ArticleThe Journal of biological chemistry2014
Functional swapping between transmembrane proteins TMEM16A and TMEM16F.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Lipid flip-flop in biological membranes: through the lens of TMEM16F.Physiological reviews · 2027Review
- Optimization of a malachite green-pyrophosphatase assay for the Zika virus RNA-dependent RNA polymerase and preliminary identification of natural product modulators.Frontiers in drug discovery · 2026Article
- TMEM16F Expressed in Kupffer Cells Regulates Liver Inflammation and Metabolism to Protect Against Listeria Monocytogenes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Phospholipid scrambling induced by an ion channel/metabolite transporter complex.Nature communications · 2024Article
- Activation of TMEM16F by inner gate charged mutations and possible lipid/ion permeation mechanisms.Biophysical journal · 2022Article
- Polymodal Control of TMEM16x Channels and Scramblases.International journal of molecular sciences · 2022Review
- Cytosolic and mitochondrial CaPlatelets · 2021Article
- Epigallocatechin gallate inhibits release of extracellular vesicles from platelets without inhibiting phosphatidylserine exposure.Scientific reports · 2021Article
- ANO5 ensures trafficking of annexins in wounded myofibers.The Journal of cell biology · 2021Article
- Evidence that polyphenols do not inhibit the phospholipid scramblase TMEM16F.The Journal of biological chemistry · 2020Article
- Out-of-the-groove transport of lipids by TMEM16 and GPCR scramblases.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Functional roles of glutamic acid E143 and E705 residues in the N-terminus and transmembrane domain 7 of Anoctamin 1 in calcium and noxious heat sensing.BMB reports · 2018Article
- Single-molecule analysis of phospholipid scrambling by TMEM16F.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Activation of the phospholipid scramblase TMEM16F by nanosecond pulsed electric fields (nsPEF) facilitates its diverse cytophysiological effects.The Journal of biological chemistry · 2017Article
- Exposure of phosphatidylserine on the cell surface.Cell death and differentiation · 2016Review
- Neuronal ClC-3 Splice Variants Differ in Subcellular Localizations, but Mediate Identical Transport Functions.The Journal of biological chemistry · 2015Article
- Variomics screen identifies the re-entrant loop of the calcium-activated chloride channel ANO1 that facilitates channel activation.The Journal of biological chemistry · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transmembrane proteins TMEM16A and -16F each carry eight transmembrane regions with cytoplasmic N and C termini. TMEM16A carries out Ca(2+)-dependent Cl(-) ion transport, and TMEM16F is responsible for Ca(2+)-dependent phospholipid scrambling. Here we established assay systems for the Ca(2+)-dependent Cl(-) channel activity using 293T cells and for the phospholipid scramblase activity using TMEM16F(-/-) immortalized fetal thymocytes. Chemical cross-linking analysis showed that TMEM16A and -16F form homodimers in both 293T cells and immortalized fetal thymocytes. Successive deletion from the N or C terminus of both proteins and the swapping of regions between TMEM16A and -16F indicated that their cytoplasmic N-terminal (147 amino acids for TMEM16A and 95 for 16F) and C-terminal (88 amino acids for TMEM16A and 68 for 16F) regions were essential for their localization at plasma membranes and protein stability, respectively, and could be exchanged. Analyses of TMEM16A and -16F mutants with point mutations in the pore region (located between the fifth and sixth transmembrane regions) indicated that the pore region is essential for both the Cl(-) channel activity of TMEM16A and the phospholipid scramblase activity of TMEM16F. Some chemicals such as epigallocatechin-3-gallate and digallic acid inhibited the Cl(-) channel activity of TMEM16A and the scramblase activity of TMEM16F with an opposite preference. These results indicate that TMEM16A and -16F use a similar mechanism for sorting to plasma membrane and protein stabilization, but their functional domains significantly differ.
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