Evidence map›Paper›PMID 16335529›Full record

ArticleMolecular and cellular biochemistry2005

Cross talk between protein kinase CK2 and eukaryotic translation initiation factor eIF2beta subunit.

Franc Llorens, Stefania Sarno, Eduard Sarró, Anna Duarri, Nerea Roher, Flavio Meggio, Maria Plana, Lorenzo A Pinna, Emilio Itarte

Abstract read
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Article in Molecular and cellular biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. 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

9 authors.

Franc LlorensDepartament de Bioquímica i Biologia Molecular, Unitat de Bioquímica de Ciències, Universitat Autinòma de Barcelona, Edifici Cs, Campus de Bellaterra, 08193 Bellaterra, Spain.
Stefania Sarno
Eduard Sarró
Anna Duarri
Nerea Roher
Flavio Meggio
Maria Plana
Lorenzo A Pinna
Emilio Itarte

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The beta-subunit of eukaryotic translation initiation factor eIF2 is a substrate and a partner for protein kinase CK2. Surface plasmon resonance analysis shows that the truncated form corresponding to residues 138-333 of eIF2beta (eIF2beta-CT) interacts with CK2beta as efficiently as full length eIF2beta, whereas the form corresponding to residues 1-137, which contains the CK2 phosphorylation sites, (eIF2beta-NT) does not bind. The use of different mutants and truncated forms of CK2alpha allowed us to map the basic segment K74-K83 at the beginning of helix alphaC and residues R191R195K198 in the p + 1 loop as the main determinants for the binding to eIF2beta-CT of either the isolated CK2alpha subunit or the CK2 holoenzyme. The presence of eIF2beta-CT stimulated the activity of CK2alpha towards the RRRAADSDDDDD peptide substrate; effect that was not observed with the CK2a K74-77A whose ability to bind to eIF2beta-CT is severely impaired. Gel filtration analysis confirmed the ability of CK2alpha to form complexes with eIF2beta-CT, and the contribution of the basic cluster in CK2alpha (K74-K77) in this association.

Indexed as

Amino Acid MotifsAnimalsCasein Kinase IICatalysisCatalytic DomainEukaryotic Initiation Factor-2HoloenzymesHumansMutationOligopeptidesPhosphorylationProtein BindingProtein SubunitsSubstrate SpecificityCasein Kinase IIEukaryotic Initiation Factor-2HoloenzymesOligopeptidesProtein Subunits

Identifiers

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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.