Evidence map›Paper›PMID 31748572›Full record

ArticleScientific reports2019

PAK1, PAK1Δ15, and PAK2: similarities, differences and mutual interactions.

Dana Grebeňová, Aleš Holoubek, Pavla Röselová, Adam Obr, Barbora Brodská, Kateřina Kuželová

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Computational Identification of New Dual PAK4 and NAMPT Inhibitors.International journal of molecular sciences · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Regulation of Cancer Metastasis by PAK2.International journal of molecular sciences · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Group I PAKs in myelin formation and repair of the central nervous system: what, when, and how.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  15. Article
  16. Article
  17. 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

6 authors at 1 institution in 1 country.

Dana GrebeňováDepartment of Proteomics, Institute of Hematology and Blood Transfusion, U Nemocnice 1, 128 20, Prague, Czech Republic.
Aleš HoloubekDepartment of Proteomics, Institute of Hematology and Blood Transfusion, U Nemocnice 1, 128 20, Prague, Czech Republic.
Pavla RöselováDepartment of Proteomics, Institute of Hematology and Blood Transfusion, U Nemocnice 1, 128 20, Prague, Czech Republic.
Adam ObrDepartment of Proteomics, Institute of Hematology and Blood Transfusion, U Nemocnice 1, 128 20, Prague, Czech Republic.
Barbora BrodskáDepartment of Proteomics, Institute of Hematology and Blood Transfusion, U Nemocnice 1, 128 20, Prague, Czech Republic.
Kateřina KuželováDepartment of Proteomics, Institute of Hematology and Blood Transfusion, U Nemocnice 1, 128 20, Prague, Czech Republic. kuzelova@uhkt.cz.
Institute of Haematology and Blood Transfusion · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P21-activated kinases (PAK) are key effectors of the small GTPases Rac1 and Cdc42, as well as of Src family kinases. In particular, PAK1 has several well-documented roles, both kinase-dependent and kinase-independent, in cancer-related processes, such as cell proliferation, adhesion, and migration. However, PAK1 properties and functions have not been attributed to individual PAK1 isoforms: besides the full-length kinase (PAK1-full), a splicing variant lacking the exon 15 (PAK1Δ15) is annotated in protein databases. In addition, it is not clear if PAK1 and PAK2 are functionally overlapping. Using fluorescently tagged forms of human PAK1-full, PAK1Δ15, and PAK2, we analyzed their intracellular localization and mutual interactions. Effects of PAK inhibition (IPA-3, FRAX597) or depletion (siRNA) on cell-surface adhesion were monitored by real-time microimpedance measurement. Both PAK1Δ15 and PAK2, but not PAK1-full, were enriched in focal adhesions, indicating that the C-terminus might be important for PAK intracellular localization. Using coimmunoprecipitation, we documented direct interactions among the studied PAK group I members: PAK1 and PAK2 form homodimers, but all possible heterocomplexes were also detected. Interaction of PAK1Δ15 or PAK2 with PAK1-full was associated with extensive PAK1Δ15/PAK2 cleavage. The impedance measurements indicate, that PAK2 depletion slows down cell attachment to a surface, and that PAK1-full is involved in cell spreading. Altogether, our data suggest a complex interplay among different PAK group I members, which have non-redundant functions.

Indexed as

Cell AdhesionCell LineCell Line, TumorCell MovementCell ProliferationExonsHEK293 CellsHeLa CellsHumansp21-Activated KinasesSignal Transductionp21-Activated KinasesPAK1 protein, humanPAK2 protein, human

Identifiers

PMID31748572
PMCPMC6868145
OpenAlexW2990614914

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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.