Purified human brain calmodulin does not alter the bicarbonate permeability of the ANO1/TMEM16A channel
نویسندگان
چکیده
Purified human brain calmodulin does not alter the bicarbonate permeability of the ANO1/TMEM16A channel Yawei Yu and Tsung-Yu Chen Volume 145, No. 1, January 5, 2015. Pages 79–81. In a revised version of Jung and Lee’s Letter to the Editor, two additional panels were added to their Fig. 1. Consequently, Yu and Chen’s references to Jung and Lee’s Fig. 1, B and C, should refer instead to Fig. 1, C and D. The HTML and PDF versions of the article have been corrected. Correction
منابع مشابه
Does calmodulin regulate the bicarbonate permeability of ANO1/TMEM16A or not?
The role of calmodulin in the activation of Ca 2+-activated Cl channels (CaCCs) has been an important topic over the past three decades of CaCC research. Recently, the discovery of ANO1/TMEM16 as a component of CaCC raised the question of whether calmodulin modulates ANO1 activity (Tian et al. permeability of human ANO1 (hANO1) can be dynamically modulated by Ca 2+ /calmodulin (Jung et al.,...
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The Ca(2+)-activated Cl channel anoctamin-1 (Ano1; Tmem16A) plays a variety of physiological roles, including epithelial fluid secretion. Ano1 is activated by increases in intracellular Ca(2+), but there is uncertainty whether Ca(2+) binds directly to Ano1 or whether phosphorylation or additional Ca(2+)-binding subunits like calmodulin (CaM) are required. Here we show that CaM is not necessary ...
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TMEM16A (anoctamin 1, Ano1), a member of a family of 10 homologous proteins, has been shown to form an essential component of Ca(2+)-activated Cl(-) channels. TMEM16A-null mice exhibit severe defects in epithelial transport along with tracheomalacia and death within 1 mo after birth. Despite its outstanding physiological significance, the mechanisms for activation of TMEM16A remain obscure. TME...
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