• Analysis of the Potential Role of GluA4 Carboxyl-Terminus in PDZ Interactions

      Coleman, Sarah K.; Cai, Chunlin; Kalkkinen, Nisse; Korpi, Esa R.; Keinanen, Kari; Mei, Lin; Department of Neurology; College of Graduate Studies (2010-01-14)
      Background: Specific delivery to synapses of a-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptors with long-tailed subunits is believed to be a key event in many forms of activity-dependent changes in synaptic strength. GluA1, the best characterized long-tailed AMPA receptor subunit, contains a C-terminal class I PDZ binding motif, which mediates its interaction with scaffold and trafficking proteins, including synapse-associated protein 97 (SAP97). In GluA4, another long-tailed subunit implicated in synaptic plasticity, the PDZ motif is blocked by a single proline residue. This feature is highly conserved in vertebrates, whereas the closest invertebrate homologs of GluA4 have a canonical class I PDZ binding motif. In this work, we have examined the role of GluA4 in PDZ interactions