Kv7 channels can function without constitutive calmodulin tethering
M-channels are voltage-gated potassium channels composed of Kv7.2-7.5 subunits that serve as important regulators of neuronal excitability. Calmodulin binding is required for Kv7 channel function and mutations in Kv7.2 that disrupt calmodulin binding cause Benign Familial Neonatal Convulsions (BFNC)...
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| Veröffentlicht in: | PloS one 2011-09, Vol.6 (9), p.e25508-e25508 |
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| creator | Gómez-Posada, Juan Camilo Aivar, Paloma Alberdi, Araitz Alaimo, Alessandro Etxeberría, Ainhoa Fernández-Orth, Juncal Zamalloa, Teresa Roura-Ferrer, Meritxell Villace, Patricia Areso, Pilar Casis, Oscar Villarroel, Alvaro |
| description | M-channels are voltage-gated potassium channels composed of Kv7.2-7.5 subunits that serve as important regulators of neuronal excitability. Calmodulin binding is required for Kv7 channel function and mutations in Kv7.2 that disrupt calmodulin binding cause Benign Familial Neonatal Convulsions (BFNC), a dominantly inherited human epilepsy. On the basis that Kv7.2 mutants deficient in calmodulin binding are not functional, calmodulin has been defined as an auxiliary subunit of Kv7 channels. However, we have identified a presumably phosphomimetic mutation S511D that permits calmodulin-independent function. Thus, our data reveal that constitutive tethering of calmodulin is not required for Kv7 channel function. |
| doi_str_mv | 10.1371/journal.pone.0025508 |
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Calmodulin binding is required for Kv7 channel function and mutations in Kv7.2 that disrupt calmodulin binding cause Benign Familial Neonatal Convulsions (BFNC), a dominantly inherited human epilepsy. On the basis that Kv7.2 mutants deficient in calmodulin binding are not functional, calmodulin has been defined as an auxiliary subunit of Kv7 channels. However, we have identified a presumably phosphomimetic mutation S511D that permits calmodulin-independent function. 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Calmodulin binding is required for Kv7 channel function and mutations in Kv7.2 that disrupt calmodulin binding cause Benign Familial Neonatal Convulsions (BFNC), a dominantly inherited human epilepsy. On the basis that Kv7.2 mutants deficient in calmodulin binding are not functional, calmodulin has been defined as an auxiliary subunit of Kv7 channels. However, we have identified a presumably phosphomimetic mutation S511D that permits calmodulin-independent function. 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are voltage-gated potassium channels composed of Kv7.2-7.5 subunits that serve as important regulators of neuronal excitability. Calmodulin binding is required for Kv7 channel function and mutations in Kv7.2 that disrupt calmodulin binding cause Benign Familial Neonatal Convulsions (BFNC), a dominantly inherited human epilepsy. On the basis that Kv7.2 mutants deficient in calmodulin binding are not functional, calmodulin has been defined as an auxiliary subunit of Kv7 channels. However, we have identified a presumably phosphomimetic mutation S511D that permits calmodulin-independent function. Thus, our data reveal that constitutive tethering of calmodulin is not required for Kv7 channel function.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21980481</pmid><doi>10.1371/journal.pone.0025508</doi><tpages>e25508</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Binding sites Biology Calcium-binding protein Calmodulin Calmodulin - metabolism Cell Membrane - metabolism Channels Convulsions Epilepsy Excitability Gene Expression Regulation HEK293 Cells Humans KCNQ2 Potassium Channel - chemistry KCNQ2 Potassium Channel - genetics KCNQ2 Potassium Channel - metabolism KCNQ3 Potassium Channel - chemistry KCNQ3 Potassium Channel - genetics KCNQ3 Potassium Channel - metabolism Kinases Medicine Molecular Sequence Data Mutants Mutation Neonates Neurons Phosphorylation Potassium Potassium channels Potassium channels (voltage-gated) Protein Structure, Secondary Protein Transport Regulators Rodents Tethering Xenopus |
| title | Kv7 channels can function without constitutive calmodulin tethering |
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