073/pnas.2009093117.

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Despite rapid advances in connectome mapping and neuronal genetics, we lack theoretical and computational tools to unveil, in an experimentally testable fashion, the genetic mechanisms that govern neuronal wiring. Here we introduce a computational framework to link the adjacency matrix of a connectome to the expression patterns of its neurons, helping us uncover a set of genetic rules that govern the interactions between neurons in contact. The method incorporates the biological realities of the system, accounting for noise from data collection limitations, as well as spatial restrictions. The resulting methodology allows us to infer a network of 19 innexin interactions that govern the formation of gap junctions in Caenorhabditis elegans, five of which are already supported by experimental data. As advances in single-cell gene expression profiling increase the accuracy and the coverage of the data, the developed framework will allow researchers to systematically infer experimentally testable connection rules, offering mechanistic predictions for synapse and gap junction formation.

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Van Epps, H., Y. Dai, Y. Qi, A. Goncharov, and Y. Jin. "Nuclear pre-mRNA 3'-end processing regulates synapse and axon development in C. elegans." Development 137, no. 13 (June 8, 2010): 2237–50. http://dx.doi.org/10.1242/dev.049692.

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Baran, R., R. Aronoff, and G. Garriga. "The C. elegans homeodomain gene unc-42 regulates chemosensory and glutamate receptor expression." Development 126, no. 10 (May 15, 1999): 2241–51. http://dx.doi.org/10.1242/dev.126.10.2241.

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Genes that specify cell fate can influence multiple aspects of neuronal differentiation, including axon guidance, target selection and synapse formation. Mutations in the unc-42 gene disrupt axon guidance along the C. elegans ventral nerve cord and cause distinct functional defects in sensory-locomotory neural circuits. Here we show that unc-42 encodes a novel homeodomain protein that specifies the fate of three classes of neurons in the Caenorhabditis elegans nervous system: the ASH polymodal sensory neurons, the AVA, AVD and AVE interneurons that mediate repulsive sensory stimuli to the nematode head and anterior body, and a subset of motor neurons that innervate head and body-wall muscles. unc-42 is required for the expression of cell-surface receptors that are essential for the mature function of these neurons. In mutant animals, the ASH sensory neurons fail to express SRA-6 and SRB-6, putative chemosensory receptors. The AVA, AVD and AVE interneurons and RME and RMD motor neurons of unc-42 mutants similarly fail to express the GLR-1 glutamate receptor. These results show that unc-42 performs an essential role in defining neuron identity and contributes to the establishment of neural circuits in C. elegans by regulating the transcription of glutamate and chemosensory receptor genes.

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Burgess, Robert W., Kevin A. Peterson, Michael J. Johnson, Jeffrey J. Roix, Ian C. Welsh, and Timothy P. O'Brien. "Evidence for a Conserved Function in Synapse Formation Reveals Phr1 as a Candidate Gene for Respiratory Failure in Newborn Mice." Molecular and Cellular Biology 24, no. 3 (February 1, 2004): 1096–105. http://dx.doi.org/10.1128/mcb.24.3.1096-1105.2004.

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ABSTRACT Genetic studies using a set of overlapping deletions centered at the piebald locus on distal mouse chromosome 14 have defined a genomic region associated with respiratory distress and lethality at birth. We have isolated and characterized the candidate gene Phr1 that is located within the respiratory distress critical genomic interval. Phr1 is the ortholog of the human Protein Associated with Myc as well as Drosophila highwire and Caenorhabditis elegans regulator of presynaptic morphology 1. Phr1 is expressed in the embryonic and postnatal nervous system. In mice lacking Phr1, the phrenic nerve failed to completely innervate the diaphragm. In addition, nerve terminal morphology was severely disrupted, comparable with the synaptic defects seen in the Drosophila hiw and C. elegans rpm-1 mutants. Although intercostal muscles were completely innervated, they also showed dysmorphic nerve terminals. In addition, sensory neuron terminals in the diaphragm were abnormal. The neuromuscular junctions showed excessive sprouting of nerve terminals, consistent with inadequate presynaptic stimulation of the muscle. On the basis of the abnormal neuronal morphology seen in mice, Drosophila, and C. elegans, we propose that Phr1 plays a conserved role in synaptic development and is a candidate gene for respiratory distress and ventilatory disorders that arise from defective neuronal control of breathing.

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Yeh, E., S. Ng, T. Starich, J. Shaw, and M. Zhen. "[P64]: The C. elegans gap junction protein UNC‐7 is required for chemical synapse formation." International Journal of Developmental Neuroscience 24, no. 8 (November 16, 2006): 523. http://dx.doi.org/10.1016/j.ijdevneu.2006.09.127.

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Margeta, Milica A., Kang Shen, and Brock Grill. "Building a synapse: lessons on synaptic specificity and presynaptic assembly from the nematode C. elegans." Current Opinion in Neurobiology 18, no. 1 (February 2008): 69–76. http://dx.doi.org/10.1016/j.conb.2008.04.003.

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Oliver, Devyn, Shankar Ramachandran, Alison Philbrook, Christopher M. Lambert, Ken C. Q. Nguyen, David H. Hall, and Michael M. Francis. "Kinesin-3 mediated axonal delivery of presynaptic neurexin stabilizes dendritic spines and postsynaptic components." PLOS Genetics 18, no. 1 (January 28, 2022): e1010016. http://dx.doi.org/10.1371/journal.pgen.1010016.

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The functional properties of neural circuits are defined by the patterns of synaptic connections between their partnering neurons, but the mechanisms that stabilize circuit connectivity are poorly understood. We systemically examined this question at synapses onto newly characterized dendritic spines of C. elegans GABAergic motor neurons. We show that the presynaptic adhesion protein neurexin/NRX-1 is required for stabilization of postsynaptic structure. We find that early postsynaptic developmental events proceed without a strict requirement for synaptic activity and are not disrupted by deletion of neurexin/nrx-1. However, in the absence of presynaptic NRX-1, dendritic spines and receptor clusters become destabilized and collapse prior to adulthood. We demonstrate that NRX-1 delivery to presynaptic terminals is dependent on kinesin-3/UNC-104 and show that ongoing UNC-104 function is required for postsynaptic maintenance in mature animals. By defining the dynamics and temporal order of synapse formation and maintenance events in vivo, we describe a mechanism for stabilizing mature circuit connectivity through neurexin-based adhesion.

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Jin, YiShi. "Unraveling the mechanisms of synapse formation and axon regeneration: the awesome power of C. elegans genetics." Science China Life Sciences 58, no. 11 (November 2015): 1084–88. http://dx.doi.org/10.1007/s11427-015-4962-9.

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Yan, Xiaojie, and Yuequan Shen. "Preliminary crystallographic analysis of the kinase domain of SAD-1, a protein essential for presynaptic differentiation inCaenorhabditis elegans." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 4 (March 28, 2013): 449–52. http://dx.doi.org/10.1107/s1744309113006088.

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SAD-1 is a serine/threonine kinase which plays an important role in the regulation of both neuronal polarity and synapse formation inCaenorhabditis elegans. The kinase domain of SAD-1 fromC. eleganswas overexpressed inEscherichia coliBL21 (DE3) cells and purified to homogeneity using nickel–nitrilotriacetic acid metal-affinity, ion-exchange and gel-filtration chromatography. Diffraction-quality crystals were grown using the sitting-drop vapour-diffusion technique from a condition consisting of 1 MCAPSO pH 9.6, 10%(w/v) polyethylene glycol 3350. The crystals belonged to the monoclinic space groupC2, with unit-cell parametersa= 205.4,b= 57.1,c= 71.7 Å, β = 106.1°. X-ray diffraction data were recorded to 3.0 Å resolution from a single crystal using synchrotron radiation.

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Jin, YiShi. "Erratum to: Unraveling the mechanisms of synapse formation and axon regeneration: the awesome power of C. elegans genetics." Science China Life Sciences 58, no. 12 (December 2015): 1306. http://dx.doi.org/10.1007/s11427-015-4978-1.

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Pandey, Pratima, Anuradha Singh, Harjot Kaur, Anindya Ghosh-Roy, and Kavita Babu. "Increased dopaminergic neurotransmission results in ethanol dependent sedative behaviors in Caenorhabditis elegans." PLOS Genetics 17, no. 2 (February 1, 2021): e1009346. http://dx.doi.org/10.1371/journal.pgen.1009346.

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Ethanol is a widely used drug, excessive consumption of which could lead to medical conditions with diverse symptoms. Ethanol abuse causes dysfunction of memory, attention, speech and locomotion across species. Dopamine signaling plays an essential role in ethanol dependent behaviors in animals ranging from C. elegans to humans. We devised an ethanol dependent assay in which mutants in the dopamine autoreceptor, dop-2, displayed a unique sedative locomotory behavior causing the animals to move in circles while dragging the posterior half of their body. Here, we identify the posterior dopaminergic sensory neuron as being essential to modulate this behavior. We further demonstrate that in dop-2 mutants, ethanol exposure increases dopamine secretion and functions in a DVA interneuron dependent manner. DVA releases the neuropeptide NLP-12 that is known to function through cholinergic motor neurons and affect movement. Thus, DOP-2 modulates dopamine levels at the synapse and regulates alcohol induced movement through NLP-12.

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Mahoney, Timothy R., Qiang Liu, Takashi Itoh, Shuo Luo, Gayla Hadwiger, Rose Vincent, Zhao-Wen Wang, Mitsunori Fukuda, and Michael L. Nonet. "Regulation of Synaptic Transmission by RAB-3 and RAB-27 in Caenorhabditis elegans." Molecular Biology of the Cell 17, no. 6 (June 2006): 2617–25. http://dx.doi.org/10.1091/mbc.e05-12-1170.

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Rab small GTPases are involved in the transport of vesicles between different membranous organelles. RAB-3 is an exocytic Rab that plays a modulatory role in synaptic transmission. Unexpectedly, mutations in the Caenorhabditis elegans RAB-3 exchange factor homologue, aex-3, cause a more severe synaptic transmission defect as well as a defecation defect not seen in rab-3 mutants. We hypothesized that AEX-3 may regulate a second Rab that regulates these processes with RAB-3. We found that AEX-3 regulates another exocytic Rab, RAB-27. Here, we show that C. elegans RAB-27 is localized to synapse-rich regions pan-neuronally and is also expressed in intestinal cells. We identify aex-6 alleles as containing mutations in rab-27. Interestingly, aex-6 mutants exhibit the same defecation defect as aex-3 mutants. aex-6; rab-3 double mutants have behavioral and pharmacological defects similar to aex-3 mutants. In addition, we demonstrate that RBF-1 (rabphilin) is an effector of RAB-27. Therefore, our work demonstrates that AEX-3 regulates both RAB-3 and RAB-27, that both RAB-3 and RAB-27 regulate synaptic transmission, and that RAB-27 potentially acts through its effector RBF-1 to promote soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) function.

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Chew, Yee Lian, Laura J. Grundy, André E. X. Brown, Isabel Beets, and William R. Schafer. "Neuropeptides encoded by nlp-49 modulate locomotion, arousal and egg-laying behaviours in Caenorhabditis elegans via the receptor SEB-3." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1758 (September 10, 2018): 20170368. http://dx.doi.org/10.1098/rstb.2017.0368.

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Neuropeptide signalling has been implicated in a wide variety of biological processes in diverse organisms, from invertebrates to humans. The Caenorhabditis elegans genome has at least 154 neuropeptide precursor genes, encoding over 300 bioactive peptides. These neuromodulators are thought to largely signal beyond ‘wired’ chemical/electrical synapse connections, therefore creating a ‘wireless’ network for neuronal communication. Here, we investigated how behavioural states are affected by neuropeptide signalling through the G protein-coupled receptor SEB-3, which belongs to a bilaterian family of orphan secretin receptors. Using reverse pharmacology, we identified the neuropeptide NLP-49 as a ligand of this evolutionarily conserved neuropeptide receptor. Our findings demonstrate novel roles for NLP-49 and SEB-3 in locomotion, arousal and egg-laying. Specifically, high-content analysis of locomotor behaviour indicates that seb-3 and nlp-49 deletion mutants cause remarkably similar abnormalities in movement dynamics, which are reversed by overexpression of wild-type transgenes. Overexpression of NLP-49 in AVK interneurons leads to heightened locomotor arousal, an effect that is dependent on seb-3. Finally, seb-3 and nlp-49 mutants also show constitutive egg-laying in liquid medium and alter the temporal pattern of egg-laying in similar ways. Together, these results provide in vivo evidence that NLP-49 peptides act through SEB-3 to modulate behaviour, and highlight the importance of neuropeptide signalling in the control of behavioural states. This article is part of a discussion meeting issue ‘Connectome to behaviour: modelling C. elegans at cellular resolution’.

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Hodul, Molly, Rakesh Ganji, Caroline L. Dahlberg, Malavika Raman, and Peter Juo. "The WD40-repeat protein WDR-48 promotes the stability of the deubiquitinating enzyme USP-46 by inhibiting its ubiquitination and degradation." Journal of Biological Chemistry 295, no. 33 (June 25, 2020): 11776–88. http://dx.doi.org/10.1074/jbc.ra120.014590.

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Ubiquitination is a reversible post-translational modification that has emerged as a critical regulator of synapse development and function. However, the mechanisms that regulate the deubiquitinating enzymes (DUBs) responsible for the removal of ubiquitin from target proteins are poorly understood. We have previously shown that the DUB ubiquitin-specific protease 46 (USP-46) removes ubiquitin from the glutamate receptor GLR-1 and regulates its trafficking and degradation in Caenorhabditis elegans. We found that the WD40-repeat proteins WDR-20 and WDR-48 bind and stimulate the catalytic activity of USP-46. Here, we identified another mechanism by which WDR-48 regulates USP-46. We found that increased expression of WDR-48, but not WDR-20, promotes USP-46 abundance in mammalian cells in culture and in C. elegans neurons in vivo. Inhibition of the proteasome increased USP-46 abundance, and this effect was nonadditive with increased WDR-48 expression. We found that USP-46 is ubiquitinated and that expression of WDR-48 reduces the levels of ubiquitin–USP-46 conjugates and increases the t1/2 of USP-46. A point-mutated WDR-48 variant that disrupts binding to USP-46 was unable to promote USP-46 abundance in vivo. Finally, siRNA-mediated knockdown of wdr48 destabilizes USP46 in mammalian cells. Together, these results support a model in which WDR-48 binds and stabilizes USP-46 protein levels by preventing the ubiquitination and degradation of USP-46 in the proteasome. Given that a large number of USPs interact with WDR proteins, we propose that stabilization of DUBs by their interacting WDR proteins may be a conserved and widely used mechanism that controls DUB availability and function.

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Garcia, E. P., P. S. McPherson, T. J. Chilcote, K. Takei, and P. De Camilli. "rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin." Journal of Cell Biology 129, no. 1 (April 1, 1995): 105–20. http://dx.doi.org/10.1083/jcb.129.1.105.

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rbSec1 is a mammalian neuronal protein homologous to the yeast SEC1 gene product which is required for exocytosis. Mutations in Sec1 homologues in the nervous systems of C. elegans and D. melanogaster lead to defective neurotransmitter secretion. Biochemical studies have shown that recombinant rbSec1 binds syntaxin 1 but not SNAP-25 or synaptobrevin/VAMP, the two proteins which together with syntaxin 1 form the synaptic SNARE complex. In this study we have examined the subcellular localization of rbSec1 and the degree of interaction between rbSec1 and syntaxin 1 in situ. rbSec1, which we show here to be represented by two alternatively spliced isoforms, rbSec1A and B, has a widespread distribution in the axon and is not restricted to the nerve terminal. This distribution parallels the localization of syntaxin 1 and SNAP-25 along the entire axonal plasmalemma. rbSec1 is found in a soluble and a membrane-associated form. Although a pool of rbSec1 is present on the plasmalemma, the majority of membrane-bound rbSec1 is not associated with syntaxin 1. We also show that rbSec1 is not part of the synaptic SNARE complex or of the syntaxin 1/SNAP-25 complex we show to be present in non-synaptic regions of the axon. Thus, in spite of biochemical studies demonstrating the high affinity interaction of rbSec1 and syntaxin 1, our results indicate that rbSec1 and syntaxin 1 are not stably associated. They also suggest that the function of rbSec1, syntaxin 1, and SNAP-25 is not restricted to synaptic vesicle exocytosis at the synapse.

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Bohr, Tisha, Christian R. Nelson, Erin Klee, and Needhi Bhalla. "Spindle assembly checkpoint proteins regulate and monitor meiotic synapsis in C. elegans." Journal of Cell Biology 211, no. 2 (October 19, 2015): 233–42. http://dx.doi.org/10.1083/jcb.201409035.

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Homologue synapsis is required for meiotic chromosome segregation, but how synapsis is initiated between chromosomes is poorly understood. In Caenorhabditis elegans, synapsis and a checkpoint that monitors synapsis depend on pairing centers (PCs), cis-acting loci that interact with nuclear envelope proteins, such as SUN-1, to access cytoplasmic microtubules. Here, we report that spindle assembly checkpoint (SAC) components MAD-1, MAD-2, and BUB-3 are required to negatively regulate synapsis and promote the synapsis checkpoint response. Both of these roles are independent of a conserved component of the anaphase-promoting complex, indicating a unique role for these proteins in meiotic prophase. MAD-1 and MAD-2 localize to the periphery of meiotic nuclei and interact with SUN-1, suggesting a role at PCs. Consistent with this idea, MAD-1 and BUB-3 require full PC function to inhibit synapsis. We propose that SAC proteins monitor the stability of pairing, or tension, between homologues to regulate synapsis and elicit a checkpoint response.

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Patel, Maulik R., Emily K. Lehrman, Vivian Y. Poon, Justin G. Crump, Mei Zhen, Cornelia I. Bargmann, and Kang Shen. "Hierarchical assembly of presynaptic components in defined C. elegans synapses." Nature Neuroscience 9, no. 12 (November 19, 2006): 1488–98. http://dx.doi.org/10.1038/nn1806.

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Devigne, Alice, and Needhi Bhalla. "Mad1’s ability to interact with Mad2 is essential to regulate and monitor meiotic synapsis in C. elegans." PLOS Genetics 17, no. 11 (November 11, 2021): e1009598. http://dx.doi.org/10.1371/journal.pgen.1009598.

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Meiotic homolog synapsis is essential to ensure accurate segregation of chromosomes during meiosis. In C. elegans, proper regulation of synapsis and a checkpoint that monitors synapsis relies on the spindle checkpoint components, Mad1 and Mad2, and Pairing Centers (PCs), cis-acting loci that interact with the nuclear envelope to mobilize chromosomes within the nucleus. Here, we test what specific functions of Mad1 and Mad2 are required to regulate and monitor synapsis. We find that a mutation that prevents Mad1’s localization to the nuclear periphery abolishes the synapsis checkpoint but has no effect on Mad2’s localization to the nuclear periphery or synapsis. By contrast, a mutation that prevents Mad1’s interaction with Mad2 abolishes the synapsis checkpoint, delays synapsis and fails to localize Mad2 to the nuclear periphery. These data indicate that Mad1’s primary role in regulating synapsis is through control of Mad2 and that Mad2 can bind other factors at the nuclear periphery. We also tested whether Mad2’s ability to adopt a specific conformation associated with its activity during spindle checkpoint function is required for its role in meiosis. A mutation that prevents Mad2 from adopting its active conformer fails to localize to the nuclear periphery, abolishes the synapsis checkpoint and exhibits substantial defects in meiotic synapsis. Thus, Mad2, and its regulation by Mad1, is an important regulator of meiotic synapsis in C. elegans.

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Lascarez-Lagunas, Laura I., Esther Herruzo, Alla Grishok, Pedro A. San-Segundo, and Mónica P. Colaiácovo. "DOT-1.1-dependent H3K79 methylation promotes normal meiotic progression and meiotic checkpoint function in C. elegans." PLOS Genetics 16, no. 10 (October 26, 2020): e1009171. http://dx.doi.org/10.1371/journal.pgen.1009171.

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Epigenetic modifiers are emerging as important regulators of the genome. However, how they regulate specific processes during meiosis is not well understood. Methylation of H3K79 by the histone methyltransferase Dot1 has been shown to be involved in the maintenance of genomic stability in various organisms. In S. cerevisiae, Dot1 modulates the meiotic checkpoint response triggered by synapsis and/or recombination defects by promoting Hop1-dependent Mek1 activation and Hop1 distribution along unsynapsed meiotic chromosomes, at least in part, by regulating Pch2 localization. However, how this protein regulates meiosis in metazoans is unknown. Here, we describe the effects of H3K79me depletion via analysis of dot-1.1 or zfp-1 mutants during meiosis in Caenorhabditis elegans. We observed decreased fertility and increased embryonic lethality in dot-1.1 mutants suggesting meiotic dysfunction. We show that DOT-1.1 plays a role in the regulation of pairing, synapsis and recombination in the worm. Furthermore, we demonstrate that DOT-1.1 is an important regulator of mechanisms surveilling chromosome synapsis during meiosis. In sum, our results reveal that regulation of H3K79me plays an important role in coordinating events during meiosis in C. elegans.

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Kelly, William G., Christine E. Schaner, Abby F. Dernburg, Min-Ho Lee, Stuart K. Kim, Anne M. Villeneuve, and Valerie Reinke. "X-chromosome silencing in the germline of C. elegans." Development 129, no. 2 (January 15, 2002): 479–92. http://dx.doi.org/10.1242/dev.129.2.479.

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Germline maintenance in the nematode C. elegans requires global repressive mechanisms that involve chromatin organization. During meiosis, the X chromosome in both sexes exhibits a striking reduction of histone modifications that correlate with transcriptional activation when compared with the genome as a whole. The histone modification spectrum on the X chromosome corresponds with a lack of transcriptional competence, as measured by reporter transgene arrays. The X chromosome in XO males is structurally analogous to the sex body in mammals, contains a histone modification associated with heterochromatin in other species and is inactivated throughout meiosis. The synapsed X chromosomes in hermaphrodites also appear to be silenced in early meiosis, but genes on the X chromosome are detectably expressed at later stages of oocyte meiosis. Silencing of the sex chromosome during early meiosis is a conserved feature throughout the nematode phylum, and is not limited to hermaphroditic species.

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Wynne, David J., Ofer Rog, Peter M. Carlton, and Abby F. Dernburg. "Dynein-dependent processive chromosome motions promote homologous pairing in C. elegans meiosis." Journal of Cell Biology 196, no. 1 (January 9, 2012): 47–64. http://dx.doi.org/10.1083/jcb.201106022.

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Meiotic chromosome segregation requires homologue pairing, synapsis, and crossover recombination, which occur during meiotic prophase. Telomere-led chromosome motion has been observed or inferred to occur during this stage in diverse species, but its mechanism and function remain enigmatic. In Caenorhabditis elegans, special chromosome regions known as pairing centers (PCs), rather than telomeres, associate with the nuclear envelope (NE) and the microtubule cytoskeleton. In this paper, we investigate chromosome dynamics in living animals through high-resolution four-dimensional fluorescence imaging and quantitative motion analysis. We find that chromosome movement is constrained before meiosis. Upon prophase onset, constraints are relaxed, and PCs initiate saltatory, processive, dynein-dependent motions along the NE. These dramatic motions are dispensable for homologous pairing and continue until synapsis is completed. These observations are consistent with the idea that motions facilitate pairing by enhancing the search rate but that their primary function is to trigger synapsis. This quantitative analysis of chromosome dynamics in a living animal extends our understanding of the mechanisms governing faithful genome inheritance.

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Jantsch, Verena, Pawel Pasierbek, Michael M. Mueller, Dieter Schweizer, Michael Jantsch, and Josef Loidl. "Targeted Gene Knockout Reveals a Role in Meiotic Recombination for ZHP-3, a Zip3-Related Protein in Caenorhabditis elegans." Molecular and Cellular Biology 24, no. 18 (September 15, 2004): 7998–8006. http://dx.doi.org/10.1128/mcb.24.18.7998-8006.2004.

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ABSTRACT The meiotically expressed Zip3 protein is found conserved from Saccharomyces cerevisiae to humans. In baker's yeast, Zip3p has been implicated in synaptonemal complex (SC) formation, while little is known about the protein's function in multicellular organisms. We report here the successful targeted gene disruption of zhp-3 (K02B12.8), the ZIP3 homolog in the nematode Caenorhabditis elegans. Homozygous zhp-3 knockout worms show normal homologue pairing and SC formation. Also, the timing of appearance and the nuclear localization of the recombination protein Rad-51 seem normal in these animals, suggesting proper initiation of meiotic recombination by DNA double-strand breaks. However, the occurrence of univalents during diplotene indicates that C. elegans ZHP-3 protein is essential for reciprocal recombination between homologous chromosomes and thus chiasma formation. In the absence of ZHP-3, reciprocal recombination is abolished and double-strand breaks seem to be repaired via alternative pathways, leading to achiasmatic chromosomes and the occurrence of univalents during meiosis I. Green fluorescent protein-tagged C. elegans ZHP-3 forms lines between synapsed chromosomes and requires the SC for its proper localization.

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Ulicna, Livia, Jana Rohozkova, and Pavel Hozak. "Multiple Aspects of PIP2 Involvement in C. elegans Gametogenesis." International Journal of Molecular Sciences 19, no. 9 (September 10, 2018): 2679. http://dx.doi.org/10.3390/ijms19092679.

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One of the most studied phosphoinositides is phosphatidylinositol 4,5-bisphosphate (PIP2), which localizes to the plasma membrane, nuclear speckles, small foci in the nucleoplasm, and to the nucleolus in mammalian cells. Here, we show that PIP2 also localizes to the nucleus in prophase I, during the gametogenesis of C. elegans hermaphrodite. The depletion of PIP2 by type I PIP kinase (PPK-1) kinase RNA interference results in an altered chromosome structure and leads to various defects during meiotic progression. We observed a decreased brood size and aneuploidy in progeny, defects in synapsis, and crossover formation. The altered chromosome structure is reflected in the increased transcription activity of a tightly regulated process in prophase I. To elucidate the involvement of PIP2 in the processes during the C. elegans development, we identified the PIP2-binding partners, leucine-rich repeat (LRR-1) protein and proteasome subunit beta 4 (PBS-4), pointing to its involvement in the ubiquitin–proteasome pathway.

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DiLoreto, Chute, Bryce, and Srinivasan. "Novel Technological Advances in Functional Connectomics in C. elegans." Journal of Developmental Biology 7, no. 2 (April 23, 2019): 8. http://dx.doi.org/10.3390/jdb7020008.

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The complete structure and connectivity of the Caenorhabditis elegans nervous system (“mind of a worm”) was first published in 1986, representing a critical milestone in the field of connectomics. The reconstruction of the nervous system (connectome) at the level of synapses provided a unique perspective of understanding how behavior can be coded within the nervous system. The following decades have seen the development of technologies that help understand how neural activity patterns are connected to behavior and modulated by sensory input. Investigations on the developmental origins of the connectome highlight the importance of role of neuronal cell lineages in the final connectivity matrix of the nervous system. Computational modeling of neuronal dynamics not only helps reconstruct the biophysical properties of individual neurons but also allows for subsequent reconstruction of whole-organism neuronal network models. Hence, combining experimental datasets with theoretical modeling of neurons generates a better understanding of organismal behavior. This review discusses some recent technological advances used to analyze and perturb whole-organism neuronal function along with developments in computational modeling, which allows for interrogation of both local and global neural circuits, leading to different behaviors. Combining these approaches will shed light into how neural networks process sensory information to generate the appropriate behavioral output, providing a complete understanding of the worm nervous system.

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Rabinowitch, Ithai, Bishal Upadhyaya, Aaradhya Pant, Dolev Galski, Lena Kreines, and Jihong Bai. "Circumventing neural damage in a C. elegans chemosensory circuit using genetically engineered synapses." Cell Systems 12, no. 3 (March 2021): 263–71. http://dx.doi.org/10.1016/j.cels.2020.12.003.

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Tucker, Dana K., Chloe S. Adams, Gauri Prasad, and Brian D. Ackley. "The Immunoglobulin Superfamily Members syg-2 and syg-1 Regulate Neurite Development in C. elegans." Journal of Developmental Biology 10, no. 1 (January 9, 2022): 3. http://dx.doi.org/10.3390/jdb10010003.

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Neurons form elaborate networks by guiding axons and dendrites to appropriate destinations. Neurites require information about the relative body axes during the initial projection from the cell body, and failure to receive or interpret those cues correctly can result in outgrowth errors. We identified a mutation in the Ig superfamily member syg-2 in a screen for animals with anterior/posterior (A/P) axon guidance defects. We found that syg-2 and its cognate Ig family member syg-1 appear to function in a linear genetic pathway to control the outgrowth of GABAergic axons. We determined that this pathway works in parallel to Wnt signaling. Specifically, mutations in syg-2 or syg-1 selectively affected the embryonically derived Dorsal D-type (DD) GABAergic neurons. We found no evidence that these mutations affected the Ventral D-type neurons (VD) that form later, during the first larval stage. In addition, mutations in syg-1 or syg-2 could result in the DD neurons forming multiple processes, becoming bipolar, rather than the expected pseudounipolar morphology. Given SYG-2′s essential function in synaptogenesis of the hermaphrodite-specific neurons (HSNs), we also examined DD neuron synapses in syg-2 mutants. We found syg-2 mutants had a decreased number of synapses formed, but synaptic morphology was largely normal. These results provide further evidence that the GABAergic motorneurons use multiple guidance pathways during development.

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Singhvi, Aakanksha, and Shai Shaham. "Glia-Neuron Interactions in Caenorhabditis elegans." Annual Review of Neuroscience 42, no. 1 (July 8, 2019): 149–68. http://dx.doi.org/10.1146/annurev-neuro-070918-050314.

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Glia are abundant components of animal nervous systems. Recognized 170 years ago, concerted attempts to understand these cells began only recently. From these investigations glia, once considered passive filler material in the brain, have emerged as active players in neuron development and activity. Glia are essential for nervous system function, and their disruption leads to disease. The nematode Caenorhabditis elegans possesses glial types similar to vertebrate glia, based on molecular, morphological, and functional criteria, and has become a powerful model in which to study glia and their neuronal interactions. Facile genetic and transgenic methods in this animal allow the discovery of genes required for glial functions, and effects of glia at single synapses can be monitored by tracking neuron shape, physiology, or animal behavior. Here, we review recent progress in understanding glia-neuron interactions in C. elegans. We highlight similarities with glia in other animals, and suggest conserved emerging principles of glial function.

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Zheng, Zihui, Kanglu Wu, Qinli Ruan, Dongfang Li, Weizhen Liu, Min Wang, Yaoyao Li, Jintao Xia, Dongqing Yang, and Jun Guo. "Suppression of Selective Voltage-Gated Calcium Channels Alleviates Neuronal Degeneration and Dysfunction through Glutathione S-Transferase-Mediated Oxidative Stress Resistance in a Caenorhabditis elegans Model of Alzheimer’s Disease." Oxidative Medicine and Cellular Longevity 2022 (November 30, 2022): 1–19. http://dx.doi.org/10.1155/2022/8287633.

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Calcium homeostasis plays a vital role in protecting against Alzheimer’s disease (AD). In this study, amyloid-β (Aβ)-induced C. elegans models of AD were used to elucidate the mechanisms underlying calcium homeostasis in AD. Calcium acetate increased the intracellular calcium content, exacerbated Aβ1–42 aggregation, which is closely associated with oxidative stress, aggravated neuronal degeneration and dysfunction, and shortened the lifespan of the C. elegans models. Ethylene glycol tetraacetic acid (EGTA) and nimodipine were used to decrease the intracellular calcium content. Both EGTA and nimodipine showed remarkable inhibitory effects on Aβ1–42 aggregations by increasing oxidative stress resistance. Moreover, both compounds significantly delayed the onset of Aβ-induced paralysis, rescued memory deficits, ameliorated behavioral dysfunction, decreased the vulnerability of two major (GABAergic and dopaminergic) neurons and synapses, and extended the lifespan of the C. elegans AD models. Furthermore, RNA sequencing of nimodipine-treated worms revealed numerous downstream differentially expressed genes related to calcium signaling. Nimodipine-induced inhibition of selective voltage-gated calcium channels was shown to activate other calcium channels of the plasma membrane (clhm-1) and endoplasmic reticulum (unc-68), in addition to sodium-calcium exchanger channels (ncx-1). These channels collaborated to activate downstream events to resist oxidative stress through glutathione S-transferase activity mediated by HPGD and skn-1, as verified by RNA interference. These results may be applied for the treatment of Alzheimer’s disease.

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Chandra, Rashmi, Fatima Farah, Fernando Muñoz-Lobato, Anirudh Bokka, Kelli Benedetti, Fatema Saifuddin, Miri VanHoven, and Noelle L'Etoile. "SLEEP IS REQUIRED FOR ODOR EXPOSURE TO CONSOLIDATE MEMORY AND REMODEL OLFACTORY SYNAPSES." Innovation in Aging 6, Supplement_1 (November 1, 2022): 591. http://dx.doi.org/10.1093/geroni/igac059.2214.

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Abstract Olfactory dysfunction precedes dementia in several neurodegenerative disorders such as Alzheimer’s disease (AD) or Parkinson’s Disease (PD), and AD/PD are associated with progressive sleep abnormalities. However, how sleep affects cognitive performance remains unclear, perhaps due to the complexities of the human nervous system. Here we demonstrate that the transparent model organism C. elegans which has well defined neural connection sleeps after repeated odor trainings. This provides us with a platform to dissect how sleep affects memory at a synaptic resolution. We identified that sleep after training is required for the animal to retain a long-term memory of the odor. We found that if animals do not sleep in the first two hours after training, memory is not consolidated. After identifying the neurons that are required for the memory, we show that the sensory-interneuron connections within the circuit are downscaled after sleep. Therefore, we found a time-specific requirement of sleep that modulates synaptic downscaling to preserve memory. Conversely, lack of sleep post-training erases the long-term memory and destabilizes the synaptic downscaling, indicating that modulating the amount of sleep is sufficient to modulate memory. These results make C. elegans an excellent tool to ask what molecular mechanisms, cell biological processes and circuit level reorganizations are engaged during sleep to promote memory. This understanding will provide insights into the functions of sleep that affects cognitive performance in neurodegenerative diseases.

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McMullan, R. "Rho is a presynaptic activator of neurotransmitter release at pre-existing synapses in C. elegans." Genes & Development 20, no. 1 (January 1, 2006): 65–76. http://dx.doi.org/10.1101/gad.359706.

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Shen, Kang, and Cornelia I. Bargmann. "The Immunoglobulin Superfamily Protein SYG-1 Determines the Location of Specific Synapses in C. elegans." Cell 112, no. 5 (March 2003): 619–30. http://dx.doi.org/10.1016/s0092-8674(03)00113-2.

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Senti, Gabriele, and Peter Swoboda. "Distinct Isoforms of the RFX Transcription Factor DAF-19 Regulate Ciliogenesis and Maintenance of Synaptic Activity." Molecular Biology of the Cell 19, no. 12 (December 2008): 5517–28. http://dx.doi.org/10.1091/mbc.e08-04-0416.

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Neurons form elaborate subcellular structures such as dendrites, axons, cilia, and synapses to receive signals from their environment and to transmit them to the respective target cells. In the worm Caenorhabditis elegans, lack of the RFX transcription factor DAF-19 leads to the absence of cilia normally found on 60 sensory neurons. We now describe and functionally characterize three different isoforms of DAF-19. The short isoform DAF-19C is specifically expressed in ciliated sensory neurons and sufficient to rescue all cilia-related phenotypes of daf-19 mutants. In contrast, the long isoforms DAF-19A/B function in basically all nonciliated neurons. We discovered behavioral and cellular phenotypes in daf-19 mutants that depend on the isoforms daf-19a/b. These novel synaptic maintenance phenotypes are reminiscent of synaptic decline seen in many human neurodegenerative disorders. The C. elegans daf-19 mutant worms can thus serve as a molecular model for the mechanisms of functional neuronal decline.

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Jung, Nadja, Martin Wienisch, Mingyu Gu, James B. Rand, Sebastian L. Müller, Gerd Krause, Erik M. Jorgensen, Jürgen Klingauf, and Volker Haucke. "Molecular basis of synaptic vesicle cargo recognition by the endocytic sorting adaptor stonin 2." Journal of Cell Biology 179, no. 7 (December 31, 2007): 1497–510. http://dx.doi.org/10.1083/jcb.200708107.

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Synaptic transmission depends on clathrin-mediated recycling of synaptic vesicles (SVs). How select SV proteins are targeted for internalization has remained elusive. Stonins are evolutionarily conserved adaptors dedicated to endocytic sorting of the SV protein synaptotagmin. Our data identify the molecular determinants for recognition of synaptotagmin by stonin 2 or its Caenorhabditis elegans orthologue UNC-41B. The interaction involves the direct association of clusters of basic residues on the surface of the cytoplasmic domain of synaptotagmin 1 and a β strand within the μ–homology domain of stonin 2. Mutation of K783, Y784, and E785 to alanine within this stonin 2 β strand results in failure of the mutant stonin protein to associate with synaptotagmin, to accumulate at synapses, and to facilitate synaptotagmin internalization. Synaptotagmin-binding–defective UNC-41B is unable to rescue paralysis in C. elegans stonin mutant animals, suggesting that the mechanism of stonin-mediated SV cargo recognition is conserved from worms to mammals.

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Kohn, Rebecca Eustance, Janet S. Duerr, John R. McManus, Angie Duke, Terese L. Rakow, Hiroko Maruyama, Gary Moulder, Ichi N. Maruyama, Robert J. Barstead, and James B. Rand. "Expression of Multiple UNC-13 Proteins in theCaenorhabditis elegans Nervous System." Molecular Biology of the Cell 11, no. 10 (October 2000): 3441–52. http://dx.doi.org/10.1091/mbc.11.10.3441.

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The Caenorhabditis elegans UNC-13 protein and its mammalian homologues are important for normal neurotransmitter release. We have identified a set of transcripts from the unc-13locus in C. elegans resulting from alternative splicing and apparent alternative promoters. These transcripts encode proteins that are identical in their C-terminal regions but that vary in their N-terminal regions. The most abundant protein form is localized to most or all synapses. We have analyzed the sequence alterations, immunostaining patterns, and behavioral phenotypes of 31 independentunc-13 alleles. Many of these mutations are transcript-specific; their phenotypes suggest that the different UNC-13 forms have different cellular functions. We have also isolated a deletion allele that is predicted to disrupt all UNC-13 protein products; animals homozygous for this null allele are able to complete embryogenesis and hatch, but they die as paralyzed first-stage larvae. Transgenic expression of the entire gene rescues the behavior of mutants fully; transgenic overexpression of one of the transcripts can partially compensate for the genetic loss of another. This finding suggests some degree of functional overlap of the different protein products.

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Liu, Hanwenheng, Spencer G. Gordon, and Ofer Rog. "Heterologous synapsis in C. elegans is regulated by meiotic double-strand breaks and crossovers." Chromosoma 130, no. 4 (October 4, 2021): 237–50. http://dx.doi.org/10.1007/s00412-021-00763-y.

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MacQueen, A. J. "Synapsis-dependent and -independent mechanisms stabilize homolog pairing during meiotic prophase in C. elegans." Genes & Development 16, no. 18 (September 15, 2002): 2428–42. http://dx.doi.org/10.1101/gad.1011602.

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MacQueen, Amy J., Carolyn M. Phillips, Needhi Bhalla, Pinky Weiser, Anne M. Villeneuve, and Abby F. Dernburg. "Chromosome Sites Play Dual Roles to Establish Homologous Synapsis during Meiosis in C. elegans." Cell 123, no. 6 (December 2005): 1037–50. http://dx.doi.org/10.1016/j.cell.2005.09.034.

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Phillips, Carolyn M., Xiangdong Meng, Lei Zhang, Jacqueline H. Chretien, Fyodor D. Urnov, and Abby F. Dernburg. "Identification of chromosome sequence motifs that mediate meiotic pairing and synapsis in C. elegans." Nature Cell Biology 11, no. 8 (July 20, 2009): 934–42. http://dx.doi.org/10.1038/ncb1904.

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Dimitriadi, Maria, Aaron Derdowski, Geetika Kalloo, Melissa S. Maginnis, Patrick O’Hern, Bryn Bliska, Altar Sorkaç, et al. "Decreased function of survival motor neuron protein impairs endocytic pathways." Proceedings of the National Academy of Sciences 113, no. 30 (July 11, 2016): E4377—E4386. http://dx.doi.org/10.1073/pnas.1600015113.

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Spinal muscular atrophy (SMA) is caused by depletion of the ubiquitously expressed survival motor neuron (SMN) protein, with 1 in 40 Caucasians being heterozygous for a disease allele. SMN is critical for the assembly of numerous ribonucleoprotein complexes, yet it is still unclear how reduced SMN levels affect motor neuron function. Here, we examined the impact of SMN depletion in Caenorhabditis elegans and found that decreased function of the SMN ortholog SMN-1 perturbed endocytic pathways at motor neuron synapses and in other tissues. Diminished SMN-1 levels caused defects in C. elegans neuromuscular function, and smn-1 genetic interactions were consistent with an endocytic defect. Changes were observed in synaptic endocytic proteins when SMN-1 levels decreased. At the ultrastructural level, defects were observed in endosomal compartments, including significantly fewer docked synaptic vesicles. Finally, endocytosis-dependent infection by JC polyomavirus (JCPyV) was reduced in human cells with decreased SMN levels. Collectively, these results demonstrate for the first time, to our knowledge, that SMN depletion causes defects in endosomal trafficking that impair synaptic function, even in the absence of motor neuron cell death.

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Yan, Dong, Zilu Wu, Andrew D. Chisholm, and Yishi Jin. "The DLK-1 Kinase Promotes mRNA Stability and Local Translation in C. elegans Synapses and Axon Regeneration." Cell 138, no. 5 (September 2009): 1005–18. http://dx.doi.org/10.1016/j.cell.2009.06.023.

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Phillips, Carolyn M., Xiangdong Meng, Lei Zhang, Jacqueline H. Chretien, Fyodor D. Urnov, and Abby F. Dernburg. "Erratum: Identification of chromosome sequence motifs that mediate meiotic pairing and synapsis in C. elegans." Nature Cell Biology 11, no. 9 (September 2009): 1163. http://dx.doi.org/10.1038/ncb0909-1163.

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Mullen, Gregory P., Eleanor A. Mathews, Paurush Saxena, Stephen D. Fields, John R. McManus, Gary Moulder, Robert J. Barstead, Michael W. Quick, and James B. Rand. "The Caenorhabditis elegans snf-11 Gene Encodes a Sodium-dependent GABA Transporter Required for Clearance of Synaptic GABA." Molecular Biology of the Cell 17, no. 7 (July 2006): 3021–30. http://dx.doi.org/10.1091/mbc.e06-02-0155.

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Sodium-dependent neurotransmitter transporters participate in the clearance and/or recycling of neurotransmitters from synaptic clefts. The snf-11 gene in Caenorhabditis elegans encodes a protein of high similarity to mammalian GABA transporters (GATs). We show here that snf-11 encodes a functional GABA transporter; SNF-11–mediated GABA transport is Na+ and Cl− dependent, has an EC50 value of 168 μM, and is blocked by the GAT1 inhibitor SKF89976A. The SNF-11 protein is expressed in seven GABAergic neurons, several additional neurons in the head and retrovesicular ganglion, and three groups of muscle cells. Therefore, all GABAergic synapses are associated with either presynaptic or postsynaptic (or both) expression of SNF-11. Although a snf-11 null mutation has no obvious effects on GABAergic behaviors, it leads to resistance to inhibitors of acetylcholinesterase. In vivo, a snf-11 null mutation blocks GABA uptake in at least a subset of GABAergic cells; in a cell culture system, all GABA uptake is abolished by the snf-11 mutation. We conclude that GABA transport activity is not essential for normal GABAergic function in C. elegans and that the localization of SNF-11 is consistent with a GABA clearance function rather than recycling.

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Journal articles on the topic 'C. elegans synapse'

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