Evidence map›Paper›PMID 21525957›Full record

ArticleEMBO reports2011

Phosphorylation of Ser 402 impedes phosphatase activity of slingshot 1.

Sandra Barišić, Anja C Nagel, Mirita Franz-Wachtel, Boris Macek, Anette Preiss, Gisela Link, Dieter Maier, Angelika Hausser

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

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  14. Regulation of protein kinase D1 activity.Molecular pharmacology · 2012
    Review
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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

8 authors at 3 institutions in 1 country.

Sandra BarišićInstitute for Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany.
Anja C Nagel
Mirita Franz-Wachtel
Boris Macek
Anette Preiss
Gisela Link
Dieter Maier
Angelika Hausser
University of Hohenheim · DEUniversity of Stuttgart · DEUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

By using mass spectrometry, we have identified Ser 402 as a new phosphorylation site within the catalytic domain of human slingshot 1 (SSH1). Phosphorylation at this site inhibits substrate binding and, thus, phosphatase activity in vitro, resulting in enrichment of phosphorylated cofilin in monolayer cell culture. We further demonstrate that protein kinase D (PKD) is upstream from Ser 402 phosphorylation. Accordingly, expression of active PKD in Drosophila phenotypically mimics the loss of SSH activity by inducing accumulation of phosphorylated cofilin and filamentous actin. We thus identify a universal mechanism by which PKD controls SSH1 phosphatase activity.

Indexed as

Actin Depolymerizing FactorsActinsAmino Acid SequenceAmino Acid SubstitutionEnzyme ActivationHEK293 CellsHeLa CellsHumansMolecular Sequence DataPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Kinase CRecombinant Fusion ProteinsSequence AlignmentSerineActin Depolymerizing FactorsActinsPhosphoprotein PhosphatasesProtein Kinase Cprotein kinase DRecombinant Fusion ProteinsSerineSSH1 protein, human

Identifiers

PMID21525957
PMCPMC3128274
OpenAlexW2124282578

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.