The asparagine 533 residue in the outer pore loop region of the mouse PKD 2L1 channel is essential for its voltage‐dependent inactivation
| Autor: | Taiga Higuchi, Toshihiro Toba, Hideki Sakai, Takahiro Shimizu, Chie Ohno, Takuto Fujii, Bernd Nilius |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Membrane potential Chemistry Mutant channel Depolarization PKD2L1 Molecular biology General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Transient receptor potential channel 030104 developmental biology 0302 clinical medicine Membrane transient receptor potential Biophysics Extracellular TRPP3 inactivation Asparagine Research Articles 030217 neurology & neurosurgery Ion channel Research Article |
| Zdroj: | FEBS Open Bio |
| ISSN: | 2211-5463 1392-1401 |
| Popis: | Voltage-dependent inactivation of ion channels contributes to the regulation of the membrane potential of excitable cells. Mouse polycystic kidney disease 2-like 1 (PKD2L1) forms voltage-dependent nonselective cation channels, which are activated but subsequently inactivated in response to membrane depolarization. Here, we found that the mutation of an asparagine 533 residue (N533Q) in the outer pore loop region of PKD2L1 caused a marked increase in outward currents induced by depolarization. In addition, the tail current analysis demonstrated that the N533Q mutants are activated during depolarization but the subsequent inactivation does not occur. Interestingly, the N533Q mutants lacked the channel activation triggered by the removal of stimuli such as extracellular alkalization and heating. Our findings suggest that the N533 residue in the outer pore loop region of PKD2L1 has a key role in the voltage-dependent channel inactivation. ispartof: FEBS Open Bio vol:7 issue:9 pages:1392-1401 ispartof: location:England status: published |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text