Figure 3
From: Amyloid precursor protein modulates Nav1.6 sodium channel currents through a Go-coupled JNK pathway
The effects of distinct APP intracellular domains on voltage-gated sodium channels.
(A) Schematic representation of APP (full-length APP695), APP intracellular domain (AICD50), APP C31 domain (C31), APP Go protein binding domain (GoBD), Fe65 binding domain (Fe65BD) and VTPEER peptides (Val667-Arg672). (B) Normalized current-voltage relationships of currents in oocytes expressing Nav1.6 α subunit and together with APP intracellular domain (AICD50; (a); closed circles), APP C31 domain (C31; (b); closed circles), APP Go protein binding domain (GoBD; (c); closed circles), Fe65 binding domain (Fe65BD; (d); closed circles), VTPEER peptide (VTPEER; (e); closed circles) and the reversed VTPEER sequence (reverse VTPEER; (f); closed circles). The oocytes expressing Nav1.6 α subunit alone were recorded as control (a–f; open squares). Insert: Representative examples of sodium current responses elicited by depolarizing voltage steps.
