Evidence map›Paper›PMID 34413451›Full record

ArticleCommunications biology2021

14-3-3 proteins inactivate DAPK2 by promoting its dimerization and protecting key regulatory phosphosites.

Matej Horvath, Olivia Petrvalska, Petr Herman, Veronika Obsilova, Tomas Obsil

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-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

20 citing papers in PubMed, 29 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

5 authors at 2 institutions in 1 country.

Matej HorvathDepartment of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic.ORCID 0000-0001-9741-3693
Olivia PetrvalskaDepartment of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic.
Petr HermanInstitute of Physics, Faculty of Mathematics and Physics, Charles University, Prague, Czech Republic.ORCID 0000-0001-6918-2576
Veronika ObsilovaDepartment of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, Vestec, Czech Republic. veronika.obsilova@fgu.cas.cz.ORCID 0000-0003-4887-0323
Tomas ObsilDepartment of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic. obsil@natur.cuni.cz.ORCID 0000-0003-4602-1272
Czech Academy of Sciences · CZCharles University · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Death-associated protein kinase 2 (DAPK2) is a CaM-regulated Ser/Thr protein kinase, involved in apoptosis, autophagy, granulocyte differentiation and motility regulation, whose activity is controlled by autoinhibition, autophosphorylation, dimerization and interaction with scaffolding proteins 14-3-3. However, the structural basis of 14-3-3-mediated DAPK2 regulation remains unclear. Here, we structurally and biochemically characterize the full-length human DAPK2:14-3-3 complex by combining several biophysical techniques. The results from our X-ray crystallographic analysis revealed that Thr369 phosphorylation at the DAPK2 C terminus creates a high-affinity canonical mode III 14-3-3-binding motif, further enhanced by the diterpene glycoside Fusicoccin A. Moreover, concentration-dependent DAPK2 dimerization is disrupted by Ca

Indexed as

14-3-3 ProteinsDeath-Associated Protein KinasesDimerizationGene Expression RegulationHumansPhosphorylation14-3-3 ProteinsDAPK2 protein, humanDeath-Associated Protein KinasesYWHAG protein, human

Identifiers

PMID34413451
PMCPMC8376927
OpenAlexW3195464522

What OpenQuestion holds

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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.