A sustained increase in the intracellular Ca2+ concentration induces proteolytic cleavage of EAG2 channel

Shimizu, Nobuhiro; Sato, Noriaki; Kikuchi, Teppei; Ishizaki, Takuro; Kobayashi, Kazuto; Kita, Kaori; Takimoto, Koichi

doi:10.1016/j.biocel.2014.12.007

Cited by 1 publication

(1 citation statement)

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“…In this scenario, disruption of peptide continuity may eliminate, or alter, propagation of regulatory signals to the channel domain and thereby impact channel activity. To date, Na + channels (Nav 1.6, ASIC-1) [11, 12], K + channels (EAG2) [14], Ca 2+ channels (Cav 1.2, TRPM7) [13, 32–34], and non-selective cation channels (CNG channels, NMDA receptors) [35, 36] have been reported as substrates whose biophysical properties are regulated by proteolysis (see Table 1). We describe several examples of Ca 2+ conducting channels where proteolysis alters their properties and finally highlight how this form of regulation alters IP 3 R activity in a subtype dependent manner.…”

Section: Regulation Of Ion Channels Activities By Proteolysismentioning

confidence: 99%

Differential regulation of ion channels function by proteolysis

Wang¹,

Yule²

2018

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Ion channels are pore-forming protein complexes in membranes that play essential roles in a diverse array of biological activities. Ion channel activity is strictly regulated at multiple levels and by numerous cellular events to selectively activate downstream effectors involved in specific biological activities. For example, ions, binding proteins, nucleotides, phosphorylation, the redox state, channel subunit composition have all been shown to regulate channel activity and subsequently allow channels to participate in distinct cellular events. While these forms of modulation are well documented and have been extensively reviewed, in this article, we will first review and summarize channel proteolysis as a novel and quite widespread mechanism for altering channel activity. We will then highlight the recent findings demonstrating that proteolysis profoundly alters Inositol 1,4,5 trisphosphate receptor activity, and then discuss its potential functional ramifications in various developmental and pathological conditions.

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