Evidence map›Paper›PMID 23990466›Full record

ArticleThe Journal of biological chemistry2013

Mitotic regulation of SEPT9 protein by cyclin-dependent kinase 1 (Cdk1) and Pin1 protein is important for the completion of cytokinesis.

Mathew P Estey, Caterina Di Ciano-Oliveira, Carol D Froese, Karen Y Y Fung, Jonathan D Steels, David W Litchfield, William S Trimble

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 54 citations in OpenAlex.

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  13. Review
  14. Structure and function of Septin 9 and its role in human malignant tumors.World journal of gastrointestinal oncology · 2020
    Review
  15. Article
  16. TheFrontiers in microbiology · 2020
    Article
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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 1 country.

Mathew P EsteyFrom the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada,; the Cell Biology Program, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada, and.
Caterina Di Ciano-Oliveirathe Cell Biology Program, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada, and.
Carol D Froesethe Cell Biology Program, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada, and.
Karen Y Y FungFrom the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada,; the Cell Biology Program, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada, and.
Jonathan D SteelsFrom the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada,; the Cell Biology Program, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada, and.
David W Litchfieldthe Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1, Canada.
William S TrimbleFrom the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada,; the Cell Biology Program, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada, and. Electronic address: wtrimble@sickkids.ca.
Hospital for Sick Children · CAUniversity of Toronto · CAWestern University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Precise cell division is essential for multicellular development, and defects in this process have been linked to cancer. Septins are a family of proteins that are required for mammalian cell division, but their function and mode of regulation during this process are poorly understood. Here, we demonstrate that cyclin-dependent kinase 1 (Cdk1) phosphorylates septin 9 (SEPT9) upon mitotic entry, and this phosphorylation controls association with the proline isomerase, Pin1. Both SEPT9 and Pin1 are critical for mediating the final separation of daughter cells. Expression of mutant SEPT9 that is defective in Pin1 binding was unable to rescue cytokinesis defects caused by SEPT9 depletion but rather induced dominant-negative defects in cytokinesis. However, unlike SEPT9 depletion, Pin1 was not required for the accumulation of the exocyst complex at the midbody. These results suggest that SEPT9 plays multiple roles in abscission, one of which is regulated by the action of Cdk1 and Pin1.

Indexed as

CDC2 Protein KinaseCytokinesisGene Expression RegulationHeLa CellsHumansMutationNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphorylationProtein BindingSeptinsCDC2 Protein KinaseNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanSEPTIN9 protein, humanSeptinsCDK (Cyclin-dependent Kinase)CytokinesisCytoskeletonGTPasePhosphorylationPin1Proline IsomeraseSeptin

Identifiers

PMID23990466
PMCPMC3798476
OpenAlexW2051532990

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.