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• W4283163958 abstract "Hyperpolarization-activated, cyclic nucleotide-sensitive (HCN) channels are key regulators of subthreshold membrane potentials in excitable cells. The four mammalian HCN channel isoforms, HCN1-HCN4, are expressed throughout the body, where they contribute to diverse physiological processes including cardiac pacemaking, sleep-wakefulness cycles, memory, and somatic sensation. While all HCN channel isoforms produce currents when expressed by themselves, an emerging list of interacting proteins shape HCN channel excitability to influence the physiologically relevant output. The best studied of these regulatory proteins is the auxiliary subunit, TRIP8b, which binds to multiple sites in the C-terminus of the HCN channels to regulate expression and disrupt cAMP binding to fine-tune neuronal HCN channel excitability. Less is known about the mechanisms of action of other HCN channel interaction partners like filamin A, Src tyrosine kinase, and MinK-related peptides, which have a range of effects on HCN channel gating and expression. More recently, the inositol trisphosphate receptor-associated cGMP-kinase substrates IRAG1 and LRMP (also known as IRAG2), were discovered as specific regulators of the HCN4 isoform. This review summarizes the known protein interaction partners of HCN channels and their mechanisms of action and identifies gaps in our knowledge." @default.
• W4283163958 created "2022-06-21" @default.
• W4283163958 creator A5014018047 @default.
• W4283163958 creator A5059162284 @default.
• W4283163958 creator A5081031628 @default.
• W4283163958 creator A5087989619 @default.
• W4283163958 date "2022-06-20" @default.
• W4283163958 modified "2023-10-03" @default.
• W4283163958 title "Regulation of HCN Channels by Protein Interactions" @default.
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• W4283163958 doi "https://doi.org/10.3389/fphys.2022.928507" @default.
• W4283163958 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35795651" @default.

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