Evidence map›Paper›PMID 22399289›Full record

ArticleThe Journal of biological chemistry2012

Disabled-2 protein facilitates assembly polypeptide-2-independent recruitment of cystic fibrosis transmembrane conductance regulator to endocytic vesicles in polarized human airway epithelial cells.

Kristine M Cihil, Philipp Ellinger, Abigail Fellows, Donna Beer Stolz, Dean R Madden, Agnieszka Swiatecka-Urban

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. LMTK2 switches on canonical TGF-β1 signaling in human bronchial epithelial cells.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. The human nephrin YThe Journal of biological chemistry · 2019
    Article
  9. Review
  10. AP2 α modulates cystic fibrosis transmembrane conductance regulator function in the human intestine.Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society · 2017
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
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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

6 authors at 2 institutions in 1 country.

Kristine M CihilDepartment of Nephrology, Children's Hospital of Pittsburgh, Pittsburgh, Pennsylvania 15224, USA.
Philipp Ellinger
Abigail Fellows
Donna Beer Stolz
Dean R Madden
Agnieszka Swiatecka-Urban
Dartmouth College · USUniversity of Pittsburgh · US

Funding

Regulation of the Endocytic Trafficking of CFTRR01HL090767 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SWIATECKA-URBAN, AGNIESZKA · 2008 to 2012
$2.2M
Keeping CFTR in its Place: An Integrated Small-Molecule ApproachR01DK075309 · NIDDK · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2008 to 2011
$1.7M
NHLBI NIH HHS R01 HL090767NHLBI NIH HHS R01HL090767NHLBI NIH HHS R01HL090767-02S1NIDDK NIH HHS R01 DK075309NIDDK NIH HHS R01DK075309
6 · The paper itself

Abstract

Cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-activated Cl(-) channel expressed in the apical plasma membrane of fluid-transporting epithelia, where the plasma membrane abundance of CFTR is in part controlled by clathrin-mediated endocytosis. The protein networks that control CFTR endocytosis in epithelial cells have only been partially explored. The assembly polypeptide-2 complex (AP-2) is the prototypical endocytic adaptor critical for optimal clathrin coat formation. AP-2 is essential for recruitment of cargo proteins bearing the YXXΦ motif. Although AP-2 interacts directly with CFTR in vitro and facilitates CFTR endocytosis in some cell types, it remains unknown whether it is critical for CFTR uptake into clathrin-coated vesicles (CCVs). Disabled-2 (Dab2) is a clathrin-associated sorting protein (CLASP) that contributes to clathrin recruitment, vesicle formation, and cargo selection. In intestinal epithelial cells Dab2 was not found to play a direct role in CFTR endocytosis. By contrast, AP-2 and Dab2 were shown to facilitate CFTR endocytosis in human airway epithelial cells, although the specific mechanism remains unknown. Our data demonstrate that Dab2 mediates AP-2 independent recruitment of CFTR to CCVs in polarized human airway epithelial cells. As a result, it facilitates CFTR endocytosis and reduces CFTR abundance and stability in the plasma membrane. These effects are mediated by the DAB homology domain. Moreover, we show that in human airway epithelial cells AP-2 is not essential for CFTR recruitment to CCVs.

Indexed as

Adaptor Protein Complex 2Adaptor Proteins, Signal TransducingAmino Acid MotifsApoptosis Regulatory ProteinsCell LineCell MembraneCell PolarityClathrinCystic Fibrosis Transmembrane Conductance RegulatorEndocytosisEpithelial CellsHumansProtein StabilityProtein Structure, TertiaryRespiratory MucosaTransport VesiclesAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsCFTR protein, humanClathrinCystic Fibrosis Transmembrane Conductance RegulatorDAB2 protein, humanTumor Suppressor Proteins

Identifiers

PMID22399289
PMCPMC3340218
OpenAlexW1986638484

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.