The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The UniProt accession P26361 corresponds to CFTR_MOUSE (cystic fibrosis transmembrane conductance regulator) from Mus musculus, matching the gene symbol Cftr (synonym Abcc7) and the expected ABC-transporter-like architecture. This mapping is explicitly stated in a UniProtKB-based cross-species analysis that lists P26361 = CFTR_MOUSE (mouse; 1476 aa). (hassan2026mathematicalsequenceanalyses pages 3-4)
CFTR (mouse Cftr/Abcc7) is a member of the ATP-binding cassette (ABC) transporter superfamily (ABCC subfamily) but is unusual in that it functions primarily as a regulated anion channel rather than a classical active transporter. (infield2021themolecularevolution pages 1-2, anwar2024cysticfibrosisunderstanding pages 1-2)
CFTR is a multi-pass membrane protein organized into: two membrane-spanning/transmembrane domains (MSD/TMD1 and MSD/TMD2; 12 TM helices total), two cytosolic nucleotide-binding domains (NBD1, NBD2), and a regulatory R domain enriched in phosphorylation sites. (baroni2025unravelingthemechanism pages 2-5, anwar2024cysticfibrosisunderstanding pages 1-2)
The primary function of CFTR is to conduct anions, especially chloride (Cl−) and bicarbonate (HCO3−), across epithelial plasma membranes down electrochemical gradients to drive fluid and electrolyte transport and regulate pH. (infield2021themolecularevolution pages 1-2, jonge2020strategiesforcystic pages 7-9, anwar2024cysticfibrosisunderstanding pages 1-2)
CFTR activity requires (i) phosphorylation of the R domain (typically via cAMP/PKA signaling; intestinal-specific PKG contributions are also described) and (ii) ATP binding and NBD dimerization to open the channel, with ATP hydrolysis at site 2 promoting closure (dissociation of the NBD dimer). (jonge2020strategiesforcystic pages 26-28, jonge2020strategiesforcystic pages 1-5)
In secretory epithelia, CFTR is predominantly localized to the apical plasma membrane of polarized epithelial cells, including airway, intestinal, pancreatic duct, sweat duct, and reproductive tract epithelia. (anwar2024cysticfibrosisunderstanding pages 1-2)
CFTR-mediated anion secretion is mechanistically coupled to basolateral transporters and channels that establish driving forces and supply substrates:
- Basolateral Na+/K+-ATPase maintains Na+ gradient and membrane potential.
- Basolateral NKCC1 loads cells with Cl− for secretion.
- Basolateral K+ channels (e.g., KCNQ1, KCNN4 in intestinal epithelia) recycle K+ and help set membrane potential.
- HCO3− supply/handling involves Na+-coupled transporters (NBCe1/NBCn1) and luminal/basolateral exchangers including SLC26A3 (DRA) and SLC26A6 (PAT-1), functionally integrated with CFTR. (jonge2020strategiesforcystic pages 7-9, jonge2020strategiesforcystic pages 26-28)
Modern models emphasize that CFTR is regulated in spatially restricted signaling “microdomains,” shaped by GPCR signaling, scaffolding proteins, phosphodiesterases, and Ca2+-linked effectors. Mouse-specific evidence described includes direct CFTR–AC6 interaction in mouse intestinal mucosa/colon epithelial cells and failure of forskolin-induced swelling in intestinal organoids derived from AC6-deficient mice, supporting AC6’s role in CFTR-dependent secretion. (varga2025beyondthemutations pages 16-20)
A 2024 cryo-EM study solved structures of the PKA catalytic subunit (PKA-C) bound to full-length CFTR, showing unphosphorylated CFTR engages PKA-C at two distinct docking locations, forming two “catalytic stations” that can access many spatially separated phosphorylation sites in the flexible R domain. The same work also provides structural and functional support for phosphorylation-independent potentiation: PKA-C binding alone can stimulate CFTR currents (“noncatalytic activation”). (fiedorczuk2024thestructuresofa pages 1-2)
Interpretation (expert analysis): These structures strengthen a model in which CFTR regulation is not simply a diffuse kinase-substrate collision process; instead, CFTR can act as a scaffold for PKA-C to enable efficient multi-site phosphorylation and potentially permit acute gating modulation through binding-based allostery. (fiedorczuk2024thestructuresofa pages 1-2)
A 2024 Nature Communications cryo-EM structure localized the CFTR gating inhibitor CFTRinh-172 inside the CFTR pore, contacting residues in TMs 1, 6, 8, 9, and 12. Binding is associated with re-orientations of extracellular segments (notably TMs 1, 8, 12), supporting an allosteric gating-inhibition mechanism. The study also reports that ivacaftor (VX-770) alters the apparent affinity of CFTRinh-172, indicating interacting allosteric sites around TM8. (gao2024allostericinhibitionof pages 1-2)
Interpretation (expert analysis): For functional annotation, this provides residue-level evidence linking CFTR’s pore architecture and gating transitions to pharmacologic control—useful for mapping mutation effects and designing inhibitors for CFTR hyperactivation states (e.g., secretory diarrhea). (gao2024allostericinhibitionof pages 1-2)
A 2023 Journal of General Physiology paper used cross-species comparison and thermodynamic mutant cycles to show how extracellular loop interactions stabilize CFTR bursting/open states and how disease mutations (e.g., R117H in human CFTR) disrupt open-state stabilization. (simon2023optimizationofcftr pages 1-2)
Mouse Cftr models (knockout and allele-specific mutants) are widely used for mechanistic studies and preclinical evaluation; they robustly model gastrointestinal disease and can be engineered by CRISPR to introduce precise alleles. Humanized or chimeric models are used to improve translational alignment (e.g., to test human-sequence–specific reagents), with the important caveat that species differences can strongly affect pharmacology. For example, a mouse-model-focused review notes ivacaftor does not act on mCFTR, motivating humanized/chimeric strategies for certain drug studies. (michicich2025developmentofcftr pages 28-33, michicich2025developmentofcftr pages 23-28, michicich2025developmentofcftr pages 33-38)
Forskolin-induced swelling (FIS) in intestinal organoids is a widely used functional CFTR readout. In a 2024 in vivo editing study, intestinal organoids from R553X homozygous mice showed ~50% base editing by sequencing and ~80% swelling after LNP-ABE treatment (versus no swelling untreated), demonstrating functional restoration via Cftr correction. (sun2024invivoediting pages 5-6)
A 2024 Science study demonstrated lung-targeting lipid nanoparticles (LNPs) enabling durable in vivo editing of lung stem cells in mice and applied this to a CFTR nonsense mutation model. Key quantitative outcomes include:
- In reporter mice: >70% lung stem cell editing and >80% lung epithelial cells remaining labeled/edited for 660 days. (sun2024invivoediting pages 1-1)
- In CFTR R553X correction experiments: in vivo NGS showed 50.0% correction in isolated lung NGFR+ stem cells, 12.2% in whole lung, and 28.7% in trachea. (sun2024invivoediting pages 6-6)
- Functional rescue (TECC): editing alone restored 53.4% of WT CFTR function (AUC 11.6 vs WT 21.7 mA/cm²·min), and combination with Trikafta improved function further (AUC 18.5 mA/cm²·min). (sun2024invivoediting pages 6-6)
Visual evidence: figure panels from this study directly display the editing frequencies and TECC/AUC functional rescue outcomes, including ~50% correction in lung NGFR+ stem cells. (sun2024invivoediting media 4be5b4c3, sun2024invivoediting media e348f72f, sun2024invivoediting media ecd86120)
A 2024 ACS Pharmacology & Translational Science review compiles recommended CFTR tool compounds with quantitative potencies used to model CFTR loss/hyperactivation and to probe gating/trafficking mechanisms. Examples include:
- PPQ-102 (reversible inhibitor) IC50 ≈ 90 nM.
- CFTRinh-172 analogs (Tetrazolo-172, Oxo-172) potency ≈ 1 μM.
- Corrector/potentiator examples: C18/VRT-534 EC50 ≈ 0.6 μM, ΔF508act-02 EC50 ≈ 600 nM. (han2024recommendedtoolcompounds pages 11-12)
| Topic | Key point | Evidence/data (include quantitative values where present) | Key source (first author, journal, year) | URL | Citation id |
|---|---|---|---|---|---|
| Identity verification | UniProt P26361 maps to CFTR_MOUSE from Mus musculus; this matches the target gene symbol Cftr/Abcc7 and the CFTR protein description. | UniProtKB-based cross-species analysis explicitly lists P26361 = CFTR_MOUSE, sequence length 1476 aa, species Mus musculus. | Hassan, preprint, 2026 | https://doi.org/10.20944/preprints202605.1213.v1 | (hassan2026mathematicalsequenceanalyses pages 3-4) |
| Domain architecture/topology | Mouse Cftr is an ABCC-family/ABC transporter-like protein that functions as an ion channel, with 2 MSD/TMDs, 12 TM helices total, 2 NBDs, and an R regulatory domain. | Canonical CFTR architecture: MSD1 (TM1-6), MSD2 (TM7-12), NBD1/NBD2, and R domain; NBDs contain Walker motifs/ABC signature; topology is consistent with a multi-pass plasma-membrane protein. | Baroni, Curr Issues Mol Biol, 2025 | https://doi.org/10.3390/cimb47020119 | (baroni2025unravelingthemechanism pages 2-5) |
| Substrates | Primary transported substrates are Cl− and HCO3−. | CFTR is described as an anion-selective channel conducting chloride and bicarbonate across apical epithelial membranes. | Infield, J Gen Physiol, 2021 | https://doi.org/10.1085/jgp.202012625 | (infield2021themolecularevolution pages 1-2) |
| Gating regulation (PKA/ATP) | CFTR opening requires R-domain phosphorylation and ATP-dependent NBD dimerization; closing is linked to ATP hydrolysis at site 2. | PKA/cAMP phosphorylates multiple R-domain serines; ATP binding promotes NBD1/NBD2 dimerization and pore opening; ATP hydrolysis at the composite active site drives channel closure. | de Jonge, FEBS Lett, 2020 | https://doi.org/10.1002/1873-3468.13971 | (jonge2020strategiesforcystic pages 26-28, jonge2020strategiesforcystic pages 1-5) |
| Apical localization | Cftr functions mainly at the apical plasma membrane of polarized epithelial cells. | Localized to apical membranes of airway, intestinal, pancreatic, sweat duct, and other secretory epithelia; drives trans-epithelial salt/water transport. | Anwar, Adv Respir Med, 2024 | https://doi.org/10.3390/arm92040026 | (anwar2024cysticfibrosisunderstanding pages 1-2) |
| Epithelial transport coupling | CFTR works in a network with NKCC1, Na+/K+-ATPase, basolateral K+ channels (e.g., KCNQ1, KCNN4), and SLC26 exchangers to support fluid and acid-base secretion. | Basolateral Na+/K+-ATPase and NKCC1 load Cl−; K+ recycling maintains driving force; HCO3− handling involves NBCe1/NBCn1 and SLC26A3/A6 exchangers. | de Jonge, FEBS Lett, 2020 | https://doi.org/10.1002/1873-3468.13971 | (jonge2020strategiesforcystic pages 7-9, jonge2020strategiesforcystic pages 26-28) |
| 2024 PKA-C–CFTR structural complex | Cryo-EM showed PKA-C bound to CFTR at two catalytic stations, explaining multisite phosphorylation and noncatalytic activation. | 2024 structures revealed PKA-C docking at 2 sites; open-pore CFTR structures stabilized by PKA-C support activation even without phosphotransfer. | Fiedorczuk, PNAS, 2024 | https://doi.org/10.1073/pnas.2409049121 | (fiedorczuk2024thestructuresofa pages 1-2) |
| 2024 CFTRinh-172 pore binding structure | Cryo-EM localized CFTRinh-172 inside the pore and supported an allosteric gating-inhibition mechanism. | Inhibitor contacts residues from TMs 1, 6, 8, 9, 12; mutating these residues lowers apparent affinity; extracellular segments of TM1, TM8, TM12 reorient upon binding. | Gao, Nat Commun, 2024 | https://doi.org/10.1038/s41467-024-50641-1 | (gao2024allostericinhibitionof pages 1-2) |
| 2024 in vivo base editing in mice | Lung-targeted LNP adenine base editing achieved substantial Cftr correction in mouse CF models and durable lung stem-cell editing. | Reporter mice: >70% lung stem-cell editing and >80% epithelial labeling persisting 660 days. CFTR-R553X models: >95% correction in engineered 16HBE cells; ~60% allelic correction in primary HBE; organoids 47.8-50% editing with >82%/80% swelling; in vivo 50.0% editing in isolated lung stem cells, 12.2% whole lung, 28.7% trachea; CFTR function restored to 53.4% of WT by editing alone (AUC 11.6 vs WT 21.7 mA/cm2·min) and improved to 18.5 mA/cm2·min with editing + Trikafta. | Sun, Science, 2024 | https://doi.org/10.1126/science.adk9428 | (sun2024invivoediting pages 1-1, sun2024invivoediting pages 6-6, sun2024invivoediting pages 5-6, sun2024invivoediting pages 6-7) |
| 2024 tool compound/modulator statistic | Recent tool-compound review reports quantitative activities for CFTR modulators/inhibitors useful in functional studies. | PPQ-102 inhibits CFTR with IC50 ~90 nM; Tetrazolo-172/Oxo-172 ~1 μM; UCCF-152 activates WT and G551D CFTR; VRT-534/C18 partially rescues ΔF508-CFTR with EC50 ~0.6 μM; DeltaF508act-02 EC50 ~600 nM. | Han, ACS Pharmacol Transl Sci, 2024 | https://doi.org/10.1021/acsptsci.3c00362 | (han2024recommendedtoolcompounds pages 11-12) |
Table: This table summarizes core functional-annotation facts for mouse Cftr (UniProt P26361) together with major 2023-2024 mechanistic and translational developments. It is useful as a compact evidence map linking function, localization, regulation, and recent applications to specific cited sources.
Key sources used here include:
- Sun et al., Science (14 Jun 2024). https://doi.org/10.1126/science.adk9428 (sun2024invivoediting pages 1-1)
- Fiedorczuk et al., PNAS (Published 4 Nov 2024). https://doi.org/10.1073/pnas.2409049121 (fiedorczuk2024thestructuresofa pages 1-2)
- Gao et al., Nature Communications (Accepted 9 Jul 2024; 2024 publication). https://doi.org/10.1038/s41467-024-50641-1 (gao2024allostericinhibitionof pages 1-2)
- Han et al., ACS Pharmacology & Translational Science (Mar 2024). https://doi.org/10.1021/acsptsci.3c00362 (han2024recommendedtoolcompounds pages 11-12)
- Anwar et al., Advances in Respiratory Medicine (Jul 2024). https://doi.org/10.3390/arm92040026 (anwar2024cysticfibrosisunderstanding pages 1-2)
- de Jonge et al., FEBS Letters (Nov 2020). https://doi.org/10.1002/1873-3468.13971 (jonge2020strategiesforcystic pages 1-5)
- Infield et al., Journal of General Physiology (Oct 2021). https://doi.org/10.1085/jgp.202012625 (infield2021themolecularevolution pages 1-2)
References
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(sun2024invivoediting pages 6-7): Yehui Sun, Sumanta Chatterjee, Xizhen Lian, Zachary Traylor, Sandhya R. Sattiraju, Yufen Xiao, Sean A. Dilliard, Yun-Chieh Sung, Minjeong Kim, Sang M. Lee, Stephen Moore, Xu Wang, Di Zhang, Shiying Wu, Pratima Basak, Jialu Wang, Jing Liu, Rachel J. Mann, David F. LePage, Weihong Jiang, Shadaan Abid, Mirko Hennig, Anna Martinez, Brandon A. Wustman, David J. Lockhart, Raksha Jain, Ronald A. Conlon, Mitchell L. Drumm, Craig A. Hodges, and Daniel J. Siegwart. In vivo editing of lung stem cells for durable gene correction in mice. Science, 384:1196-1202, Jun 2024. URL: https://doi.org/10.1126/science.adk9428, doi:10.1126/science.adk9428. This article has 171 citations and is from a highest quality peer-reviewed journal.