Evidence map›Paper›PMID 14685694›Full record

ArticleCellular and molecular life sciences : CMLS2003

Targeting of the Akt/PKB kinase to the actin skeleton.

V Cenni, A Sirri, M Riccio, G Lattanzi, S Santi, A de Pol, N M Maraldi, S Marmiroli

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-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

36 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  7. MYO1F Regulates IgE and MRGPRX2-Dependent Mast Cell Exocytosis.Journal of immunology (Baltimore, Md. : 1950) · 2021
    Article
  8. Review
  9. Article
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  12. The role of heat shock proteins and co-chaperones in heart failure.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Ubl4A is required for insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. Review
  20. mTORC2 regulates mechanically induced cytoskeletal reorganization and lineage selection in marrow-derived mesenchymal stem cells.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2014
    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

8 authors at 2 institutions in 1 country.

V CenniLaboratory of Cell Biology and Electron Microscopy, Rizzoli Orthopedic Institute, via di Barbiano 1/10, 40136 Bologna, Italy.
A Sirri
M Riccio
G Lattanzi
S Santi
A de Pol
N M Maraldi
S Marmiroli
Istituto Ortopedico Rizzoli · ITUniversity of Modena and Reggio Emilia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serine/threonine kinase Akt/PKB intracellular distribution undergoes rapid changes in response to agonists such as Platelet-derived growth factor (PDGF) or Insulin-like growth factor (IGF). The concept has recently emerged that Akt subcellular movements are facilitated by interaction with nonsubstrate ligands. Here we show that Akt is bound to the actin skeleton in in situ cytoskeletal matrix preparations from PDGF-treated Saos2 cells, suggesting an interaction between the two proteins. Indeed, by immunoprecipitation and subcellular fractioning, we demonstrate that endogenous Akt and actin physically interact. Using recombinant proteins in in vitro binding and overlay assays, we further demonstrate that Akt interacts with actin directly. Expression of Akt mutants strongly indicates that the N-terminal PH domain of Akt mediates this interaction. More important, we show that the partition between actin bound and unbound Akt is not constant, but is modulated by growth factor stimulation. In fact, PDGF treatment of serum-starved cells triggers an increase in the amount of Akt associated with the actin skeleton, concomitant with an increase in Akt phosphorylation. Conversely, expression of an Akt mutant in which both Ser473 and Thr308 have been mutated to alanine completely abrogates PDGF-induced binding. The small GTPases Rac1 and Cdc42 seem to facilitate actin binding, possibly increasing Akt phosphorylation.

Indexed as

3-Phosphoinositide-Dependent Protein KinasesActinscdc42 GTP-Binding ProteinCytoskeletonHumansIntercellular Signaling Peptides and ProteinsPlatelet-Derived Growth FactorProtein BindingProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-akt3-Phosphoinositide-Dependent Protein KinasesActinsAKT1 protein, humancdc42 GTP-Binding ProteinIntercellular Signaling Peptides and ProteinsmyotrophinPDPK1 protein, humanPlatelet-Derived Growth FactorProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-akt

Identifiers

PMID14685694
PMCPMC11146087
OpenAlexW2044319476

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.