The cholinergic antagonist alpha-bungarotoxin also binds and blocks a subset of GABA receptors.
The polypeptide snake toxin alpha-bungarotoxin (BTX) has been used in hundreds of studies on the structure, function, and development of the neuromuscular junction because it binds tightly and specifically to the nicotinic acetylcholine receptors (nAChRs) at this synapse. We show here that BTX also binds to and blocks a subset of GABA(A) receptors (GABA(A)Rs) that contain the GABA(A)R beta3 subunit. These results introduce a previously unrecognized tool for analysis of GABA(A)Rs but may complicate interpretation of some studies on neuronal nAChRs.
Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.
Corey M
CM
McCann
John
J
Bracamontes
Joe Henry
JH
Steinbach
Joshua R
JR
Sanes
D000818:Animals; D001665:Binding Sites; D002038:Bungarotoxins / Q000378:metabolism* / Q000494:pharmacology*; D002460:Cell Line; D002712:Chlorides / Q000037:antagonists & inhibitors / Q000494:pharmacology; D018680:Cholinergic Antagonists / Q000378:metabolism* / Q000494:pharmacology*; D006224:Cricetinae; D004553:Electric Conductivity; D005110:Extracellular Space / Q000378:metabolism; D018756:GABA Antagonists / Q000378:metabolism* / Q000494:pharmacology*; D006801:Humans; D009865:Oocytes / Q000378:metabolism; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism; D018079:Receptors, GABA / Q000235:genetics / Q000378:metabolism*; D014982:Xenopus laevis / Q000235:genetics
D002038:Bungarotoxins; D002712:Chlorides; D018680:Cholinergic Antagonists; D018756:GABA Antagonists; D021122:Protein Subunits; D018079:Receptors, GABA