The C-terminal domains of TARPs: Unexpectedly versatile domains

• DOI: 10.4161/chan.4.3.11349
• Publication Date: 2010-05-25T16:04:09Z
• Authors: Charlotte Sager; Daniel Tapken; Michael Hollmann
• Keywords: 0301 basic medicine; Protein Subunits; Protein Transport; 0303 health sciences; 03 medical and health sciences; Humans; Amino Acid Sequence; Receptors, AMPA; Ligand-Gated Ion Channels; Protein Structure, Tertiary

AMPA receptors mediate the majority of fast synaptic transmission in central nervous system and are therefore among most intensively studied ligand-gated ion channels over last decades. However, recent discovery that native receptor complexes contain auxiliary subunits classified as transmembrane regulatory proteins (TARPs) was quite a surprise dramatically changed field research. TARPs regulate trafficking well localization receptors, alter their pharmacological biophysical properties, generally resulting strongly elevated receptor-mediated currents. Thus, association with increases heterogeneity diversity postsynaptic In this regard, unravelling mechanisms by which modulate function is an intriguing challenge. Studying functional importance carboxy-terminal domain (CTD) for modulation, we found increased mediated two γ2 γ3 attributable to CTDs. Furthermore, demonstrated CTD additionally determines differences between regarding modulation function. As case point, showed unique role γ4, suggesting via individual mechanisms.