Differences in AMPA and Kainate Receptor Interactomes Facilitate Identification of AMPA Receptor Auxiliary Subunit GSG1L
Autor: | Ondrej Cais, Souichi Oe, Natalie F. Shanks, Yasuko Noda, Tomohiko Maruo, Ingo H. Greger, John R. Yates, Atsushi Hirao, Terunaga Nakagawa, Anirvan Ghosh, Jeffrey N. Savas |
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Rok vydání: | 2012 |
Předmět: |
Male
Protein subunit Molecular Sequence Data Kainate receptor Gating AMPA receptor Biology Interactome Mass Spectrometry Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences 0302 clinical medicine Receptors Kainic Acid Animals Humans Amino Acid Sequence Protein Interaction Maps Receptors AMPA Claudin lcsh:QH301-705.5 030304 developmental biology Neurons 0303 health sciences Sequence Homology Amino Acid Brain Proteins Rats Cell biology Protein Subunits Protein Transport HEK293 Cells lcsh:Biology (General) nervous system Biochemistry Claudins Ionotropic glutamate receptor 030217 neurology & neurosurgery Function (biology) Protein Binding |
Zdroj: | Cell Reports, Vol 1, Iss 6, Pp 590-598 (2012) |
ISSN: | 2211-1247 |
DOI: | 10.1016/j.celrep.2012.05.004 |
Popis: | SummaryAMPA 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. |
Databáze: | OpenAIRE |
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