Targeting of Intracellular TMEM16 Proteins to the Plasma Membrane and Activation by Purinergic Signaling.

International Journal of Molecular Sciences
Rainer SchreiberKarl Kunzelmann

Abstract

Anoctamins such as TMEM16A and TMEM16B are Ca2+-dependent Cl- channels activated through purinergic receptor signaling. TMEM16A (ANO1), TMEM16B (ANO2) and TMEM16F (ANO6) are predominantly expressed at the plasma membrane and are therefore well accessible for functional studies. While TMEM16A and TMEM16B form halide-selective ion channels, TMEM16F and probably TMEM16E operate as phospholipid scramblases and nonselective ion channels. Other TMEM16 paralogs are expressed mainly in intracellular compartments and are therefore difficult to study at the functional level. Here, we report that TMEM16E (ANO5), -H (ANO8), -J (ANO9) and K (ANO10) are targeted to the plasma membrane when fused to a C-terminal CAAX (cysteine, two aliphatic amino acids plus methionin, serine, alanin, cystein or glutamin) motif. These paralogs produce Ca2+-dependent ion channels. Surprisingly, expression of the TMEM16 paralogs in the plasma membrane did not produce additional scramblase activity. In contrast, endogenous scrambling induced by stimulation of purinergic P2X7 receptors was attenuated, in parallel with reduced plasma membrane blebbing. This could suggest that intracellular TMEM16 paralogs operate differently when compared to plasma membrane-locali...Continue Reading

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Citations

Feb 14, 2021·The Journal of Biological Chemistry·Jarred M Whitlock, Leonid V Chernomordik
Nov 10, 2021·Clinical Science·Anastasia V SudarikovaDaria V Ilatovskaya

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Methods Mentioned

BETA
GTPase
biosensor
transfection

Software Mentioned

PULSE
Metafluor
ZEN
BEBuilder

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