Title: The asparagine 533 residue in the outer pore loop region of the mouse PKD2L1 channel is essential for its voltage-dependent inactivation
Authors: Shimizu, Takahiro ×
Higuchi, Taiga
Toba, Toshihiro
Ohno, Chie
Fujii, Takuto
Nilius, Bernd
Sakai, Hideki #
Issue Date: Sep-2017
Publisher: Elsevier BV
Series Title: FEBS Open Bio vol:7 issue:9 pages:1392-1401
Article number: 10.1002/2211-5463.12273
Abstract: 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.
ISSN: 2211-5463
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Ion Channel Research (VIB-KU Leuven Center for Brain & Disease Research)
Department of Cellular and Molecular Medicine - miscellaneous
× corresponding author
# (joint) last author

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