Evidence map›Paper›PMID 25986610›Full record

ArticleMolecular and cellular biology2015

Phosphorylation of SAF-A/hnRNP-U Serine 59 by Polo-Like Kinase 1 Is Required for Mitosis.

Pauline Douglas, Ruiqiong Ye, Nicholas Morrice, Sébastien Britton, Laura Trinkle-Mulcahy, Susan P Lees-Miller

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2015. 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 27% 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, 30 citations in OpenAlex.

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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

6 authors at 4 institutions in 3 countries.

Pauline DouglasDepartments of Biochemistry & Molecular Biology and Oncology, Robson DNA Science Centre, Southern Alberta Cancer Research Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.
Ruiqiong YeDepartments of Biochemistry & Molecular Biology and Oncology, Robson DNA Science Centre, Southern Alberta Cancer Research Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.
Nicholas MorriceBeatson Institute for Cancer Research, Glasgow, Scotland, United Kingdom.
Sébastien BrittonInstitut de Pharmacologie et de Biologie Structurale, Centre National de la Recherche Scientifique, Université de Toulouse-Université Paul Sabatier, Equipe Labellisée Ligue contre le Cancer, Toulouse, France.
Laura Trinkle-MulcahyDepartment of Cellular & Molecular Medicine and Ottawa Institute of Systems Biology, University of Ottawa, Ottawa, Ontario, Canada.
Susan P Lees-MillerDepartments of Biochemistry & Molecular Biology and Oncology, Robson DNA Science Centre, Southern Alberta Cancer Research Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada leesmill@ucalgary.ca.
University of Calgary · CACancer Research UK Scotland Institute · GBUniversité Fédérale de Toulouse Midi-Pyrénées · FRUniversity of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scaffold attachment factor A (SAF-A), also called heterogenous nuclear ribonuclear protein U (hnRNP-U), is phosphorylated on serine 59 by the DNA-dependent protein kinase (DNA-PK) in response to DNA damage. Since SAF-A, DNA-PK catalytic subunit (DNA-PKcs), and protein phosphatase 6 (PP6), which interacts with DNA-PKcs, have all been shown to have roles in mitosis, we asked whether DNA-PKcs phosphorylates SAF-A in mitosis. We show that SAF-A is phosphorylated on serine 59 in mitosis, that phosphorylation requires polo-like kinase 1 (PLK1) rather than DNA-PKcs, that SAF-A interacts with PLK1 in nocodazole-treated cells, and that serine 59 is dephosphorylated by protein phosphatase 2A (PP2A) in mitosis. Moreover, cells expressing SAF-A in which serine 59 is mutated to alanine have multiple characteristics of aberrant mitoses, including misaligned chromosomes, lagging chromosomes, polylobed nuclei, and delayed passage through mitosis. Our findings identify serine 59 of SAF-A as a new target of both PLK1 and PP2A in mitosis and reveal that both phosphorylation and dephosphorylation of SAF-A serine 59 by PLK1 and PP2A, respectively, are required for accurate and timely exit from mitosis.

Indexed as

CDC2 Protein KinaseCell Cycle ProteinsCell Line, TumorCyclin B1Cyclin-Dependent KinasesDNA DamageHeLa CellsHeterogeneous-Nuclear Ribonucleoprotein UHumansMitosisNocodazolePaclitaxelPhosphoprotein PhosphatasesPhosphorylationPolo-Like Kinase 1Protein Phosphatase 2CCNB1 protein, humanCDC2 Protein KinaseCDK1 protein, humanCell Cycle ProteinsCyclin B1Cyclin-Dependent KinasesHeterogeneous-Nuclear Ribonucleoprotein UNocodazolePaclitaxelPhosphoprotein PhosphatasesPolo-Like Kinase 1Protein Phosphatase 2protein phosphatase 6Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, Small InterferingSecurinTubulin Modulators

Identifiers

PMID25986610
PMCPMC4524121
OpenAlexW1912902862

What OpenQuestion holds

Textmetadata
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Registered trials

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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.