biostudies-literatureUnknown25(11)Yuan WTransmembrane protein 16A (TMEM16A) localizes at plasma membrane and controls chloride influx in various type of cells. We here showed an intracellular localization pattern of TMEM16A molecules. In myoblasts, TMEM16A was primarily localized to the cytosolic compartment and partially co-localized with intracellular organelles. The global deletion of TMEM16A led to severe skeletal muscle developmental defect. In vitro observation showed that the proliferation of Tmem16a-/- myoblasts was significantly promoted along with activated ERK1/2 and Cyclin D expression; the myogenic differentiation was impaired accompanied by the enhanced caspase 12/3 activation, implying enhanced endoplasmic reticulum (ER) stress. Interestingly, the bradykinin-induced Ca2+ release from ER caiScience105446https://www.ebi.ac.uk/biostudies/studies/S-EPMC9647518biostudies-literatureIntracellular TMEM16A is necessary for myogenesis of skeletal muscle.PMC9647518Fan HWChen HQLi JHu BXChen YCFan CEWang PShi MYZhang ZSun ZYMa TXCui CCZhu MSYuan WXu YHfalseIntracellular TMEM16A is necessary for myogenesis of skeletal muscle.Transmembrane protein 16A (TMEM16A) localizes at plasma membrane and controls chloride influx in various type of cells. We here showed an intracellular localization pattern of TMEM16A molecules. In myoblasts, TMEM16A was primarily localized to the cytosolic compartment and partially co-localized with intracellular organelles. The global deletion of TMEM16A led to severe skeletal muscle developmental defect. In vitro observation showed that the proliferation of Tmem16a-/- myoblasts was significantly promoted along with activated ERK1/2 and Cyclin D expression; the myogenic differentiation was impaired accompanied by the enhanced caspase 12/3 activation, implying enhanced endoplasmic reticulum (ER) stress. Interestingly, the bradykinin-induced Ca2+ release from ER ca2022-01-01T00:00:00Z2022 Nov2026-05-31T23:07:53.604Z2025-04-04T21:00:49.656ZS-EPMC96475183638895510.1016/j.isci.2022.105446