Abstract
Anoctamin 6 (Ano6) belongs to a conserved gene family (TMEM16) predicted to code for eight transmembrane proteins with putative Ca2+-activated chloride channel (CaCC) activity. Recent work revealed that disruption of ANO6 leads to a blood coagulation defect and impaired skeletal development. However, its function in skeletal muscle cells remains to be determined. By using a RNA interference mediated (RNAi) loss-of-function approach, we show that Ano6 regulates C2C12 myoblast proliferation. Ano6 is highly expressed in C2C12 myoblasts and its expression decreases upon differentiation. Knocking down Ano6 significantly reduces C2C12 myoblast proliferation but has minimal effect on differentiation. Ano6 deficiency significantly reduces ERK/AKT phosphorylation, which has been shown to be involved in regulation of cancer cell proliferation by another Anoctamin member. Taken together, our data demonstrate for the first time that Ano6 plays an essential role in C2C12 myoblast proliferation, likely via regulating the ERK/AKT signaling pathway.
Highlights
The anoctamin family is comprised of 10 proteins, each possessing eight transmembrane domains and cytosolic amino- and carboxyl-termini [1,2]
To test whether a similar expression pattern exists in mouse skeletal muscle, we examined the expression of Anoctamin 6 (Ano6) in young and adult skeletal muscle of wild-type mice
We demonstrate that Ano6 is highly expressed in undifferentiated myoblasts with peak expression during initial stages of myotube formation in vitro
Summary
The anoctamin family ( referred to as TMEM16) is comprised of 10 proteins, each possessing eight transmembrane domains and cytosolic amino- and carboxyl-termini [1,2]. They show distinct but overlapping expression patterns in a variety of cell types and tissues during development [3,4]. In addition to its potential function as a chloride channel, Ano has recently been identified as a calcium-activated cation channel that regulates Ca2+-dependent phosphatidylserine (PS) scrambling from the interior to exterior leaflet of the plasma membrane in blood cells [5]. The cellular functions of Ano in skeletal muscle have not been determined
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