Evidence map›Paper›PMID 24434581›Full record

ArticleJournal of cell science2014

PIPKIγ targets to the centrosome and restrains centriole duplication.

Qingwen Xu, Yuxia Zhang, Xunhao Xiong, Yan Huang, Jeffery L Salisbury, Jinghua Hu, Kun Ling

Abstract read
In one paragraph

Article in Journal of cell science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

16 citing papers in PubMed, 19 citations in OpenAlex.

  1. A Ciliary Phosphoinositide Pathway Regulates the Dosage of Polycystins in Primary Cilia.Journal of the American Society of Nephrology : JASN · 2026
    Article
  2. Local PI(4,5)PNature communications · 2026
    Article
  3. Review
  4. Phosphoinositides in New Spaces.Cold Spring Harbor perspectives in biology · 2023
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. PIPKIJournal of immunology research · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. 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 1 institution in 1 country.

Qingwen XuDepartment of Biochemistry and Molecular Biology, and Division of Hypertension and Nephrology, Mayo Clinic, 200 First Street SW, Rochester, MN 55902, USA.
Yuxia Zhang
Xunhao Xiong
Yan Huang
Jeffery L Salisbury
Jinghua Hu
Kun Ling
Mayo Clinic · US

Funding

Women's Cancer ProgramP30CA015083 · NCI · MAYO CLINIC ROCHESTER · PI Felicity Enders · 1985 to 2026
$151.3M
Pilot and FeasibilityP30DK090728 · NIDDK · MAYO CLINIC ROCHESTER · PI ROMERO, MICHAEL F. · 2010 to 2019
$11.8M
Molecular dissection of the ciliary gateR01DK099160 · NIDDK · MAYO CLINIC ROCHESTER · PI Jinghua Hu · 2014 to 2026
$4.0M
Exploration of the functions of the ciliopathy Arls in cilia.R01DK090038 · NIDDK · MAYO CLINIC ROCHESTER · PI HU, JINGHUA · 2011 to 2019
$3.1M
Phosphoinsitide signaling in Breast Epithelial Morphogenesis and MetastasisR01CA149039 · NCI · MAYO CLINIC ROCHESTER · PI LING, KUN · 2010 to 2014
$1.6M
NCI NIH HHS 1R01CA149039-01A1NCI NIH HHS P30 CA015083NCI NIH HHS R01 CA149039NIDDK NIH HHS DK90728NIDDK NIH HHS P30 DK090728NIDDK NIH HHS R01 DK090038NIDDK NIH HHS R01-DK090038NIDDK NIH HHS R01 DK099160
6 · The paper itself

Abstract

Centriole biogenesis depends on the polo-like kinase (PLK4) and a small group of structural proteins. The spatiotemporal regulation of these proteins at pre-existing centrioles is essential to ensure that centriole duplication occurs once per cell cycle. Here, we report that phosphatidylinositol 4-phosphate 5-kinase type-1 gamma (PIP5K1C, hereafter referred to as PIPKIγ) plays an important role in centriole fidelity. PIPKIγ localized in a ring-like pattern in the intermediate pericentriolar materials around the proximal end of the centriole in G1, S and G2 phases, but not in M phase. This localization was dependent upon an association with centrosomal protein of 152 KDa (CEP152). Without detaining cells in S or M phase, the depletion of PIPKIγ led to centriole amplification in a manner that was dependent upon PLK4 and spindle assembly abnormal protein 6 homolog (SAS6). The expression of exogenous PIPKIγ reduced centriole amplification that occurred as a result of endogenous PIPKIγ depletion, hydroxyurea treatment or PLK4 overexpression, suggesting that PIPKIγ is likely to function at the PLK4 level to restrain centriole duplication. Importantly, we found that PIPKIγ bound to the cryptic polo-box domain of PLK4 and that this binding reduced the kinase activity of PLK4. Together, our findings suggest that PIPKIγ is a novel negative regulator of centriole duplication, which acts by modulating the homeostasis of PLK4 activity.

Indexed as

UbiquitinationAnimalsCalcium-Binding ProteinsCell Cycle ProteinsCentriolesHEK293 CellsHeLa CellsHumansMiceNIH 3T3 CellsPhosphotransferases (Alcohol Group Acceptor)Protein Interaction Domains and MotifsProtein Serine-Threonine KinasesProtein TransportProteolysis1-phosphatidylinositol-4-phosphate 5-kinaseCalcium-Binding ProteinsCell Cycle ProteinsCEP152 protein, humanCETN2 protein, humanPhosphotransferases (Alcohol Group Acceptor)PLK4 protein, humanProtein Serine-Threonine KinasesCentriole duplicationCEP152CEP192phosphatidylinositol 4-phosphate 5-kinase type-1 gammaPLK4

Identifiers

PMID24434581
PMCPMC3953817
OpenAlexW2140163671

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.