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- W3011107890 endingPage "122" @default.
- W3011107890 startingPage "110" @default.
- W3011107890 abstract "Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels are expressed throughout the mammalian central nervous system (CNS). These channels have been implicated in a wide range of diseases, including Major Depressive Disorder and multiple subtypes of epilepsy. The diversity of functions that HCN channels perform is in part attributable to differences in their subcellular localization. To facilitate a broad range of subcellular distributions, HCN channels are bound by auxiliary subunits that regulate surface trafficking and channel function. One of the best studied auxiliary subunits is tetratricopeptide-repeat containing, Rab8b-interacting protein (TRIP8b). TRIP8b is an extensively alternatively spliced protein whose only known function is to regulate HCN channels. TRIP8b binds to HCN pore-forming subunits at multiple interaction sites that differentially regulate HCN channel function and subcellular distribution. In this review, we summarize what is currently known about the structure and function of TRIP8b isoforms with an emphasis on the role of this auxiliary subunit in health and disease." @default.
- W3011107890 created "2020-03-23" @default.
- W3011107890 creator A5006991821 @default.
- W3011107890 creator A5015534864 @default.
- W3011107890 creator A5034366784 @default.
- W3011107890 creator A5074699244 @default.
- W3011107890 date "2020-01-01" @default.
- W3011107890 modified "2023-10-16" @default.
- W3011107890 title "The structure and function of TRIP8b, an auxiliary subunit of hyperpolarization-activated cyclic-nucleotide gated channels" @default.
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