Pinan-Lucarre B

References (5)

Title : The Ig-like domain of Punctin\/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1 - Platsaki_2020_J.Biol.Chem_295_16267
Author(s) : Platsaki S , Zhou X , Pinan-Lucarre B , Delauzun V , Tu H , Mansuelle P , Fourquet P , Bourne Y , Bessereau JL , Marchot P
Ref : Journal of Biological Chemistry , 295 :16267 , 2020
Abstract : Punctin/MADD-4, a member of the ADAMTSL extracellular matrix protein family, was identified as an anterograde synaptic organizer in the nematode Caenorhabditis elegans. At GABAergic neuromuscular junctions, the short isoform MADD-4B binds the ectodomain of neuroligin NLG-1, itself a postsynaptic organizer of inhibitory synapses. To identify the molecular bases of their partnership, we generated recombinant forms of the two proteins and carried out a comprehensive biochemical and biophysical study of their interaction, complemented by an in vivo localization study. We show that spontaneous proteolysis of MADD-4B first generates a shorter N-MADD-4B form, which comprises four thrombospondin (TSP) domains and one Ig-like domain and binds NLG-1. A second processing event eliminates the C-terminal Ig-like domain along with the ability of N-MADD-4B to bind NLG-1. These data identify the Ig-like domain as the primary determinant for N-MADD-4B interaction with NLG-1 in vitro We further demonstrate in vivo that this Ig-like domain is essential, albeit not sufficient per se, for efficient recruitment of GABA(A) receptors at GABAergic synapses in C. elegans The interaction of N-MADD-4B with NLG-1 is also disrupted by heparin, used as a surrogate for the extracellular matrix component, heparan sulfate. High-affinity binding of heparin/heparan sulfate to the Ig-like domain may proceed from surface charge complementarity, as suggested by homology three-dimensional modeling. These data point to N-MADD-4B processing and cell-surface proteoglycan binding as two possible mechanisms to regulate the interaction between MADD-4B and NLG-1 at GABAergic synapses.
ESTHER : Platsaki_2020_J.Biol.Chem_295_16267
PubMedSearch : Platsaki_2020_J.Biol.Chem_295_16267
PubMedID: 32928959

Title : The netrin receptor UNC-40\/DCC assembles a postsynaptic scaffold and sets the synaptic content of GABAA receptors - Zhou_2020_Nat.Commun_11_2674
Author(s) : Zhou X , Gueydan M , Jospin M , Ji T , Valfort A , Pinan-Lucarre B , Bessereau JL
Ref : Nat Commun , 11 :2674 , 2020
Abstract : Increasing evidence indicates that guidance molecules used during development for cellular and axonal navigation also play roles in synapse maturation and homeostasis. In C. elegans the netrin receptor UNC-40/DCC controls the growth of dendritic-like muscle cell extensions towards motoneurons and is required to recruit type A GABA receptors (GABAARs) at inhibitory neuromuscular junctions. Here we show that activation of UNC-40 assembles an intracellular synaptic scaffold by physically interacting with FRM-3, a FERM protein orthologous to FARP1/2. FRM-3 then recruits LIN-2, the ortholog of CASK, that binds the synaptic adhesion molecule NLG-1/Neuroligin and physically connects GABAARs to prepositioned NLG-1 clusters. These processes are orchestrated by the synaptic organizer CePunctin/MADD-4, which controls the localization of GABAARs by positioning NLG-1/neuroligin at synapses and regulates the synaptic content of GABAARs through the UNC-40-dependent intracellular scaffold. Since DCC is detected at GABA synapses in mammals, DCC might also tune inhibitory neurotransmission in the mammalian brain.
ESTHER : Zhou_2020_Nat.Commun_11_2674
PubMedSearch : Zhou_2020_Nat.Commun_11_2674
PubMedID: 32471987

Title : C. elegans Punctin Clusters GABA Receptors via Neuroligin Binding and UNC-40\/DCC Recruitment - Tu_2015_Neuron_86_1407
Author(s) : Tu H , Pinan-Lucarre B , Ji T , Jospin M , Bessereau JL
Ref : Neuron , 86 :1407 , 2015
Abstract : Positioning type A GABA receptors (GABAARs) in front of GABA release sites sets the strength of inhibitory synapses. The evolutionarily conserved Ce-Punctin/MADD-4 is an anterograde synaptic organizer that specifies GABAergic versus cholinergic identity of postsynaptic domains at the C. elegans neuromuscular junctions (NMJs). Here we show that the Ce-Punctin secreted by GABAergic motor neurons controls the clustering of GABAARs through the synaptic adhesion molecule neuroligin (NLG-1) and the netrin receptor UNC-40/DCC. The short isoform of Ce-Punctin binds and clusters NLG-1 postsynaptically at GABAergic NMJs. NLG-1 disruption causes a strong reduction of GABAAR content at GABAergic synapses. Ce-Punctin also binds and localizes UNC-40 receptors in the postsynaptic membrane of NMJs, which promotes the recruitment of GABAARs by NLG-1. Since the mammalian orthologs of these genes are expressed in the central nervous system and their mutations are implicated in neuropsychiatric diseases, this molecular pathway might have been evolutionarily conserved.
ESTHER : Tu_2015_Neuron_86_1407
PubMedSearch : Tu_2015_Neuron_86_1407
PubMedID: 26028575
Gene_locus related to this paper: caeel-NLGN1

Title : C. elegans Punctin specifies cholinergic versus GABAergic identity of postsynaptic domains - Pinan-Lucarre_2014_Nature_511_466
Author(s) : Pinan-Lucarre B , Tu H , Pierron M , Cruceyra PI , Zhan H , Stigloher C , Richmond JE , Bessereau JL
Ref : Nature , 511 :466 , 2014
Abstract : Because most neurons receive thousands of synaptic inputs, the neuronal membrane is a mosaic of specialized microdomains where neurotransmitter receptors cluster in register with the corresponding presynaptic neurotransmitter release sites. In many cases the coordinated differentiation of presynaptic and postsynaptic domains implicates trans-synaptic interactions between membrane-associated proteins such as neurexins and neuroligins. The Caenorhabditis elegans neuromuscular junction (NMJ) provides a genetically tractable system in which to analyse the segregation of neurotransmitter receptors, because muscle cells receive excitatory innervation from cholinergic neurons and inhibitory innervation from GABAergic neurons. Here we show that Ce-Punctin/madd-4 (ref. 5), the C. elegans orthologue of mammalian punctin-1 and punctin-2, encodes neurally secreted isoforms that specify the excitatory or inhibitory identity of postsynaptic NMJ domains. These proteins belong to the ADAMTS (a disintegrin and metalloprotease with thrombospondin repeats)-like family, a class of extracellular matrix proteins related to the ADAM proteases but devoid of proteolytic activity. Ce-Punctin deletion causes the redistribution of synaptic acetylcholine and GABAA (gamma-aminobutyric acid type A) receptors into extrasynaptic clusters, whereas neuronal presynaptic boutons remain unaltered. Alternative promoters generate different Ce-Punctin isoforms with distinct functions. A short isoform is expressed by cholinergic and GABAergic motoneurons and localizes to excitatory and inhibitory NMJs, whereas long isoforms are expressed exclusively by cholinergic motoneurons and are confined to cholinergic NMJs. The differential expression of these isoforms controls the congruence between presynaptic and postsynaptic domains: specific disruption of the short isoform relocalizes GABAA receptors from GABAergic to cholinergic synapses, whereas expression of a long isoform in GABAergic neurons recruits acetylcholine receptors to GABAergic NMJs. These results identify Ce-Punctin as a previously unknown synaptic organizer and show that presynaptic and postsynaptic domain identities can be genetically uncoupled in vivo. Because human punctin-2 was identified as a candidate gene for schizophrenia, ADAMTS-like proteins may also control synapse organization in the mammalian central nervous system.
ESTHER : Pinan-Lucarre_2014_Nature_511_466
PubMedSearch : Pinan-Lucarre_2014_Nature_511_466
PubMedID: 24896188
Gene_locus related to this paper: caeel-NLGN1

Title : The genome sequence of the model ascomycete fungus Podospora anserina - Espagne_2008_Genome.Biol_9_R77
Author(s) : Espagne E , Lespinet O , Malagnac F , Da Silva C , Jaillon O , Porcel BM , Couloux A , Aury JM , Segurens B , Poulain J , Anthouard V , Grossetete S , Khalili H , Coppin E , Dequard-Chablat M , Picard M , Contamine V , Arnaise S , Bourdais A , Berteaux-Lecellier V , Gautheret D , de Vries RP , Battaglia E , Coutinho PM , Danchin EG , Henrissat B , Khoury RE , Sainsard-Chanet A , Boivin A , Pinan-Lucarre B , Sellem CH , Debuchy R , Wincker P , Weissenbach J , Silar P
Ref : Genome Biol , 9 :R77 , 2008
Abstract : BACKGROUND: The dung-inhabiting ascomycete fungus Podospora anserina is a model used to study various aspects of eukaryotic and fungal biology, such as ageing, prions and sexual development. RESULTS: We present a 10X draft sequence of P. anserina genome, linked to the sequences of a large expressed sequence tag collection. Similar to higher eukaryotes, the P. anserina transcription/splicing machinery generates numerous non-conventional transcripts. Comparison of the P. anserina genome and orthologous gene set with the one of its close relatives, Neurospora crassa, shows that synteny is poorly conserved, the main result of evolution being gene shuffling in the same chromosome. The P. anserina genome contains fewer repeated sequences and has evolved new genes by duplication since its separation from N. crassa, despite the presence of the repeat induced point mutation mechanism that mutates duplicated sequences. We also provide evidence that frequent gene loss took place in the lineages leading to P. anserina and N. crassa. P. anserina contains a large and highly specialized set of genes involved in utilization of natural carbon sources commonly found in its natural biotope. It includes genes potentially involved in lignin degradation and efficient cellulose breakdown. CONCLUSION: The features of the P. anserina genome indicate a highly dynamic evolution since the divergence of P. anserina and N. crassa, leading to the ability of the former to use specific complex carbon sources that match its needs in its natural biotope.
ESTHER : Espagne_2008_Genome.Biol_9_R77
PubMedSearch : Espagne_2008_Genome.Biol_9_R77
PubMedID: 18460219
Gene_locus related to this paper: podan-b2a8u1 , podan-b2a9c4 , podan-b2a9k6 , podan-b2aa90 , podan-b2ab33 , podan-b2abs0 , podan-b2ac17 , podan-b2ack2 , podan-b2ad07 , podan-b2adj6 , podan-b2adk0 , podan-b2ae59 , podan-b2aee7 , podan-b2af51 , podan-b2afn5 , podan-b2afu6 , podan-b2akq7 , podan-b2aly0 , podan-b2am11 , podan-b2an24 , podan-b2ank1 , podan-b2apa8 , podan-b2api8 , podan-b2apj6 , podan-b2arl9 , podan-b2arz7 , podan-b2ase4 , podan-b2atn0 , podan-b2au46 , podan-b2aun9 , podan-b2av47 , podan-b2ava6 , podan-b2avm3 , podan-b2avu5 , podan-b2avx3 , podan-b2awk8 , podan-b2axk2 , podan-b2axz2 , podan-b2b1p7 , podan-b2b5e4 , podan-b2b6n7 , podan-b2b069 , podan-b2b073 , podan-b2b395 , podan-dapb , podan-b2afr0 , podan-b2a9k8 , podan-b2atb3 , podan-b2aca3 , podan-b2arv3 , podan-b2ank5 , podan-b2ax54 , podan-b2ad56 , podan-b2anm1 , podan-b2aya1 , podan-b2b164 , podan-a0a090d4h4 , podan-a0a090ccl8 , podan-b2b5p4 , podan-b2azp1 , podan-b2af75 , podan-b2alm5 , podan-b2ass5 , podan-b2aez8 , podan-kex1 , podan-cbpya