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PKA phosphorylates KCND2 on S552. 12 / 14
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sparser
"Compared with the marked redistribution of Kv4.2g observed in xref , these data clearly indicate that the activity-dependent internalization of Kv4.2 channels requires PKA phosphorylation of Kv4.2 at Ser552."

sparser
"Previous studies have shown that Kv4.2 can be phosphorylated by PKA at S552, and by ERK1/2 at residues T602, T607 and S616 in the cytoplasmic C-terminus of the channel protein ( xref , xref )."

sparser
"Additionally, the finding that PKA phosphorylation of Kv4.2 at site S552 underlies reduced Kv4.2 surface expression in the presence of AKAP79 is consistent with our previous finding that PKA phosphorylation of S552 mediates activity-dependent Kv4.2 trafficking ( xref )."

reach
"Previous studies have shown that Kv4.2 can be phosphorylated by PKA at S552, and by ERK1/2 at residues T602, T607 and S616 in the cytoplasmic C-terminus of the channel protein (Adams et al., 2000, Anderson et al., 2000)."

sparser
"As PKA phosphorylation of Kv4.2 S552 is necessary for activity-dependent Kv4.2 trafficking we wondered if PKA anchoring by AKAPs affected Kv4.2 surface expression."

sparser
"Specifically, PKA phosphorylation of Kv4.2 at Ser552 is necessary for its activity-dependent internalization ( xref ; xref , available atas supplemental material)."

sparser
"PKA phosphorylation at Kv4.2-S552 reduces the current mediated by Kv4 channels in HEK293 cells, cardiomyocytes, and neurons."

sparser
"PKA can phosphorylate Kv4.2-S552 to increase channel internalization in heterologous expression systems, neurons, and cardiomyocytes [ xref , xref , xref ]."

sparser
"PKA phosphorylation of Kv4.2 at site S552 was not required for AKAP-Kv4.2 co-IP, however, as mutating this site did not prevent its IP with wild type AKAP79 using an AKAP79/150 antibody ( xref )."

sparser
"We found that while interaction between Kv4.2 and KChIP4a does not require PKA phosphorylation of Kv4.2 S552 , phosphorylation of this site is necessary for both enhanced stabilization and membrane expression of Kv4.2 channel complexes produced by KChIP4a."

sparser
"Enhanced surface expression and protein stability conferred by co-expression of Kv4.2 with other KChIP isoforms did not require PKA phosphorylation of Kv4.2 S552."

sparser
"We found that PKA phosphorylation of Kv4.2 at Ser552 is necessary for the activity-dependent internalization of Kv4.2."