TY - JOUR
T1 - Calcium-calmodulin modulation of the olfactory cyclic nucleotide-gated cation channel
AU - Liu, Mingyao
AU - Chen, Tsung Yu
AU - Ahamed, Basheer
AU - Li, Jess
AU - Yau, King Wai
PY - 1994
Y1 - 1994
N2 - Although several ion channels have been reported to be directly modulated by calcium-calmodulin, they have not been conclusively shown to bind calmodulin, nor are the modulatory mechanisms understood. Study of the olfactory cyclic nucleotide-activated cation channel, which is modulated by calcium-calmodulin, indicates that calcium-calmodulin directly binds to a specific domain on the amino terminus of the channel. This binding reduces the effective affinity of the channel for cyclic nucleotides, apparently by acting on channel gating, which is tightly coupled to ligand binding. The data reveal a control mechanism that resembles those underlying the regulation of enzymes by calmodulin. The results also point to the amino-terminal part of the olfactory channel as an element for gating, which may have general significance in the operation of ion channels with similar overall structures.
AB - Although several ion channels have been reported to be directly modulated by calcium-calmodulin, they have not been conclusively shown to bind calmodulin, nor are the modulatory mechanisms understood. Study of the olfactory cyclic nucleotide-activated cation channel, which is modulated by calcium-calmodulin, indicates that calcium-calmodulin directly binds to a specific domain on the amino terminus of the channel. This binding reduces the effective affinity of the channel for cyclic nucleotides, apparently by acting on channel gating, which is tightly coupled to ligand binding. The data reveal a control mechanism that resembles those underlying the regulation of enzymes by calmodulin. The results also point to the amino-terminal part of the olfactory channel as an element for gating, which may have general significance in the operation of ion channels with similar overall structures.
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U2 - 10.1126/science.266.5189.1348
DO - 10.1126/science.266.5189.1348
M3 - Article
C2 - 7526466
AN - SCOPUS:0028600648
SN - 0036-8075
VL - 266
SP - 1348
EP - 1354
JO - Science
JF - Science
IS - 5189
ER -