Evidence map›Paper›PMID 26616734›Full record

ArticleNature communications2015

p38- and MK2-dependent signalling promotes stress-induced centriolar satellite remodelling via 14-3-3-dependent sequestration of CEP131/AZI1.

Maxim A X Tollenaere, Bine H Villumsen, Melanie Blasius, Julie C Nielsen, Sebastian A Wagner, Jiri Bartek, Petra Beli, Niels Mailand, Simon Bekker-Jensen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed, 51 citations in OpenAlex.

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  19. 14-3-3γ, a novel regulator of the large-conductance CaAmerican journal of physiology. Renal physiology · 2020
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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

9 authors at 5 institutions in 3 countries.

Maxim A X TollenaereUbiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen DK-2200, Denmark.
Bine H VillumsenUbiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen DK-2200, Denmark.
Melanie BlasiusDanish Cancer Society Research Center, Strandboulevarden 49, Copenhagen DK-2100, Denmark.
Julie C NielsenUbiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen DK-2200, Denmark.
Sebastian A WagnerDepartment of Medicine, Hematology/Oncology, Goethe University Medical School, Theodor-Stern-Kai 7, Frankfurt DE-60590, Germany.
Jiri BartekDanish Cancer Society Research Center, Strandboulevarden 49, Copenhagen DK-2100, Denmark.
Petra BeliInstitute of Molecular Biology, Ackermannweg 4, Mainz DE-55128, Germany.
Niels MailandUbiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen DK-2200, Denmark.ORCID http://orcid.org/0000-0002-6623-709X
Simon Bekker-JensenUbiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen DK-2200, Denmark.
University of Copenhagen · DKDanish Cancer Society · DKGoethe University Frankfurt · DEInstitute of Molecular Biology · DEScience for Life Laboratory · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Centriolar satellites (CS) are small granular structures that cluster in the vicinity of centrosomes. CS are highly susceptible to stress stimuli, triggering abrupt displacement of key CS factors. Here we discover a linear p38-MK2-14-3-3 signalling pathway that specifically targets CEP131 to trigger CS remodelling after cell stress. We identify CEP131 as a substrate of the p38 effector kinase MK2 and pinpoint S47 and S78 as critical MK2 phosphorylation sites in CEP131. Ultraviolet-induced phosphorylation of these residues generates direct binding sites for 14-3-3 proteins, which sequester CEP131 in the cytoplasm to block formation of new CS, thereby leading to rapid depletion of these structures. Mutating S47 and S78 in CEP131 is sufficient to abolish stress-induced CS reorganization, demonstrating that CEP131 is the key regulatory target of MK2 and 14-3-3 in these structures. Our findings reveal the molecular mechanism underlying dynamic CS remodelling to modulate centrosome functions on cell stress.

Indexed as

14-3-3 ProteinsCell Cycle ProteinsCentriolesCytoskeletal ProteinsHumansIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2Microtubule Proteinsp38 Mitogen-Activated Protein KinasesProtein BindingProtein Serine-Threonine KinasesSignal Transduction14-3-3 ProteinsCell Cycle ProteinsCEP131 protein, humanCytoskeletal ProteinsIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2Microtubule Proteinsp38 Mitogen-Activated Protein KinasesProtein Serine-Threonine KinasesYWHAE protein, humanYWHAZ protein, human

Identifiers

PMID26616734
PMCPMC4674683
OpenAlexW2183800400

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.