Evidence map›Paper›PMID 20679239›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear envelope breakdown during prophase.

Hongchang Li, X Shawn Liu, Xiaoming Yang, Bing Song, Yun Wang, Xiaoqi Liu

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

35 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022
    Review
  6. The LEM-ESCRT toolkit: Repair and maintenance of the nucleus.Frontiers in cell and developmental biology · 2022
    Review
  7. Article
  8. Dissecting the mechanisms of cell division.The Journal of biological chemistry · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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 3 institutions in 1 country.

Hongchang LiDepartment of Biochemistry and Center for Cancer Research, Purdue University, West Lafayette, IN 47907, USA.
X Shawn Liu
Xiaoming Yang
Bing Song
Yun Wang
Xiaoqi Liu
Center for Cancer Research · USHarvard University Press · USPurdue University West Lafayette · US

Funding

Functional studies of Plk1 and its interacting proteinsK01CA114401 · NCI · PURDUE UNIVERSITY · PI LIU, XIAOQI · 2005 to 2009
$747k
NCI NIH HHS K01 CA114401NCI NIH HHS K01CA114401
6 · The paper itself

Abstract

Nuclear envelope breakdown (NEBD) is an essential step during the G2/M transition in higher eukaryotic cells. Increasing evidence supports the notion that both microtubules and microtubule-associated motor proteins are critical regulators of NEBD. Although it has been described that p150(Glued), the major component of the dynein/dynactin complex, localizes in the nuclear envelope during prophase, the exact role of p150(Glued) and its regulation during NEBD are largely elusive. Polo-like kinase 1 (Plk1), the best characterized Ser/Thr kinase, is involved in mitotic entry in several systems; however, the targets of Plk1 during NEBD are unknown. Herein, we show that in mammalian cells both Plk1 and p150(Glued) regulate NEBD and that Plk1 interacts with and phosphoryates p150(Glued) during NEBD at prophase. Using various approaches, we showed that Plk1 phosphorylates p150(Glued) at Ser-179 and that the pS179 epitope is generated at the nuclear envelope of prophase cells. Significantly, Plk1-mediated phosphorylation of p150(Glued) at Ser-179 positively regulates its accumulation at the nuclear envelope during prophase. Finally, we found that cells expressing the Plk1-unphosphorylatable mutant (p150(Glued)-S179A) arrest at G2, as indicated by reduced NEBD, increased levels of cyclin B and phospho-H3, but a decreased level of Cdc2 kinase activity. Taking these data together, we conclude that Plk1 phosphorylation of p150(Glued) might be one major pathway of NEBD regulation.

Indexed as

ProphaseAmino Acid SequenceAmino Acid SubstitutionBlotting, WesternCell Cycle ProteinsCell LineCell Line, TumorDynactin ComplexFluorescent Antibody TechniqueGreen Fluorescent ProteinsHeLa CellsHumansImmunohistochemistryMicrotubule-Associated ProteinsMicrotubulesMutationCell Cycle ProteinsDCTN1 protein, humanDynactin ComplexGreen Fluorescent ProteinsMicrotubule-Associated ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene Proteins

Identifiers

PMID20679239
PMCPMC2930408
OpenAlexW2046550179

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.