2012
DOI: 10.1073/pnas.1219987110
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MDGAs interact selectively with neuroligin-2 but not other neuroligins to regulate inhibitory synapse development

Abstract: The MAM domain-containing GPI anchor proteins MDGA1 and MDGA2 are Ig superfamily adhesion molecules composed of six IG domains, a fibronectin III domain, a MAM domain, and a GPI anchor. MDGAs contribute to the radial migration and positioning of a subset of cortical neurons during early neural development. However, MDGAs continue to be expressed in postnatal brain, and their functions during postnatal neural development remain unknown. Here, we demonstrate that MDGAs specifically and with a nanomolar affinity … Show more

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Cited by 118 publications
(174 citation statements)
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“…The psPAX and pMD2G plasmids encode the elements essential for packaging viral particles. HEK293T cell supernatants were harvested 48 h post transfection and purified 46 . Hippocampal neurons infected at DIV3 with control lentiviruses (shControl) or shRNA targeting PTPs (sh-PTPs) or co-infected with lentiviruses expressing PTPs shRNA plus the human shRNA-resistant PTPs splice variant with an MeB insert ( þ PTPs MeB þ ), or PTPs shRNA plus the human shRNAresistant PTPs splice variant without an MeB insert ( þ PTPs MeB À ).…”
Section: Methodsmentioning
confidence: 99%
“…The psPAX and pMD2G plasmids encode the elements essential for packaging viral particles. HEK293T cell supernatants were harvested 48 h post transfection and purified 46 . Hippocampal neurons infected at DIV3 with control lentiviruses (shControl) or shRNA targeting PTPs (sh-PTPs) or co-infected with lentiviruses expressing PTPs shRNA plus the human shRNA-resistant PTPs splice variant with an MeB insert ( þ PTPs MeB þ ), or PTPs shRNA plus the human shRNAresistant PTPs splice variant without an MeB insert ( þ PTPs MeB À ).…”
Section: Methodsmentioning
confidence: 99%
“…Furthermore, NLGN dimerization seems to be essential for its cell-surface function 66 and for instructing the differentiation of the presynaptic terminal 122 , providing another mechanism for regulating its interactions with synaptic scaffolding molecules. Recently, the MAM domain-containing GPI anchor proteins MDGA1 and MDGA2 (which are Ig superfamily adhesion molecules) were shown to selectively bind to NLGN2 and interfere with its synaptogenic activity 123,124 (FIG. 2D).…”
Section: Gephyrin and Gabaergic Synapse Formationmentioning
confidence: 99%
“…Super-resolution imaging has revealed the existence of distinct subsynaptic domains, where NL-2 and gephyrin are coupled to constitute one domain, whereas IgSF9 is indirectly linked to NL-2 via another domain. 105 It would be informative to use similar approaches to examine systematically the localization of other 'endogenous' inhibitory synapse proteins, such as collybistin, Slitrk3 and MDGA1 106 .…”
Section: Synaptic Functions Of Gephyrinmentioning
confidence: 99%