Differences in AMPA and kainate receptor interactomes facilitate identification of AMPA receptor auxiliary subunit GSG1L.

Shanks NF, Savas JN, Maruo T, Cais O, Hirao A, Oe S, Ghosh A, Noda Y, Greger IH, Yates JR, Nakagawa T
Cell Rep. 2012 1 (6): 590-8

PMID: 22813734 · PMCID: PMC3401968 · DOI:10.1016/j.celrep.2012.05.004

AMPA receptor (AMPA-R) complexes consist of channel-forming subunits, GluA1-4, and auxiliary proteins, including TARPs, CNIHs, synDIG1, and CKAMP44, which can modulate AMPA-R function in specific ways. The combinatorial effects of four GluA subunits binding to various auxiliary subunits amplify the functional diversity of AMPA-Rs. The significance and magnitude of molecular diversity, however, remain elusive. To gain insight into the molecular complexity of AMPA and kainate receptors, we compared the proteins that copurify with each receptor type in the rat brain. This interactome study identified the majority of known interacting proteins and, more importantly, provides candidates for additional studies. We validate the claudin homolog GSG1L as a newly identified binding protein and unique modulator of AMPA-R gating, as determined by detailed molecular, cellular, electrophysiological, and biochemical experiments. GSG1L extends the functional variety of AMPA-R complexes, and further investigation of other candidates may reveal additional complexity of ionotropic glutamate receptor function.

Copyright © 2012 The Authors. Published by Elsevier Inc. All rights reserved.

MeSH Terms (19)

Amino Acid Sequence Animals Brain Claudins HEK293 Cells Humans Male Mass Spectrometry Molecular Sequence Data Neurons Protein Binding Protein Interaction Maps Proteins Protein Subunits Protein Transport Rats Receptors, AMPA Receptors, Kainic Acid Sequence Homology, Amino Acid

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