Evidence map›Paper›PMID 42403151›Full record

ReviewFEBS letters2026

Regulation of CFTR stability at the plasma membrane-Mechanisms and therapeutic opportunities in cystic fibrosis.

Carlos M Farinha, João Oliveira

Abstract readReview
In one paragraph

Review in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Carlos M FarinhaBioISI-Biosystems and Integrative Sciences Institute, Faculty of Sciences, University of Lisboa, Lisbon, Portugal.ORCID https://orcid.org/0000-0002-5467-1710
João OliveiraBioISI-Biosystems and Integrative Sciences Institute, Faculty of Sciences, University of Lisboa, Lisbon, Portugal.

Funding

Cystic Fibrosis Foundation FARINH24G0Fondazione Fibrosi Cistica Ricerca FFC#2/2023
6 · The paper itself

Abstract

CFTR stability at the plasma membrane is controlled by a dynamic balance between trafficking, endocytosis, recycling, and degradation. Interactions with scaffold proteins such as NHERF1 and ezrin anchor CFTR to the actin cytoskeleton, reducing mobility and enhancing stability. Cytoskeletal dynamics, regulated by GTPases like RhoA, Rac1, and Rap1, further influence CFTR retention and function. Phosphorylation by kinases including PKA, LMTK2, and SYK modulates channel activity and membrane presence. Whereas rescue of F508del-CFTR with modulators can rescue its defective folding and premature degradation, reduced membrane stability persists. Overall, understanding the molecular mechanisms governing CFTR regulation provides critical insights for developing more effective treatments targeting its stability and function in cystic fibrosis.

Indexed as

Cell MembraneCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorAnimalsHumansProtein StabilityProtein TransportCFTR protein, humanCystic Fibrosis Transmembrane Conductance RegulatorCFTRcystic fibrosismembrane stabilityprotein traffickingtherapeutic approaches

Identifiers

PMID42403151
PMCPMC13404153

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.