Dendrotoxin-binding brain membrane protein displays a K+ channel activity that is stimulated by both cAMP-dependent and endogenous phosphorylations.
The purified protein that binds the K+ channel ligands dendrotoxin I and mast cell degranulating peptide can be phosphorylated by cAMP-dependent protein kinase and by an endogenous protein kinase, which may be a specific K+ channel kinase. Phosphorylations take place on the toxin-binding subunit, a polypeptide of 76-80 kDa. Phosphorylation by both kinases leads to activation of the reconstituted dendrotoxin-sensitive K+ channel.
Rehm
H
H
Centre de Biochimie du Centre National de la Recherche Scientifique, Parc Valrose, Nice, France.
Pelzer
S
S
Cochet
C
C
Chambaz
E
E
Tempel
B L
BL
Trautwein
W
W
Pelzer
D
D
Lazdunski
M
M
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004546:Elapid Venoms / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008051:Lipid Bilayers; D009498:Neurotoxins / Q000378:metabolism*; D010766:Phosphorylation; D015221:Potassium Channels / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011950:Receptors, Cholinergic / Q000302:isolation & purification / Q000378:metabolism*
D004546:Elapid Venoms; D008051:Lipid Bilayers; D009498:Neurotoxins; D015221:Potassium Channels; D011950:Receptors, Cholinergic; C042467:dendrotoxin receptor; C020273:dendrotoxin; D011494:Protein Kinases