The NH2 terminus regulates voltage-dependent gating of CALHM ion channels

American Journal of Physiology. Cell Physiology
Jessica E TanisJ Kevin Foskett

Abstract

Calcium homeostasis modulator protein-1 (CALHM1) and its Caenorhabditis elegans (ce) homolog, CLHM-1, belong to a new family of physiologically important ion channels that are regulated by voltage and extracellular Ca2+ (Ca2+o) but lack a canonical voltage-sensing domain. Consequently, the intrinsic voltage-dependent gating mechanisms for CALHM channels are unknown. Here, we performed voltage-clamp experiments on ceCLHM-1 chimeric, deletion, insertion, and point mutants to assess the role of the NH2 terminus (NT) in CALHM channel gating. Analyses of chimeric channels in which the ceCLHM-1 and human (h)CALHM1 NH2 termini were interchanged showed that the hCALHM1 NT destabilized channel-closed states, whereas the ceCLHM-1 NT had a stabilizing effect. In the absence of Ca2+o, deletion of up to eight amino acids from the ceCLHM-1 NT caused a hyperpolarizing shift in the conductance-voltage relationship with little effect on voltage-dependent slope. However, deletion of nine or more amino acids decreased voltage dependence and induced a residual conductance at hyperpolarized voltages. Insertion of amino acids into the NH2-terminal helix also decreased voltage dependence but did not prevent channel closure. Mutation of ceCLHM-1 valin...Continue Reading

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Citations

Jun 22, 2018·The Journal of Biological Chemistry·Pingzheng ZhouThomas J Jentsch
Jun 20, 2020·Protein Science : a Publication of the Protein Society·Weixin YangXuejun C Zhang
Jan 29, 2020·Nature Structural & Molecular Biology·Johanna L SyrjanenHiro Furukawa
Aug 25, 2020·Science Advances·Yue RenYuequan Shen
Oct 20, 2020·The Journal of General Physiology·Pablo S GaeteJorge E Contreras
Dec 11, 2020·Cell Discovery·Jie LiuSheng Ye
Apr 19, 2021·Journal of Molecular Biology·Johanna SyrjanenHiro Furukawa

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Methods Mentioned

BETA
PCR
antisense oligonucleotide

Software Mentioned

MegAlign
ceCLHM

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