Evidence map›Paper›PMID 30256714›Full record

ArticleMolecular biology of the cell2018

Asterless is a Polo-like kinase 4 substrate that both activates and inhibits kinase activity depending on its phosphorylation state.

Cody J Boese, Jonathan Nye, Daniel W Buster, Tiffany A McLamarrah, Amy E Byrnes, Kevin C Slep, Nasser M Rusan, Gregory C Rogers

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Generating CRISPR-edited clonal lines of culturedBiology methods & protocols · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. The E3 ligase Poe promotes Pericentrin degradation.Molecular biology of the cell · 2023
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Journal of cell science · 2020
    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 3 institutions in 1 country.

Cody J BoeseDepartment of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, AZ 85724.
Jonathan NyeDepartment of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, AZ 85724.
Daniel W BusterDepartment of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, AZ 85724.
Tiffany A McLamarrahDepartment of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, AZ 85724.
Amy E ByrnesDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Kevin C SlepDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Nasser M RusanNational Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Gregory C RogersDepartment of Cellular and Molecular Medicine, University of Arizona Cancer Center, University of Arizona, Tucson, AZ 85724.
University of Arizona · USUniversity of North Carolina at Chapel Hill · USNational Institutes of Health · US

Funding

VITAMIN AP30CA023074 · NCI · UNIVERSITY OF ARIZONA · PI Dan Theodorescu · 1985 to 2026
$110.2M
Integrative Cancer Scholars Training GrantT32CA009213 · NCI · UNIVERSITY OF ARIZONA · PI CAREW, JENNIFER S, CURIEL-LEWANDROWSKI, CLARA · 1985 to 2024
$8.6M
Regulating Centrosome Duplication and MaturationZIAHL006104 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI RUSAN, NASSER · 2011 to 2021
$8.6M
Characterizing the molecular mechanisms of centriole duplication, growth and maturationR35GM136265 · NIGMS · UNIVERSITY OF ARIZONA · PI Gregory Charles Rogers · 2020 to 2026
$3.9M
Identifying molecular mechanisms that suppress centriole amplification.R01GM110166 · NIGMS · UNIVERSITY OF ARIZONA · PI ROGERS, GREGORY CHARLES · 2015 to 2019
$1.4M
Inherent mechanisms that govern centrosome function and duplicationR01GM126035 · NIGMS · UNIVERSITY OF ARIZONA · PI ROGERS, GREGORY CHARLES · 2018 to 2020
$1.0M
NCI NIH HHS P30 CA023074NCI NIH HHS T32 CA009213NIGMS NIH HHS R01 GM110166NIGMS NIH HHS R01 GM126035NIGMS NIH HHS R35 GM136265
6 · The paper itself

Abstract

Centriole assembly initiates when Polo-like kinase 4 (Plk4) interacts with a centriole "targeting-factor." In Drosophila, Asterless/Asl (Cep152 in humans) fulfills the targeting role. Interestingly, Asl also regulates Plk4 levels. The N-terminus of Asl (Asl-A; amino acids 1-374) binds Plk4 and promotes Plk4 self-destruction, although it is unclear how this is achieved. Moreover, Plk4 phosphorylates the Cep152 N-terminus, but the functional consequence is unknown. Here, we show that Plk4 phosphorylates Asl and mapped 13 phospho-residues in Asl-A. Nonphosphorylatable alanine (13A) and phosphomimetic (13PM) mutants did not alter Asl function, presumably because of the dominant role of the Asl C-terminus in Plk4 stabilization and centriolar targeting. To address how Asl-A phosphorylation specifically affects Plk4 regulation, we generated Asl-A fragment phospho-mutants and expressed them in cultured Drosophila cells. Asl-A-13A stimulated kinase activity by relieving Plk4 autoinhibition. In contrast, Asl-A-13PM inhibited Plk4 activity by a novel mechanism involving autophosphorylation of Plk4's kinase domain. Thus, Asl-A's phosphorylation state determines which of Asl-A's two opposing effects are exerted on Plk4. Initially, nonphosphorylated Asl binds Plk4 and stimulates its kinase activity, but after Asl is phosphorylated, a negative-feedback mechanism suppresses Plk4 activity. This dual regulatory effect by Asl-A may limit Plk4 to bursts of activity that modulate centriole duplication.

Indexed as

Amino Acid SequenceAnimalsCell CycleCell Cycle ProteinsCell LineCentriolesDrosophilaDrosophila ProteinsPhosphorylationProtein BindingProtein Serine-Threonine KinasesAsl protein, DrosophilaCell Cycle ProteinsDrosophila ProteinsPLK4 protein, humanProtein Serine-Threonine KinasesSak protein, Drosophila

Identifiers

PMID30256714
PMCPMC6249866
OpenAlexW2892455446

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.