TY - JOUR
T1 - Coxsackievirus and adenovirus receptor (CAR) mediates trafficking of acid sensing ion channel 3 (ASIC3) via PSD-95
AU - Excoffon, Katherine J.D.A.
AU - Kolawole, Abimbola O.
AU - Kusama, Nobuyoshi
AU - Gansemer, Nicholas D.
AU - Sharma, Priyanka
AU - Hruska-Hageman, Alesia M.
AU - Petroff, Elena
AU - Benson, Christopher J.
PY - 2012/8/17
Y1 - 2012/8/17
N2 - We have previously shown that the Coxsackievirus and adenovirus receptor (CAR) can interact with post-synaptic density 95 (PSD-95) and localize PSD-95 to cell-cell junctions. We have also shown that activity of the acid sensing ion channel (ASIC3), a H+-gated cation channel that plays a role in mechanosensation and pain signaling, is negatively modulated by PSD-95 through a PDZ-based interaction. We asked whether CAR and ASIC3 simultaneously interact with PSD-95, and if so, whether co-expression of these proteins alters their cellular distribution and localization. Results indicate that CAR and ASIC3 co-immunoprecipitate only when co-expressed with PSD-95. CAR also brings both PSD-95 and ASIC3 to the junctions of heterologous cells. Moreover, CAR rescues PSD-95-mediated inhibition of ASIC3 currents. These data suggest that, in addition to activity as a viral receptor and adhesion molecule, CAR can play a role in trafficking proteins, including ion channels, in a PDZ-based scaffolding complex.
AB - We have previously shown that the Coxsackievirus and adenovirus receptor (CAR) can interact with post-synaptic density 95 (PSD-95) and localize PSD-95 to cell-cell junctions. We have also shown that activity of the acid sensing ion channel (ASIC3), a H+-gated cation channel that plays a role in mechanosensation and pain signaling, is negatively modulated by PSD-95 through a PDZ-based interaction. We asked whether CAR and ASIC3 simultaneously interact with PSD-95, and if so, whether co-expression of these proteins alters their cellular distribution and localization. Results indicate that CAR and ASIC3 co-immunoprecipitate only when co-expressed with PSD-95. CAR also brings both PSD-95 and ASIC3 to the junctions of heterologous cells. Moreover, CAR rescues PSD-95-mediated inhibition of ASIC3 currents. These data suggest that, in addition to activity as a viral receptor and adhesion molecule, CAR can play a role in trafficking proteins, including ion channels, in a PDZ-based scaffolding complex.
KW - ASIC3
KW - Coxsackievirus and adenovirus receptor
KW - PSD-95
KW - Protein trafficking
UR - http://www.scopus.com/inward/record.url?scp=84865182181&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2012.07.033
DO - 10.1016/j.bbrc.2012.07.033
M3 - Article
C2 - 22809504
AN - SCOPUS:84865182181
SN - 0006-291X
VL - 425
SP - 13
EP - 18
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -