Dynamic landscape of the intracellular termini of acid-sensing ion channel 1a.

Acid-sensing ion channels (ASICs) are trimeric proton-gated sodium channels. Recent work has shown that these channels play a role in necroptosis following prolonged acidic exposure like occurs in stroke. The C-terminus of ASIC1a is thought to mediate necroptotic cell death through interaction with receptor interacting serine threonine kinase 1 (RIPK1).

Dynamic landscape of the intracellular termini of acid-sensing ion channel 1a.

Acid-sensing ion channels (ASICs) are trimeric proton-gated sodium channels. Recently it has been shown that these channels play a role in necroptosis following prolonged acidic exposure like occurs in stroke. The C-terminus of the channel is thought to mediate necroptotic cell death through interaction with receptor interacting serine threonine kinase 1 (RIPK1).

Regulation of acid-sensing ion channels by protein binding partners.

Acid-sensing ion channels (ASICs) are a family of proton-gated cation channels that contribute to a diverse array of functions including pain sensation, cell death during ischemia, and more broadly to neurotransmission in the central nervous system. There is an increasing interest in understanding the physiological regulatory mechanisms of this family of channels. ASICs have relatively short N- and C-termini, yet a number of proteins have been shown to interact with these domains both and .

Insights into the molecular mechanisms underlying the inhibition of acid-sensing ion channel 3 gating by stomatin.

Stomatin (STOM) is a monotopic integral membrane protein found in all classes of life that has been shown to regulate members of the acid-sensing ion channel (ASIC) family. However, the mechanism by which STOM alters ASIC function is not known. Using chimeric channels, we combined patch-clamp electrophysiology and FRET to search for regions of ASIC3 critical for binding to and regulation by STOM.