Evidence map›Paper›PMID 30040488›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019

Cdk5-mediated phosphorylation regulates phosphatidylinositol 4-phosphate 5-kinase type I γ 90 activity and cell invasion.

Liqing Li, Tomasz Kołodziej, Naser Jafari, Jing Chen, Haining Zhu, Zenon Rajfur, Cai Huang

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Loss of CDCP1 triggers FAK activation in detached prostate cancer cells.American journal of clinical and experimental urology · 2021
    Article
  10. Targeting the cyclin-dependent kinase 5 in metastatic melanoma.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
  12. Article
  13. PIPKIJournal of immunology research · 2019
    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

7 authors at 3 institutions in 2 countries.

Liqing LiMarkey Cancer Center, University of Kentucky, Lexington, Kentucky, USA.
Tomasz KołodziejMarkey Cancer Center, University of Kentucky, Lexington, Kentucky, USA.
Naser JafariMarkey Cancer Center, University of Kentucky, Lexington, Kentucky, USA.
Jing ChenDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA; and.
Haining ZhuDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky, USA; and.
Zenon RajfurFaculty of Physics, Astronomy, and Applied Computer Science, Institute of Physics, Jagiellonian University, Krakow, Poland.
Cai HuangMarkey Cancer Center, University of Kentucky, Lexington, Kentucky, USA.
University of Kentucky · USMarkey Cancer Center · USInstitute of Physics · PL

Funding

Talin2-mediated traction force drives MMP secretion and cell invasionR01GM122994 · NIGMS · UNIVERSITY OF KENTUCKY · PI HUANG, CAI · 2017 to 2017
$300k
NIGMS NIH HHS R01 GM122994
6 · The paper itself

Abstract

Phosphatidylinositol 4-phosphate 5-kinase type I γ (PIPKIγ90) regulates cell migration, invasion, and metastasis. However, it is unknown how cellular signals regulate those processes. Here, we show that cyclin-dependent kinase 5 (Cdk5), a protein kinase that regulates cell migration and invasion, phosphorylates PIPKIγ90 at S453, and that Cdk5-mediated PIPKIγ90 phosphorylation is essential for cell invasion. Moreover, Cdk5-mediated phosphorylation down-regulates the activity of PIPKIγ90 and the secretion of fibronectin, an extracellular matrix protein that regulates cell migration and invasion. Furthermore, inhibition of PIPKIγ activity with the chemical inhibitor UNC3230 suppresses fibronectin secretion in a dose-dependent manner, whereas depletion of Cdk5 enhances fibronectin secretion. With total internal reflection fluorescence microscopy, we found that secreted fibronectin appears as round dots, which colocalize with Tks5 and CD9 but not with Zyxin. These data suggest that Cdk5-mediated PIPKIγ90 phosphorylation regulates cell invasion by controlling PIPKIγ90 activity and fibronectin secretion.-Li, L., Kołodziej, T., Jafari, N., Chen, J., Zhu, H., Rajfur, Z., Huang, C. Cdk5-mediated phosphorylation regulates phosphatidylinositol 4-phosphate 5-kinase type I γ 90 activity and cell invasion.

Indexed as

Gene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticBreast NeoplasmsCyclin-Dependent Kinase 5FemaleFibronectinsHumansNeoplasm InvasivenessPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Signal TransductionTumor Cells, Cultured1-phosphatidylinositol-4-phosphate 5-kinaseCDK5 protein, humanCyclin-Dependent Kinase 5FibronectinsFN1 protein, humanPhosphotransferases (Alcohol Group Acceptor)cell migrationextracellular matrix proteinfibronectinphosphatidylinositol kinasesecretion

Identifiers

PMID30040488
PMCPMC6355064
OpenAlexW2883497819

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.