The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1

Platsaki, Semeli; Zhou, Xin J.; Pinan‐Lucarré, Bérangère; Delauzun, Vincent; Tu, Haijun; Mansuelle, Pascal; Fourquet, Patrick; Bourne, Yves; Bessereau, Jean-Louis; Marchot, Pierre

doi:10.1074/jbc.ra120.014591

Cited by 13 publications

(8 citation statements)

References 65 publications

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“…HSs form long, highly negatively charged molecules able to engage versatile electrostatic interactions ( Xu and Esko, 2014 ). Punctin is a good candidate for synaptic stabilization of SDN-1 through HS interaction, because it contains an immunoglobulin-like domain with a predicted highly electropositive surface pocket, which we demonstrated to bind heparin in vitro ( Platsaki et al, 2020 ). SDN-1 is the first identified component able to regulate the amount of Punctin.…”

Section: Discussionmentioning

confidence: 95%

The HSPG syndecan is a core organizer of cholinergic synapses

Zhou

Vachon

Cizeron

et al. 2021

Journal of Cell Biology

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The extracellular matrix has emerged as an active component of chemical synapses regulating synaptic formation, maintenance, and homeostasis. The heparan sulfate proteoglycan (HSPG) syndecans are known to regulate cellular and axonal migration in the brain. They are also enriched at synapses, but their synaptic functions remain more elusive. Here, we show that SDN-1, the sole orthologue of syndecan in C. elegans, is absolutely required for the synaptic clustering of homomeric α7-like acetylcholine receptors (AChRs) and regulates the synaptic content of heteromeric AChRs. SDN-1 is concentrated at neuromuscular junctions (NMJs) by the neurally secreted synaptic organizer Ce-Punctin/MADD-4, which also activates the transmembrane netrin receptor DCC. Those cooperatively recruit the FARP and CASK orthologues that localize α7-like-AChRs at cholinergic NMJs through physical interactions. Therefore, SDN-1 stands at the core of the cholinergic synapse organization by bridging the extracellular synaptic determinants to the intracellular synaptic scaffold that controls the postsynaptic receptor content.

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Section: Discussionmentioning

confidence: 95%

The HSPG syndecan is a core organizer of cholinergic synapses

Zhou

Vachon

Cizeron

et al. 2021

Journal of Cell Biology

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“…The IG-like domain is probably the most widespread in animals and involves binding functions 23 . In C. elegans , the IG-like domain plays a key role for MADD-4 interaction with NLG-1, which is believed to interact with the presynaptic neurexin protein to mediate heterophilic adhesion 21 , 24 . These reports imply that Bxy-MADD-4 may play an important role in cell proliferation, tissue expansion, and the synaptic junction of B. xylophilus .…”

Section: Discussionmentioning

confidence: 99%

madd-4 plays a critical role in light against Bursaphelenchus xylophilus

Zhou

Sheng

Zhang

et al. 2022

Sci Rep

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Bursaphelenchus xylophilus is a notorious invasive species, causing extensive losses to pine ecosystems globally. Previous studies had shown that the development of B. xylophilus was seriously suppressed by light. However, the mechanism involved in the inhibition is unknown. Here, it is the first report that Bxy-madd-4 is a light-regulated gene, plays a potential role in B. xylophilus in responding to the blue light. Transcriptome sequencing revealed that the expression level of Bxy-madd-4 declined by 86.39% under blue light. The reverse transcription quantitative real-time PCR results were in accord with the transcriptome sequencing, confirming the expression level of Bxy-madd-4 was suppressed by blue light. Bxy-madd-4 promoter::mCherry reporter constructed in Caenorhabditis elegans were utilized to mimic the spatiotemporal expression patterns of Bxy-madd-4. Bxy-madd-4A promoter activity had a strong continuity throughout all development stages in C. elegans. Further RNA interference indicated that only 36.8% of the Bxy-madd-4 dsRNA treated embryos were hatched. Moreover, 71.6% of the hatched nematodes were abnormal, such as particles on the body surface and concave tissues. Our findings contribute towards a better understanding of the mechanism of light against the destructive invasive nematode, providing a promising hint for control of the destructive invasive nematode.

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“…MADD is an enzyme encoded by the MADD gene. The Ig-like domain of MADD is the primary determinant for N-MADD-4B interactions with NLG-1 in vitro ( Platsaki et al, 2020 ). At GABAergic neuromuscular junctions, the short isoform MADD-4B binds the ectodomain of neuroligin (NLG-1), which is also a postsynaptic organizer of inhibitory synapses ( Tu et al, 2015 ).…”

Section: Developmental Animal Models Used To Examine Neural Development and Regulation In A Whole Organism Environmentmentioning

confidence: 99%

Neural Tissue Homeostasis and Repair Is Regulated via CS and DS Proteoglycan Motifs

Hayes

Melrose

2021

Front. Cell Dev. Biol.

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Chondroitin sulfate (CS) is the most abundant and widely distributed glycosaminoglycan (GAG) in the human body. As a component of proteoglycans (PGs) it has numerous roles in matrix stabilization and cellular regulation. This chapter highlights the roles of CS and CS-PGs in the central and peripheral nervous systems (CNS/PNS). CS has specific cell regulatory roles that control tissue function and homeostasis. The CNS/PNS contains a diverse range of CS-PGs which direct the development of embryonic neural axonal networks, and the responses of neural cell populations in mature tissues to traumatic injury. Following brain trauma and spinal cord injury, a stabilizing CS-PG-rich scar tissue is laid down at the defect site to protect neural tissues, which are amongst the softest tissues of the human body. Unfortunately, the CS concentrated in gliotic scars also inhibits neural outgrowth and functional recovery. CS has well known inhibitory properties over neural behavior, and animal models of CNS/PNS injury have demonstrated that selective degradation of CS using chondroitinase improves neuronal functional recovery. CS-PGs are present diffusely in the CNS but also form denser regions of extracellular matrix termed perineuronal nets which surround neurons. Hyaluronan is immobilized in hyalectan CS-PG aggregates in these perineural structures, which provide neural protection, synapse, and neural plasticity, and have roles in memory and cognitive learning. Despite the generally inhibitory cues delivered by CS-A and CS-C, some CS-PGs containing highly charged CS disaccharides (CS-D, CS-E) or dermatan sulfate (DS) disaccharides that promote neural outgrowth and functional recovery. CS/DS thus has varied cell regulatory properties and structural ECM supportive roles in the CNS/PNS depending on the glycoform present and its location in tissue niches and specific cellular contexts. Studies on the fruit fly, Drosophila melanogaster and the nematode Caenorhabditis elegans have provided insightful information on neural interconnectivity and the role of the ECM and its PGs in neural development and in tissue morphogenesis in a whole organism environment.

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The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1

Cited by 13 publications

References 65 publications

The HSPG syndecan is a core organizer of cholinergic synapses

The HSPG syndecan is a core organizer of cholinergic synapses

madd-4 plays a critical role in light against Bursaphelenchus xylophilus

Neural Tissue Homeostasis and Repair Is Regulated via CS and DS Proteoglycan Motifs

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