Role of TARP interaction in S-SCAM-mediated regulation of AMPA receptors. Channels (Austin) 2012;6(5):393-7
Date
08/11/2012Pubmed ID
22878254Pubmed Central ID
PMC3508780DOI
10.4161/chan.21301Scopus ID
2-s2.0-84878175337 (requires institutional sign-in at Scopus site) 8 CitationsAbstract
Scaffolding proteins are involved in the incorporation, anchoring, maintenance, and removal of AMPA receptors (AMPARs) at synapses, either through a direct interaction with AMPARs or via indirect association through auxiliary subunits of transmembrane AMPAR regulatory proteins (TARPs). Synaptic scaffolding molecule (S-SCAM) is a newly characterized member of the scaffolding proteins critical for the regulation and maintenance of AMPAR levels at synapses, and directly binds to TARPs through a PDZ interaction. However, the functional significance of S-SCAM-TARP interaction in the regulation of AMPARs has not been tested. Here we show that overexpression of the C-terminal peptide of TARP-γ2 fused to EGFP abolished the S-SCAM-mediated enhancement of surface GluA2 expression. Conversely, the deletion of the PDZ-5 domain of S-SCAM that binds TARPs greatly attenuated the S-SCAM-induced increase of surface GluA2 expression. In contrast, the deletion of the guanylate kinase domain of S-SCAM did not show a significant effect on the regulation of AMPARs. Together, these results suggest that S-SCAM is regulating AMPARs through TARPs.
Author List
Danielson E, Metallo J, Lee SHAuthor
Sang H. Lee PhD Professor in the Pharmacology and Toxicology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Adaptor Proteins, Signal TransducingAmino Acid Sequence
Animals
Calcium Channels
Cells, Cultured
Guanylate Kinases
Hippocampus
PDZ Domains
Rats
Receptors, AMPA
