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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hong, Xiaoqi Avetisyan, Mariam Ronilo, Mason Standley, Steve |
| Description | Author Affiliation: Hong X ( Graduate College of Biomedical Sciences, Western University of Health Sciences, 701 E. Second Street, Pomona, CA 91766, USA.); Avetisyan M ( Graduate College of Biomedical Sciences, Western University of Health Sciences, 701 E. Second Street, Pomona, CA 91766, USA.); Ronilo M ( Graduate College of Biomedical Sciences, Western University of Health Sciences, 701 E. Second Street, Pomona, CA 91766, USA.); Standley S ( Graduate College of Biomedical Sciences, Western University of Health Sciences, 701 E. Second Street, Pomona, CA 91766, USA. Electronic address: sstandley@westernu.edu.) |
| Abstract | 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. While other domains of SAP97 were involved in forward trafficking of GluN1-3 out of the ER, the SH3 domain was necessary and sufficient to block the ER retention. This is the first direct evidence for the masking of ER-retention signals by PDZ domain-containing proteins, and provides detailed underlying mechanistic requirements. Such a mechanism could be central to modulating the ER exit of receptors into local, non-conventional or conventional, secretory pathways in neurons. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 2 |
| Volume Number | 1853 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-02-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Adaptor Proteins, Signal Transducing Metabolism Endoplasmic Reticulum Membrane Proteins Protein Subunits Receptors, N-Methyl-D-Aspartate Chemistry Retinoid X Receptors Src Homology Domains Amino Acid Sequence Animals COS Cells Cell Membrane Cercopithecus Aethiops Green Fluorescent Proteins HeLa Cells Models, Biological Molecular Sequence Data Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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