Evidence map›Paper›PMID 20923971›Full record

ArticleMolecular & cellular proteomics : MCP2010

eEF1A phosphorylation in the nucleus of insulin-stimulated C2C12 myoblasts: Ser⁵³ is a novel substrate for protein kinase C βI.

Manuela Piazzi, Alberto Bavelloni, Irene Faenza, William Blalock, Andrea Urbani, Simona D'Aguanno, Roberta Fiume, Giulia Ramazzotti, Nadir Mario Maraldi, Lucio Cocco

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. KAT8-catalyzed lactylation promotes eEF1A2-mediated protein synthesis and colorectal carcinogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. Article
  5. Lipid-independent activation of a muscle-specific PKCα splicing variant.American journal of physiology. Heart and circulatory physiology · 2022
    Article
  6. Glycosylating Effectors ofBiomolecules · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Regulation of mRNA translation by signaling pathways.Cold Spring Harbor perspectives in biology · 2012
    Review
  13. Article
  14. Article
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

10 authors at 5 institutions in 1 country.

Manuela PiazziCellular Signaling Laboratory, Department of Human Anatomical Sciences, University of Bologna, Via Irnerio 48, 40126 Bologna, Italy.
Alberto Bavelloni
Irene Faenza
William Blalock
Andrea Urbani
Simona D'Aguanno
Roberta Fiume
Giulia Ramazzotti
Nadir Mario Maraldi
Lucio Cocco
Istituto di Genetica Molecolare · ITUniversity of Bologna · ITBologna Research Area · ITFondazione Santa Lucia · ITIstituto Ortopedico Rizzoli · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent data indicate that some PKC isoforms are translocated to the nucleus, in response to certain stimuli, where they play an important role in nuclear signaling events. To identify novel interacting proteins of conventional PKC (cPKC) at the nuclear level during myogenesis and to find new PKC isozyme-specific phosphosubstrates, we performed a proteomics analysis of immunoprecipitated nuclear samples from mouse myoblast C2C12 cells following insulin administration. Using a phospho(Ser)-PKC substrate antibody, specific interacting proteins were identified by LC-MS/MS spectrometry. A total of 16 proteins with the exact and complete motif recognized by the phospho-cPKC substrate antibody were identified; among these, particular interest was given to eukaryotic elongation factor 1α (eEF1A). Nuclear eEF1A was focalized in the nucleoli, and its expression was observed to increase following insulin treatment. Of the cPKC isoforms, only PKCβI was demonstrated to be expressed in the nucleus of C2C12 myocytes and to co-immunoprecipitate with eEF1A. In-depth analysis using site-directed mutagenesis revealed that PKCβI could phosphorylate Ser⁵³ of the eEF1A2 isoform and that the association between eEF1A2 and PKCβI was dependent on the phosphorylation status of eEF1A2.

Indexed as

AnimalsBase SequenceCell LineCell NucleusChromatography, LiquidDNA PrimersElectrophoresis, Polyacrylamide GelEukaryotic Initiation Factor-1MiceMusclesPhosphoproteinsPhosphorylationPolymerase Chain ReactionProtein Kinase CProtein Kinase C betaSerineDNA PrimersEukaryotic Initiation Factor-1PhosphoproteinsProtein Kinase CProtein Kinase C betaSerine

Identifiers

PMID20923971
PMCPMC3101858
OpenAlexW2047060352

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.