Evidence map›Paper›PMID 30545002›Full record

ArticleInternational journal of molecular sciences2018

The Stress-Inducible Protein DRR1 Exerts Distinct Effects on Actin Dynamics.

Anja Kretzschmar, Jan-Philip Schülke, Mercè Masana, Katharina Dürre, Marianne B Müller, Andreas R Bausch, Theo Rein

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

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  8. Molecular Psychiatry: Trends and Study Examples.International journal of molecular sciences · 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

7 authors at 3 institutions in 2 countries.

Anja KretzschmarMax Planck Institute of Psychiatry, Kraepelinstraße 2-10, 80805 München, Germany. anja.kc@gmail.com.
Jan-Philip SchülkeMax Planck Institute of Psychiatry, Kraepelinstraße 2-10, 80805 München, Germany. jan.schuelke@gmail.com.
Mercè MasanaMax Planck Institute of Psychiatry, Kraepelinstraße 2-10, 80805 München, Germany. mmasana@ub.edu.ORCID 0000-0003-1392-4774
Katharina DürreLehrstuhl für Biophysik E27, Technische Universität München, Garching, Germany. katharina.duerre@tum.de.
Marianne B MüllerMax Planck Institute of Psychiatry, Kraepelinstraße 2-10, 80805 München, Germany. marianne.mueller@unimedizin-mainz.de.
Andreas R BauschLehrstuhl für Biophysik E27, Technische Universität München, Garching, Germany. abausch@mytum.de.
Theo ReinMax Planck Institute of Psychiatry, Kraepelinstraße 2-10, 80805 München, Germany. theorein@psych.mpg.de.ORCID 0000-0003-2850-4289
Max Planck Institute of Psychiatry · DEJohannes Gutenberg University Mainz · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytoskeletal dynamics are pivotal to memory, learning, and stress physiology, and thus psychiatric diseases. Downregulated in renal cell carcinoma 1 (DRR1) protein was characterized as the link between stress, actin dynamics, neuronal function, and cognition. To elucidate the underlying molecular mechanisms, we undertook a domain analysis of DRR1 and probed the effects on actin binding, polymerization, and bundling, as well as on actin-dependent cellular processes.

methodsDRR1 domains were cloned and expressed as recombinant proteins to perform in vitro analysis of actin dynamics (binding, bundling, polymerization, and nucleation). Cellular actin-dependent processes were analyzed in transfected HeLa cells with fluorescence recovery after photobleaching (FRAP) and confocal microscopy.

resultsDRR1 features an actin binding site at each terminus, separated by a coiled coil domain. DRR1 enhances actin bundling, the cellular F-actin content, and serum response factor (SRF)-dependent transcription, while it diminishes actin filament elongation, cell spreading, and actin treadmilling. We also provide evidence for a nucleation effect of DRR1. Blocking of pointed end elongation by addition of profilin indicates DRR1 as a novel barbed end capping factor.

conclusionsDRR1 impacts actin dynamics in several ways with implications for cytoskeletal dynamics in stress physiology and pathophysiology.

Indexed as

ActinsCytoskeletonFluorescence Recovery After PhotobleachingGenes, Tumor SuppressorHeLa CellsHumansMicroscopy, ConfocalNuclear ProteinsActinsFAM107A protein, humanNuclear Proteinsactin dynamicscytoskeletonDRR1FAM107Astress physiologyTU3A

Identifiers

PMID30545002
PMCPMC6321462
OpenAlexW2905041022

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.