ArticleNature2014
X-ray structure of a calcium-activated TMEM16 lipid scramblase.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 291 papers.
What it found
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Who cites it
291 citing papers in PubMed, 472 citations in OpenAlex.
- Lipid flip-flop in biological membranes: through the lens of TMEM16F.Physiological reviews · 2027Review
- Distinct structural mechanisms drive gain-of-function activation of TMEM16E in gnathodiaphyseal dysplasia.Research square · 2026Article
- Structural insight into sodium-dependent bile acid transport by members of the SLC10 family.Structure (London, England : 1993) · 2026Article
- Lipid traffic: an enigmatic alliance between ORPs and a TMEM16-like protein at membrane contact sites.Biochemical Society transactions · 2026Review
- Structural evolution of the MTCH family of mitochondrial insertases.Science advances · 2026Article
- Functional Divergence and Emerging Roles of the ANO-TMC-TMEM63 Channel Families in Olfaction and Gustation.International journal of molecular sciences · 2026Review
- Structural evolution of the MTCH family of mitochondrial insertases.bioRxiv : the preprint server for biology · 2026Article
- Organelle contact sites in cancer cells.Cell death & disease · 2026Review
- Calcium dependent activation of the TMEM16F scramblase and ion channel.Nature structural & molecular biology · 2026Article
- TMEM63 proteins act as mechanically activated cholesterol modulated lipid scramblases contributing to membrane mechano-resilience.Nature communications · 2026Article
- Conformational changes upon pore blocker removal reveal conductive states of TMEM16A.bioRxiv : the preprint server for biology · 2026Article
- Interplay of CaThe Journal of physiology · 2026Article
- From plasma membrane to lysosomes: expanding roles of TMEM63/OSCA channels in mechanosensation and intracellular signaling.Frontiers in pharmacology · 2026Review
- Anoctamin 5 mutation leads to abnormal bone homeostasis of GDD by regulating AMPK-dependent glucose metabolism.Frontiers in endocrinology · 2026Article
- MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony.Nature methods · 2025Article
- Ist2 promotes lipid transfer by Osh6 via its membrane tethering and lipid scramblase activities.Science advances · 2025Article
- Mechanism of Phosphatidylserine Lipid Scrambling by Human SERINC3, an HIV-1 Restriction Factor.bioRxiv : the preprint server for biology · 2025Article
- Structural basis for lipid transport at membrane contact sites by the IST2-OSH6 complex.Nature structural & molecular biology · 2025Article
- Preparation and Photophysical Characterization of N‑Substituted 7‑Nitro-2,1,3-benzoxadiazol-4-amine Derivatives.ACS omega · 2025Article
- Exploring Niclosamide as a Multi-target Drug Against SARS-CoV-2: Molecular Dynamics Simulation Studies on Host and Viral Proteins.Molecular biotechnology · 2025Article
231 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TMEM16 family of proteins, also known as anoctamins, features a remarkable functional diversity. This family contains the long sought-after Ca(2+)-activated chloride channels as well as lipid scramblases and cation channels. Here we present the crystal structure of a TMEM16 family member from the fungus Nectria haematococca that operates as a Ca(2+)-activated lipid scramblase. Each subunit of the homodimeric protein contains ten transmembrane helices and a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer as a potential site of catalysis. This cavity harbours a conserved Ca(2+)-binding site located within the hydrophobic core of the membrane. Mutations of residues involved in Ca(2+) coordination affect both lipid scrambling in N. haematococca TMEM16 and ion conduction in the Cl(-) channel TMEM16A. The structure reveals the general architecture of the family and its mode of Ca(2+) activation. It also provides insight into potential scrambling mechanisms and serves as a framework to unravel the conduction of ions in certain TMEM16 proteins.
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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.