Evidence map›Paper›PMID 17079732›Full record

ArticleMolecular biology of the cell2007

Akt-PDK1 complex mediates epidermal growth factor-induced membrane protrusion through Ral activation.

Hisayoshi Yoshizaki, Naoki Mochizuki, Yukiko Gotoh, Michiyuki Matsuda

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. 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
1.6field-weighted citation impact, top 18% 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, 65 citations in OpenAlex.

  1. Review
  2. Review
  3. Lysosomal PIPProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Multiphoton intravital microscopy of rodents.Nature reviews. Methods primers · 2022
    Article
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  10. Review
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  12. Akt signaling dynamics in individual cells.Journal of cell science · 2015
    Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. 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

4 authors at 3 institutions in 1 country.

Hisayoshi YoshizakiDepartment of Structural Analysis, National Cardiovascular Center Research Institute, Osaka 565-8565, Japan.
Naoki Mochizuki
Yukiko Gotoh
Michiyuki Matsuda
Kyoto University · JPNational Cerebral and Cardiovascular Center · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We studied the spatiotemporal regulation of Akt (also called protein kinase B), phosphatidylinositol-3,4-bisphosphate [PtdIns(3,4)P2], and phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4,5)P3] by using probes based on the principle of fluorescence resonance energy transfer. On epidermal growth factor (EGF) stimulation, the amount of PtdIns(3,4,5)P3 was increased diffusely in the plasma membrane, whereas that of PtdIns(3,4)P2 was increased more in the nascent lamellipodia than in the plasma membrane of the central region. The distribution and time course of Akt activation were similar to that of increased PtdIns(3,4)P2 levels, which were most prominent in the nascent lamellipodia. Moreover, we found that upon EGF stimulation 3-phosphoinositide-dependent protein kinase-1 (PDK1) was also recruited to nascent lamellipodia in an Akt-dependent manner. Because PDK1 is known to activate Ral GTPase and because Ral is required for EGF-induced lamellipodial protrusion, we speculated that the PDK1-Akt complex may be indispensable for the induction of lamellipodia. In agreement with this idea, EGF-induced lamellipodia formation was promoted by the overexpression of Akt and inhibited by an Akt inhibitor or a Ral-binding domain of Sec5. These results identified the Akt-PDK1 complex as an upstream positive regulator of Ral GTPase in the induction of lamellipodial protrusion.

Indexed as

3-Phosphoinositide-Dependent Protein KinasesAnimalsCell MembraneChlorocebus aethiopsCOS CellsEpidermal Growth FactorFluorescence Resonance Energy TransferImmunoprecipitationMiceMultienzyme ComplexesNIH 3T3 CellsPhosphatidylinositol PhosphatesProtein BindingProtein Serine-Threonine KinasesProtein TransportProto-Oncogene Proteins c-akt3-Phosphoinositide-Dependent Protein KinasesEpidermal Growth FactorMultienzyme ComplexesPdpk1 protein, mousephosphatidylinositol 3,4-diphosphatePhosphatidylinositol PhosphatesProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktral GTP-Binding Proteinsral Guanine Nucleotide Exchange Factor

Identifiers

PMID17079732
PMCPMC1751317
OpenAlexW2110812466

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.