Evidence map›Paper›PMID 24603559›Full record

ArticlePloS one2014

Specificity of ε and non-ε isoforms of arabidopsis 14-3-3 proteins towards the H+-ATPase and other targets.

Roberta Pallucca, Sabina Visconti, Lorenzo Camoni, Giovanni Cesareni, Sonia Melino, Simona Panni, Paola Torreri, Patrizia Aducci

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In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

35 citing papers in PubMed, 57 citations in OpenAlex.

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  6. 14-3-3 Proteins and the Plasma Membrane HPlants (Basel, Switzerland) · 2023
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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

8 authors at 3 institutions in 1 country.

Roberta PalluccaDepartment of Biology, University of Rome "Tor Vergata", Rome, Italy.
Sabina ViscontiDepartment of Biology, University of Rome "Tor Vergata", Rome, Italy.
Lorenzo CamoniDepartment of Biology, University of Rome "Tor Vergata", Rome, Italy.
Giovanni CesareniDepartment of Biology, University of Rome "Tor Vergata", Rome, Italy; IRCSS, Research Institute "Fondazione Santa Lucia", Rome, Italy.
Sonia MelinoDepartment of Sciences and Chemical Technologies, University of Rome "Tor Vergata", Rome, Italy.
Simona PanniDepartment DiBEST, University of Calabria, Rende, Italy.
Paola TorreriDepartment of Cell Biology and Neuroscience, Istituto Superiore di Sanità, Rome, Italy.
Patrizia AducciDepartment of Biology, University of Rome "Tor Vergata", Rome, Italy.
University of Rome Tor Vergata · ITIstituto Superiore di Sanità · ITUniversity of Calabria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

14-3-3 proteins are a family of ubiquitous dimeric proteins that modulate many cellular functions in all eukaryotes by interacting with target proteins. 14-3-3s exist as a number of isoforms that in Arabidopsis identifies two major groups named ε and non-ε. Although isoform specificity has been demonstrated in many systems, the molecular basis for the selection of specific sequence contexts has not been fully clarified. In this study we have investigated isoform specificity by measuring the ability of different Arabidopsis 14-3-3 isoforms to activate the H+-ATPase. We observed that GF14 isoforms of the non-ε group were more effective than ε group isoforms in the interaction with the H+-ATPase and in the stimulation of its activity. Kinetic and thermodynamic parameters of the binding of GF14ε and GF14ω isoforms, representative of ε and non-ε groups respectively, with the H+-ATPase, have been determined by Surface Plasmon Resonance analysis demonstrating that the higher affinity of GF14ω is mainly due to slower dissociation. The role of the C-terminal region and of a Gly residue located in the loop 8 and conserved in all non-ε isoforms has also been studied by deletion and site-specific mutagenesis. The C-terminal domains, despite their high divergence, play an auto-inhibitory role in both isoforms and they, in addition to a specific residue located in the loop 8, contribute to isoform specificity. To investigate the generality of these findings, we have used the SPOT-synthesis technology to array a number of phosphopeptides matching known or predicted 14-3-3 binding sites present in a number of clients. The results of this approach confirmed isoform specificity in the recognition of several target peptides, suggesting that the isoform specificity may have an impact on the modulation of a variety of additional protein activities, as suggested by probing of a phosphopeptide array with members of the two 14-3-3 groups.

Indexed as

14-3-3 ProteinsAmino Acid SequenceArabidopsis ProteinsCalcium-Binding ProteinsKineticsMolecular Sequence DataProtein BindingProtein IsoformsProton-Translocating ATPasesSequence Homology, Amino AcidSurface Plasmon ResonanceThermodynamics14-3-3chi protein, Arabidopsis14-3-3 ProteinsAHA1 protein, ArabidopsisArabidopsis ProteinsCalcium-Binding ProteinsGF14 protein, ArabidopsisProtein IsoformsProton-Translocating ATPases

Identifiers

PMID24603559
PMCPMC3946203
OpenAlexW1967294399

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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.