ArticleThe Journal of physiology2013
Putative pore-loops of TMEM16/anoctamin channels affect channel density in cell membranes.
Article in The Journal of physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed.
- Gating and anion selectivity are reciprocally regulated in TMEM16A (ANO1).The Journal of general physiology · 2022Article
- The Ca2+-gated channel TMEM16A amplifies capillary pericyte contraction and reduces cerebral blood flow after ischemia.The Journal of clinical investigation · 2022Article
- Polymodal Control of TMEM16x Channels and Scramblases.International journal of molecular sciences · 2022Review
- An outer-pore gate modulates the pharmacology of the TMEM16A channel.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Anion and Cation Permeability of the Mouse TMEM16F Calcium-Activated Channel.International journal of molecular sciences · 2021Article
- Differential Regulation of CaInternational journal of molecular sciences · 2021Article
- Structure-Function of TMEM16 Ion Channels and Lipid Scramblases.Advances in experimental medicine and biology · 2021Article
- Gating and Regulatory Mechanisms of TMEM16 Ion Channels and Scramblases.Frontiers in physiology · 2021Review
- Allosteric modulation of alternatively spliced CaProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K.Nature communications · 2019Article
- Defining the ionic mechanisms of optogenetic control of vascular tone by channelrhodopsin-2.British journal of pharmacology · 2018Article
- TMEM16A and TMEM16B channel proteins generate CaThe Journal of biological chemistry · 2018Article
- Lipids and ions traverse the membrane by the same physical pathway in the nhTMEM16 scramblase.eLife · 2017Article
- Contrasting effects of phosphatidylinositol 4,5-bisphosphate on cloned TMEM16A and TMEM16B channels.British journal of pharmacology · 2017Article
- Article
- Independent activation of distinct pores in dimeric TMEM16A channels.The Journal of general physiology · 2016Article
- A Pore Idea: the ion conduction pathway of TMEM16/ANO proteins is composed partly of lipid.Pflugers Archiv : European journal of physiology · 2016Review
- Mechanism of allosteric activation of TMEM16A/ANO1 channels by a commonly used chloride channel blocker.British journal of pharmacology · 2016Article
- Gating modes of calcium-activated chloride channels TMEM16A and TMEM16B.The Journal of physiology · 2015Article
- Ion channel and lipid scramblase activity associated with expression of TMEM16F/ANO6 isoforms.The Journal of physiology · 2015Article
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Abstract
The recently identified TMEM16/anoctamin protein family includes Ca(2+)-activated anion channels (TMEM16A, TMEM16B), a cation channel (TMEM16F) and proteins with unclear function. TMEM16 channels consist of eight putative transmembrane domains (TMs) with TM5-TM6 flanking a re-entrant loop thought to form the pore. In TMEM16A this region has also been suggested to contain residues involved in Ca(2+) binding. The role of the putative pore-loop of TMEM16 channels was investigated using a chimeric approach. Heterologous expression of either TMEM16A or TMEM16B resulted in whole-cell anion currents with very similar conduction properties but distinct kinetics and degrees of sensitivity to Ca(2+). Furthermore, whole-cell currents mediated by TMEM16A channels were ∼six times larger than TMEM16B-mediated currents. Replacement of the putative pore-loop of TMEM16A with that of TMEM16B (TMEM16A-B channels) reduced the currents by ∼six-fold, while the opposite modification (TMEM16B-A channels) produced a ∼six-fold increase in the currents. Unexpectedly, these changes were not secondary to variations in channel gating by Ca(2+) or voltage, nor were they due to changes in single-channel conductance. Instead, they depended on the number of functional channels present on the plasma membrane. Generation of additional, smaller chimeras within the putative pore-loop of TMEM16A and TMEM16B led to the identification of a region containing a non-canonical trafficking motif. Chimeras composed of the putative pore-loop of TMEM16F transplanted into the TMEM16A protein scaffold did not conduct anions or cations. These data suggest that the putative pore-loop does not form a complete, transferable pore domain. Furthermore, our data reveal an unexpected role for the putative pore-loop of TMEM16A and TMEM16B channels in the control of the whole-cell Ca(2+)-activated Cl(-) conductance.
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