ArticleProceedings of the National Academy of Sciences of the United States of America2013
Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC).
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.
What it found
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Who cites it
43 citing papers in PubMed, 72 citations in OpenAlex.
- TMEM16A channel signalling microdomains in the regulation of vascular function.The Journal of physiology · 2026Review
- Calcium-activated chloride channel TMEM16A opens via pi-helical transition in transmembrane segment 4.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The epsilon toxin from Clostridium perfringens stimulates calcium-activated chloride channels, generating extracellular vesicles in Xenopus oocytes.Pharmacology research & perspectives · 2024Article
- Missense variants in ANO4 cause sporadic encephalopathic or familial epilepsy with evidence for a dominant-negative effect.American journal of human genetics · 2024Article
- Structural heterogeneity of the ion and lipid channel TMEM16F.Nature communications · 2024Article
- Article
- Two to tango: endothelial cell TMEM16 scramblases drive coagulation and thrombosis.The Journal of clinical investigation · 2023Article
- Low signaling efficiency from receptor to effector in olfactory transduction: A quantified ligand-triggered GPCR pathway.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Role of the IgG4-related cholangitis autoantigen annexin A11 in cholangiocyte protection.Journal of hepatology · 2022Article
- 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
- Comparison of ion transport determinants between a TMEM16 chloride channel and phospholipid scramblase.The Journal of general physiology · 2019Article
- Known structures and unknown mechanisms of TMEM16 scramblases and channels.The Journal of general physiology · 2018Review
- Calcium-Activated ClInternational journal of molecular sciences · 2018Review
- 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
- The Sixth Transmembrane Segment Is a Major Gating Component of the TMEM16A Calcium-Activated Chloride Channel.Neuron · 2018Article
- TMEM16A and TMEM16B channel proteins generate CaThe Journal of biological chemistry · 2018Article
- Highlights for the 6th International Ion Channel Conference: ion channel structure, function, disease and therapeutics.Acta pharmaceutica Sinica. B · 2017Article
- The long tale of the calcium activated ClChannels (Austin, Tex.) · 2017Review
- Substituted 2-Acylaminocycloalkylthiophene-3-carboxylic Acid Arylamides as Inhibitors of the Calcium-Activated Chloride Channel Transmembrane Protein 16A (TMEM16A).Journal of medicinal chemistry · 2017Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Transmembrane proteins with unknown function 16 (TMEM16A) is a calcium-activated chloride channel (CaCC) important for neuronal, exocrine, and smooth muscle functions. TMEM16A belongs to a family of integral membrane proteins that includes another CaCC, TMEM16B, responsible for controlling action potential waveform and synaptic efficacy, and a small-conductance calcium-activated nonselective cation channel, TMEM16F, linked to Scott syndrome. We find that these channels in the TMEM16 family share a homodimeric architecture facilitated by their cytoplasmic N termini. This dimerization domain is important for channel assembly in eukaryotic cells, and the in vitro association of peptides containing the dimerization domain is consistent with a homotypic protein-protein interaction. Amino acid substitutions in the dimerization domain affect functional TMEM16A-CaCC channel expression, as expected from its critical role in channel subunit assembly.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.