Neuroligin1: a cell adhesion molecule that recruits PSD-95 and NMDA receptors by distinct mechanisms during synaptogenes
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Neuroligin1: a cell adhesion molecule that recruits PSD-95 and NMDA receptors by distinct mechanisms during synaptogenesis Stephanie L Barrow et al.
Neural Development 2009, 4:17 http://www.neuraldevelopment.com/content/4/1/17
Neural Development
BioMed Central
Open Access
Research article
Neuroligin1: a cell adhesion molecule that recruits PSD-95 and NMDA receptors by distinct mechanisms during synaptogenesis Stephanie L Barrow1, John RL Constable2, Eliana Clark1, Faten El-Sabeawy1, A Kimberley McAllister†1 and Philip Washbourne*†2 Address: 1Center for Neuroscience, University of California Davis, 1544 Newton Ct, Davis, California 95616, USA and 2Institute of Neuroscience, University of Oregon, Eugene, Oregon 97403, USA Email: Stephanie L Barrow - [email protected]; John RL Constable - [email protected]; Eliana Clark - [email protected]; Faten El-Sabeawy - [email protected]; A Kimberley McAllister - [email protected]; Philip Washbourne* - [email protected] * Corresponding author †Equal contributors
Published: 18 May 2009 Neural Development 2009, 4:17
doi:10.1186/1749-8104-4-17
Received: 7 August 2008 Accepted: 18 May 2009
This article is available from: http://www.neuraldevelopment.com/content/4/1/17 © 2009 Barrow et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract Background: The cell adhesion molecule pair neuroligin1 (Nlg1) and -neurexin (-NRX) is a powerful inducer of postsynaptic differentiation of glutamatergic synapses in vitro. Because Nlg1 induces accumulation of two essential components of the postsynaptic density (PSD) – PSD-95 and NMDA receptors (NMDARs) – and can physically bind PSD-95 and NMDARs at mature synapses, it has been proposed that Nlg1 recruits NMDARs to synapses through its interaction with PSD-95. However, PSD-95 and NMDARs are recruited to nascent synapses independently and it is not known if Nlg1 accumulates at synapses before these PSD proteins. Here, we investigate how a single type of cell adhesion molecule can recruit multiple types of synaptic proteins to new synapses with distinct mechanisms and time courses. Results: Nlg1 was present in young cortical neurons in two distinct pools before synaptogenesis, diffuse and clustered. Time-lapse imaging revealed that the diffuse Nlg1 aggregated at, and the clustered Nlg1 moved to, sites of axodendritic contact with a rapid time course. Using a patching assay that artificially induced clusters of Nlg, the time course and mechanisms of recruitment of PSD-95 and NMDARs to those Nlg clusters were characterized. Patching Nlg induced clustering of PSD-95 via a slow palmitoylation-dependent step. In contrast, NMDARs directly associated with clusters of Nlg1 during trafficking. Nlg1 and NMD
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