The role of NG2-LNS-domain-mediated glia-to-neuron signaling in neuronal synapse formation and function
Final Report Abstract
The overriding aim of the planned study was to reveal the molecular mechanism of the novel oligodendrocyte precursor cell (OPC)-based modulation of neuronal synaptic function by the OPC proteoglycan NG2 (Sakry et al. PLoS Biol. 2014), and to determine how the NG2 LNS domains function as modulators of defined neuronal synapses and networks. The potential interaction partner of the NG2 LNS domains, CD166, failed to show an interaction in brain lysates, in contrast to the effects in cell culture. Analysis of the previously generated proteomics data (NG2-immunoprecipitation from brain lysates) also failed to yield new partners for the NG2 LNS domains, as did binding assays under a range of detergent conditions to other classical synaptic partners. Neuronal glutamate receptor trafficking was not altered in the presence of NG2-Laminin Neurexin Sex Hormone Binding Globulin (LNS) Peptide. However, electrophysiological studies of autaptic cultures of neurones showed alterations in the presence of the LNS peptide. Further electrophysiological studies are needed to clarify these effects and integrate them with the published results observed in studies of the NG2 knockout mouse.
Publications
- (2018) The Intracellular Cleavage Product of the NG2 Proteoglycan Modulates Translation and Cell-Cycle Kinetics via Effects on mTORC1/FMRP Signaling. Front Cell Neurosci. 7;12:231
Nayak T, Trotter J, Sakry D
(See online at https://doi.org/10.3389/fncel.2018.00231)
