Evidence map›Paper›PMID 22609948›Full record

ArticleThe EMBO journal2012

Identification of a novel Wnt5a-CK1ɛ-Dvl2-Plk1-mediated primary cilia disassembly pathway.

Kyung Ho Lee, Yoshikazu Johmura, Li-Rong Yu, Jung-Eun Park, Yuan Gao, Jeong K Bang, Ming Zhou, Timothy D Veenstra, Bo Yeon Kim, Kyung S Lee

Abstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

116 citing papers in PubMed, 158 citations in OpenAlex.

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  12. Positive regulation of Hedgehog signaling via phosphorylation of GLI2/GLI3 by DYRK2 kinase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. The interplay between Wnt signaling pathways and microtubule dynamics.In vitro cellular & developmental biology. Animal · 2024
    Review
  14. Midbody remnant regulates the formation of primary cilia and their roles in tumor growth.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024
    Review
  15. Review
  16. Article
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56 more citing papers are in PubMed but not listed here.

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

10 authors at 5 institutions in 2 countries.

Kyung Ho LeeLaboratory of Metabolism, Center for Cancer Research, National Cancer Institute, Bethesda, MD, USA.
Yoshikazu Johmura
Li-Rong Yu
Jung-Eun Park
Yuan Gao
Jeong K Bang
Ming Zhou
Timothy D Veenstra
Bo Yeon Kim
Kyung S Lee
National Cancer Institute · USFrederick National Laboratory for Cancer Research · USNational Center for Toxicological Research · USKorea Basic Science Institute · KRKorea Research Institute of Bioscience and Biotechnology · KR

Funding

Polo-like kinase 1 (Plk1)-dependent centrosome maturation and spindle bipolarityZIABC011324 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI LEE, KYUNG · 2010 to 2018
$3.2M
Characterization of the hCenexin-Plk1 interaction at the centrosomesZIABC010680 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI LEE, KYUNG · 2009 to 2012
$1.3M
6 · The paper itself

Abstract

Non-motile primary cilium is an antenna-like structure whose defect is associated with a wide range of pathologies, including developmental disorders and cancer. Although mechanisms regulating cilia assembly have been extensively studied, how cilia disassembly is regulated remains poorly understood. Here, we report unexpected roles of Dishevelled 2 (Dvl2) and interphase polo-like kinase 1 (Plk1) in primary cilia disassembly. We demonstrated that Dvl2 is phosphorylated at S143 and T224 in a manner that requires both non-canonical Wnt5a ligand and casein kinase 1 epsilon (CK1ɛ), and that this event is critical to interact with Plk1 in early stages of the cell cycle. The resulting Dvl2-Plk1 complex mediated Wnt5a-CK1ɛ-Dvl2-dependent primary cilia disassembly by stabilizing the HEF1 scaffold and activating its associated Aurora-A (AurA), a kinase crucially required for primary cilia disassembly. Thus, via the formation of the Dvl2-Plk1 complex, Plk1 plays an unanticipated role in primary cilia disassembly by linking Wnt5a-induced biochemical steps to HEF1/AurA-dependent cilia disassembly. This study may provide new insights into the mechanism underlying ciliary disassembly processes and various cilia-related disorders.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsAurora Kinase AAurora KinasesCasein Kinase 1 epsilonCell Cycle ProteinsCiliaDishevelled ProteinsHeLa CellsHumansL CellsMiceMultienzyme ComplexesPhosphoproteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesAdaptor Proteins, Signal TransducingAurka protein, mouseAurora Kinase AAurora KinasesCasein Kinase 1 epsilonCell Cycle ProteinsDishevelled ProteinsDVL2 protein, humanDvl2 protein, mouseMultienzyme ComplexesNEDD9 protein, humanNEDD9 protein, mousePhosphoproteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsWnt-5a ProteinWNT5A protein, humanWnt5a protein, mouseWnt Proteins

Identifiers

PMID22609948
PMCPMC3400010
OpenAlexW1799771027

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.