Evidence map›Paper›PMID 22641346›Full record

ArticleThe Journal of cell biology2012

LATS1/WARTS phosphorylates MYPT1 to counteract PLK1 and regulate mammalian mitotic progression.

Tatsuyuki Chiyoda, Naoyuki Sugiyama, Takatsune Shimizu, Hideaki Naoe, Yusuke Kobayashi, Jo Ishizawa, Yoshimi Arima, Hiroshi Tsuda, Masaaki Ito, Kozo Kaibuchi and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Moonlighting at the Poles: Non-Canonical Functions of Centrosomes.Frontiers in cell and developmental biology · 2022
    Review
  5. Review
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  8. The Journal of biological chemistry · 2020
    Article
  9. Article
  10. Mass Spectrometry-Based Discovery ofMass spectrometry (Tokyo, Japan) · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Overexpression of Myosin Phosphatase Target Subunit 1 (MYPT1) Inhibits Tumor Progression and Metastasis of Gastric Cancer.Medical science monitor : international medical journal of experimental and clinical research · 2018
    Article
  17. Article
  18. Article
  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

14 authors at 4 institutions in 1 country.

Tatsuyuki ChiyodaDivision of Gene Regulation, Institute for Advanced Medical Research, Department of Obstetrics and Gynecology, School of Medicine, Keio University, Shinjuku-ku, Tokyo 160-8582, Japan.
Naoyuki Sugiyama
Takatsune Shimizu
Hideaki Naoe
Yusuke Kobayashi
Jo Ishizawa
Yoshimi Arima
Hiroshi Tsuda
Masaaki Ito
Kozo Kaibuchi
Daisuke Aoki
Yasushi Ishihama
Hideyuki Saya
Shinji Kuninaka
Keio University · JPJapan Science and Technology Agency · JPMie University · JPNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the mitotic exit network of budding yeast, Dbf2 kinase phosphorylates and regulates Cdc14 phosphatase. In contrast, no phosphatase substrates of LATS1/WARTS kinase, the mammalian equivalent of Dbf2, has been reported. To address this discrepancy, we performed phosphoproteomic screening using LATS1 kinase. Screening identified MYPT1 (myosin phosphatase-targeting subunit 1) as a new substrate for LATS1. LATS1 directly and preferentially phosphorylated serine 445 (S445) of MYPT1. An MYPT1 mutant (S445A) failed to dephosphorylate Thr 210 of PLK1 (pololike kinase 1), thereby activating PLK1. This suggests that LATS1 promotes MYPT1 to antagonize PLK1 activity. Consistent with this, LATS1-depleted HeLa cells or fibroblasts from LATS1 knockout mice showed increased PLK1 activity. We also found deoxyribonucleic acid (DNA) damage-induced LATS1 activation caused PLK1 suppression via the phosphorylation of MYPT1 S445. Furthermore, LATS1 knockdown cells showed reduced G2 checkpoint arrest after DNA damage. These results indicate that LATS1 phosphorylates a phosphatase as does the yeast Dbf2 and demonstrate a novel role of LATS1 in controlling PLK1 at the G2 DNA damage checkpoint.

Indexed as

MitosisAnimalsCell Cycle ProteinsCells, CulturedHEK293 CellsHeLa CellsHumansMiceMice, Inbred C57BLMice, KnockoutMyosin-Light-Chain PhosphatasePhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsCell Cycle ProteinsLATS1 protein, humanMyosin-Light-Chain PhosphatasePolo-Like Kinase 1PPP1R12A protein, humanProtein Serine-Threonine KinasesProto-Oncogene Proteins

Identifiers

PMID22641346
PMCPMC3404884
OpenAlexW1999349518

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.