Evidence map›Paper›PMID 24058532›Full record

ArticlePloS one2013

Detection of phospho-sites generated by protein kinase CK2 in CFTR: mechanistic aspects of Thr1471 phosphorylation.

Andrea Venerando, Cinzia Franchin, Natasha Cant, Giorgio Cozza, Mario A Pagano, Kendra Tosoni, Ateeq Al-Zahrani, Giorgio Arrigoni, Robert C Ford, Anil Mehta and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

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  9. NM23 proteins: innocent bystanders or local energy boosters for CFTR?Laboratory investigation; a journal of technical methods and pathology · 2018
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  17. Predicting CK2 beta-dependent substrates using linear patterns.Biochemistry and biophysics reports · 2015
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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

11 authors at 4 institutions in 2 countries.

Andrea VenerandoDepartment of Biomedical Sciences, University of Padova, and CNR Institute of Neurosciences, Padova, Italy.
Cinzia Franchin
Natasha Cant
Giorgio Cozza
Mario A Pagano
Kendra Tosoni
Ateeq Al-Zahrani
Giorgio Arrigoni
Robert C Ford
Anil Mehta
Lorenzo A Pinna
University of Padua · ITUniversity of Manchester · GBNinewells Hospital · GBUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research CouncilWellcome TrustWellcome Trust 069150Wellcome Trust 088929
6 · The paper itself

Abstract

By mass spectrometry analysis of mouse Cystic Fibrosis Transmembrane-conductance Regulator (mCFTR) expressed in yeast we have detected 21 phosphopeptides accounting for 22 potential phospho-residues, 12 of which could be unambiguously assigned. Most are conserved in human CFTR (hCFTR) and the majority cluster in the Regulatory Domain, lying within consensus sequences for PKA, as identified in previous mammalian studies. This validates our yeast expression model. A number of phospho-residues were novel and human conserved, notably mouse Ser670, Ser723, Ser737, and Thr1467, that all lie in acidic sequences, compatible with their phosphorylation by protein kinase CK2. Thr1467 is localized in the C-terminal tail, embedded in a functionally important and very acidic sequence (EETEEE) which displays an optimal consensus for protein kinase CK2. Herein, we show that Thr1467, homologous to human Thr1471 is readily phosphorylated by CK2. Indeed a 42 amino acid peptide encompassing the C-terminal segment of human CFTR is readily phosphorylated at Thr1471 with favorable kinetics (Km 1.7 µM) by CK2 holoenzyme, but neither by its isolated catalytic subunit nor by other acidophilic Ser/Thr kinases (CK1, PLK2/3, GCK/FAM20C). Our finding that by treating CFTR expressing BHK cells with the very specific CK2 inhibitor CX4945, newly synthesized wild type CFTR (and even more its Phe508del mutant) accumulates more abundantly than in the absence of CK2 inhibitor, supports the conclusion that phosphorylation of CFTR by CK2 correlates with decreased stability of the protein.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCasein Kinase IICell LineCricetinaeCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorHumansKineticsMass SpectrometryMiceModels, MolecularMolecular Sequence DataNaphthyridinesPhenazinesCasein Kinase IICyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorNaphthyridinesPhenazinesPhosphopeptidesProtein Kinase InhibitorsSerinesilmitasertibThreonine

Identifiers

PMID24058532
PMCPMC3776838
OpenAlexW2019630456

What OpenQuestion holds

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Registered trials

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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.