Publications by authors named "Mason Ronilo"
A novel function for the ER retention signals in the C-terminus of kainate receptor subunit, GluK5.
Biochim Biophys Acta Mol Cell Res
March 2019
Article Synopsis
- The study investigates the role of endoplasmic reticulum (ER) retention signals in the GluK5 protein, which is part of kainate receptors, emphasizing that these signals require the protein to assemble with others before exiting the ER.
- GluK5 contains two ER retention signals in its C-terminus, and while it associates with GluK2, this association does not prevent GluK5 from being retained in the ER.
- The retention signals are instead blocked by the proteins SAP97 and CASK, which help facilitate the sorting of GluK5 for transport to local dendritic secretory pathways in neurons, highlighting a new role for ER retention signals in neuronal protein trafficking.
SAP97 blocks the RXR ER retention signal of NMDA receptor subunit GluN1-3 through its SH3 domain.
Biochim Biophys Acta
February 2015
SAP97 is directly involved in exporting NMDA receptors with a specific subunit composition from the endoplasmic reticulum (ER). Characterization of the interactions between SAP97 and an NMDA receptor splice variant, GluN1-3, and of the effects on forward trafficking revealed that an ER-level interaction blocked the RXR ER-retention motif in the GluN1-3 cytoplasmic C-terminus in the context of both reporter molecules and full-length receptors. Binding of SAP97 to the PDZ-binding domain of GluN1-3 was required, but the blockade of ER-retention was mediated by the SH3-GuK domains coupled with the action of the N-terminus of SAP97.
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